|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
102-769 |
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: 1345.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 153945790 742 KKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
102-769 |
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: 1338.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 153945790 742 KKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14913 641 KKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
102-769 |
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: 1324.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDEsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES-GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKP-LGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKvvKGKAEAHF 580
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAdssAKKGAKKKGSSFQTVSALFRENLNK 660
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---GGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 661 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFiD 740
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 153945790 741 SKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01377 634 GKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-769 |
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: 1258.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 580 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADS-SAKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 153945790 739 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
102-769 |
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: 1253.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 580 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSS---AKKGAKKKGSSFQTVSALFRE 656
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAgggAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 657 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEG 736
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 153945790 737 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
102-769 |
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: 1245.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEaaSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 580 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAD-SSAKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 153945790 739 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
102-769 |
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: 1214.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKD-ESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEqQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 580
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSS--AKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 153945790 739 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
104-769 |
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: 1159.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14927 3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESG----KMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14927 83 GAGKTVNTKRVIQYFAIVAALGDGPGKKAQflatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14927 163 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14927 243 DILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14927 323 VEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFIL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 578
Cdd:cd14927 403 EQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEA---DSSAKKGAKKKGSSFQTVSALFR 655
Cdd:cd14927 483 HFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLHK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 656 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 735
Cdd:cd14927 563 ENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPD 642
|
650 660 670
....*....|....*....|....*....|....
gi 153945790 736 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14927 643 DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
102-769 |
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: 1159.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 153945790 742 KKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14917 641 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
102-769 |
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: 1142.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEK-KKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 580
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEA-DSSAKKGAKKKGSSFQTVSALFRENLN 659
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 660 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 739
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 153945790 740 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
102-769 |
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: 1035.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-----LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 153945790 742 KKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14929 635 RKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
90-769 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1033.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 90 IEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 170 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKdesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSIDD 328
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 329 QEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 409 VGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANF 566
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 567 QKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKK---- 642
Cdd:pfam00063 472 QKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrt 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 643 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 722
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 153945790 723 QRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:pfam00063 629 QRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
83-781 |
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: 996.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 83 NPPKYDKIEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISD 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 163 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRND 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS--------GSNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 243 NSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQG-EI 321
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 322 TVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLQSLNSADLLK 400
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 401 ALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLC 480
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 481 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYdQH 559
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 560 LGKSANFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEadssakkg 639
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNA-------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 640 akKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 719
Cdd:smart00242 539 --GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 720 DFKQRYKVLNASAIPEGQFiDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD 781
Cdd:smart00242 617 EFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
104-769 |
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: 992.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14934 3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDEsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14934 83 GAGKTENTKKVIQYFANIGGTGKQSSDG----KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 344 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 423
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 424 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 503
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 504 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AEAHFSL 582
Cdd:cd14934 399 YKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 583 IHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAdssakKGAKKKGSSFQTVSALFRENLNKLM 662
Cdd:cd14934 479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLNKLM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 663 TNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSK 742
Cdd:cd14934 554 TTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNK 632
|
650 660
....*....|....*....|....*..
gi 153945790 743 KASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14934 633 KASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
102-769 |
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: 978.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTgeKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGAS--KKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVK-GKAEAHF 580
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKG-SSFQTVSALFRENLN 659
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKgGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 660 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQfi 739
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 153945790 740 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14909 637 DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
102-769 |
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: 836.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAvtgEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS---GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDY----AFVSQGEITVPSIDDQEELMATD 336
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylndYLNSSGCDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 415 TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 493 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKv 571
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 572 vkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKsamktlaslfstyasaeadssakkgakkkgssfqtvS 651
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------------------------------------G 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 652 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd00124 517 SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 153945790 732 AiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd00124 597 A-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1118 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 818.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 32 KPFDAKTSVFVAEPKESYVKSTIqskeggKVTVKTEGGATLTVREDQV--FPMNPPKYDKIEDMAMMTHLHEPGVLYNLK 109
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKV------TEEGKKEDGESVSVKKKVLgnDRIKLPKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 110 ERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTV 189
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 190 NTKRVIQYFATIAvtgekkkDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETY 269
Cdd:COG5022 168 NAKRIMQYLASVT-------SSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 270 LLEKSRVTFQLKAERSYHIFYQITSNKkPDLIEMLLITTNPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDILGFTPEE 348
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 349 KVSIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVG 428
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 429 ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 508
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 509 IEWTFIDFgMDLAACIELIEK--PLGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSANFQKPKVVKGKaeahFSLIHY 585
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 586 AGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEadssakkgakkKGSSFQTVSALFRENLNKLMTNL 665
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------SKGRFPTLGSRFKESLNSLMSTL 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 666 RSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI---DSK 742
Cdd:COG5022 623 NSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 743 KASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQIITRTQAVCRGFLMRVEYQKMLQRREALFCIQYNVR 822
Cdd:COG5022 703 NAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFR 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 823 AFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKtkdeLAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEAdslA 902
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIK----LQKTIKREKKLRETEEVEFSLKAEVLIQKFGRS---L 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 903 DAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRK-----LEDECSELKKDID-----DLELTLAKVEKEKH 972
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKlvnleLESEIIELKKSLSsdlieNLEFKTELIARLKK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 973 ATEN-KVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQekklRMDL 1051
Cdd:COG5022 936 LLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGAL 1011
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1052 ERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKefEISNLISKIEDEQAveiQLQKKIKELQARI 1118
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSASKIISSESTELSILK--PLQKLKGLLLLENN---QLQARYKALKLRR 1073
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
104-769 |
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: 780.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14911 3 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESGK-------MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 256
Cdd:cd14911 83 GAGKTENTKKVIQFLAYVAASKPKGSGAVPHpavnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 257 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATD 336
Cdd:cd14911 163 ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14911 242 KSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 416 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 495 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLgksanfQKPKVVKG 574
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMKT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 575 --KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----STYASAEADSSAKKGAKKKGSSFQ 648
Cdd:cd14911 475 dfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaeIVGMAQQALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 649 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153945790 729 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14911 635 TPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
104-769 |
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: 774.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14920 3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14920 83 GAGKTENTKKVIQYLAHVASSHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 342
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 343 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14920 318 QADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKA 576
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKDKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 577 EahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF--------STYASAEADSSAKKGAKKKGSSFQ 648
Cdd:cd14920 476 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivgLDQVTGMTETAFGSAYKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 649 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153945790 729 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14920 634 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
104-769 |
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: 717.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14932 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESGKM--QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14932 83 GAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14932 163 VGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14932 242 MSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKA 576
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSSAKKGAKKKGSSFQT 649
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldKVAGMGESLHGAFKTRKGMFRT 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 650 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 729
Cdd:cd14932 558 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 637
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 153945790 730 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14932 638 PNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
104-769 |
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: 700.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14921 3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14921 83 GAGKTENTKKVIQYLAVVASSHKGKKDTS--ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 344 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 422
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 423 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEa 578
Cdd:cd14921 399 EEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDKTE- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 hFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSSAKKGAKKKGSSFQTV 650
Cdd:cd14921 477 -FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRTV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 651 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 730
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 153945790 731 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14921 636 NAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
102-769 |
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: 676.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATiaVTGekkkdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGG------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd01380 313 QQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGK-SANFQKPKVVKGKae 577
Cdd:cd01380 393 LEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 578 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKtlaslfstyasaeadssakkgakkkgssFQTVSALFREN 657
Cdd:cd01380 470 --FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR----------------------------KKTVGSQFRDS 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 658 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAipEGQ 737
Cdd:cd01380 520 LILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--EWL 597
|
650 660 670
....*....|....*....|....*....|..
gi 153945790 738 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01380 598 RDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
104-769 |
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: 674.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14919 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14919 83 GAGKTENTKKVIQYLAHVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 342
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 343 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14919 315 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 577
Cdd:cd14919 395 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKAD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 578 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSSAKKGAKKKGSSFQT 649
Cdd:cd14919 474 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTRKGMFRT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 650 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 729
Cdd:cd14919 552 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 153945790 730 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14919 632 PNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
104-769 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 671.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd15896 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESGKM--QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd15896 83 GAGKTENTKKVIQYLAHVASSHKTKKDQNSLAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd15896 163 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd15896 242 MGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd15896 322 QAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAE 577
Cdd:cd15896 402 QEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLKDE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 578 AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYAS------AEADSSAKKGAKKKGSSFQTVS 651
Cdd:cd15896 479 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldkVSGMSEMPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 652 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*...
gi 153945790 732 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd15896 639 AIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
104-769 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 658.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14930 3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14930 83 GAGKTENTKKVIQYLAHVASSPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIDILG 343
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 344 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 422
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 423 VYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14930 318 ADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKAE 577
Cdd:cd14930 397 QEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 578 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKG------AKKKGSSFQTVS 651
Cdd:cd14930 476 --FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppgGRPRRGMFRTVG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 652 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd14930 554 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 153945790 732 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14930 634 AIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
102-769 |
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: 630.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGekkkdesgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-----------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAID 340
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFqkpkvvKGKAEA 578
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660 670
....*....|....*....|....*....|.
gi 153945790 739 IDSkkASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01383 619 PLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
103-769 |
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: 630.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 183 SGAGKTVNTKRVIQYFATIavtgekkkdeSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI----------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDI 341
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPkvvKG 574
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP---KS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 575 KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKgakkkgssfQTVSALF 654
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS---------PTLSSQF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 655 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnASAIP 734
Cdd:cd01381 535 RKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGIP 613
|
650 660 670
....*....|....*....|....*....|....*
gi 153945790 735 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01381 614 PAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
107-769 |
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: 629.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 107 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 186
Cdd:cd01378 6 NLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 187 KTVNTKRVIQYFAtiAVTGekkkDESGKMQGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 266
Cdd:cd01378 86 KTEASKRIMQYIA--AVSG----GSESEVERV-KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 267 ETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTP 346
Cdd:cd01378 159 TNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 347 EEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY---VTKGQTVQQV 423
Cdd:cd01378 239 EEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 424 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhmFVL--E 500
Cdd:cd01378 318 AYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTLkaE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 501 QEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSANFQKPKVVKGKAEA 578
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFELRRG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyasaEADSSAKKGAKKkgssfqTVSALFRENL 658
Cdd:cd01378 474 EFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP-----EGVDLDSKKRPP------TAGTKFKNSA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd01378 543 NALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG 622
|
650 660 670
....*....|....*....|....*....|.
gi 153945790 739 IDsKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01378 623 TW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
103-769 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 612.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 183 SGAGKTVNTKRVIQYFAtiAVTGEkkkdesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN---------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNPYDYAFVSQ-GEITVPSIDDQEELMATDSAID 340
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14883 231 VLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14883 311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 500 EQEEYKKEGIEWTFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKvvKGKAEA 578
Cdd:cd14883 391 EQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQ-----TVSAL 653
Cdd:cd14883 467 EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTskgkpTVGDT 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 654 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAI 733
Cdd:cd14883 547 FKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRAR 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 153945790 734 PEGQFIDsKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14883 627 SADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
102-769 |
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: 585.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAvtgekKKDESGkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----GRAVTE--GRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAI 339
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAAYLQSLNSADLL--------KALCYPRVKVGN 411
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVTPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 412 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01384 308 GIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 492 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQKPK 570
Cdd:cd01384 388 FNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 571 vvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAdssakkgakKKGSSFQTV 650
Cdd:cd01384 466 ----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT---------SSSSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 651 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnA 730
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL-A 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 153945790 731 SAIPEGQFiDSKKASEKLLASIDIDhtQYKFGHTKVFFK 769
Cdd:cd01384 612 PEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
105-769 |
3.16e-172 |
|
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: 539.14 E-value: 3.16e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 105 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFAtiavtgekkkdES-GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01382 84 GAGKTESTKYILRYLT-----------ESwGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLittnpydyafvsqgeiTVPSIDDQEELMATDSAIDIL 342
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 343 GFTPEEKVSIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLQSLNSADLLKALCYpRVKVGNEY 413
Cdd:cd01382 217 GLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 414 VTKGQ------TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd01382 291 GAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLgKSANF 566
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 567 QKPKvvKGKAEAH--------FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADssakK 638
Cdd:cd01382 448 SIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKD----S 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 639 GAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 718
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 719 GDFKQRYKVLNASAIPEgqfIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01382 602 HDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
104-769 |
5.76e-170 |
|
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: 533.58 E-value: 5.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSIL 178
Cdd:cd14890 3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 179 ITGESGAGKTVNTKRVIQYFATI--------AVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14890 83 ISGESGAGKTEATKIIMQYLARItsgfaqgaSGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 251 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQE 330
Cdd:cd14890 163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 331 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLQSLNSADLLKALCYPRVKV 409
Cdd:cd14890 242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 410 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd14890 322 GGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPlGIFSILEEECMFPKA-TDTSFKNKLYDQHLGKS 563
Cdd:cd14890 402 RHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 564 ------------ANFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAmKTLASLfstyasae 631
Cdd:cd14890 480 gsggtrrgssqhPHFVHPKF---DADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-RSIREV-------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 632 adssakkgakkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 711
Cdd:cd14890 548 -----------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 712 FPSRILYGDFKQRYKVLNASAipegqfiDSKKASEKLLASI-DIDHTQYKFGHTKVFFK 769
Cdd:cd14890 611 FALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
102-769 |
8.80e-170 |
|
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: 533.50 E-value: 8.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAVTGEKKKDesgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF----- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 256 ----GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS-----------------------NKKPDLIEMLLITT 308
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFEP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 309 -NPYDYAFVSqGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVA 384
Cdd:cd14888 233 hLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 385 DKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVL 463
Cdd:cd14888 312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 464 DIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPLGIFSILEEECM 542
Cdd:cd14888 392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 543 FPKATDTSFKNKLYDQHlgksANFQKPKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLAS 622
Cdd:cd14888 471 VPGGKDQGLCNKLCQKH----KGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 623 LFSTYASAEADssakkgAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 702
Cdd:cd14888 546 LFSAYLRRGTD------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 703 EGIRICRKGFPSRILYGDFKQRYKVLnasAIPEGQfidskkasekllasidIDHTQYKFGHTKVFFK 769
Cdd:cd14888 620 QAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
102-769 |
1.41e-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: 520.87 E-value: 1.41e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTgekkkdesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS-----------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSnkKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMATDSAID 340
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEP----DGTEVADKAAYLQsLNSADLLKALCYPRVKVgneyvtK 416
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVATLLG-VDAATLEEALTSRLMEI------K 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 417 GQ-------TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14872 300 GCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQ 567
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAAKSTFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 568 KPKVvkGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYasaEADSSAKKGakkkgssf 647
Cdd:cd14872 458 YAEV--RTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPS---EGDQKTSKV-------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 648 qTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 727
Cdd:cd14872 525 -TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 153945790 728 LNaSAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14872 604 LV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
102-767 |
9.87e-164 |
|
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: 516.65 E-value: 9.87e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 174 --NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 252 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNP-YDYAFVSQGEITVPSIDDQE 330
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 331 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LQSLNSADLLKALCYPRVKV 409
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 410 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANF 566
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 567 QKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASlfstyasaeadssakkgakkkgss 646
Cdd:cd14901 477 SVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 647 fqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14901 531 --TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 153945790 727 VLNAS------AIPEGQFIDSKKASEKLLASIDIDHTQykFGHTKVF 767
Cdd:cd14901 609 CLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
102-769 |
1.51e-161 |
|
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: 510.47 E-value: 1.51e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAvtgekkkdeSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLiEMLLITTNPYDYAFvSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14903 151 LVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14903 229 LIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 419 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14903 309 KKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKgkaeA 578
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR----T 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSS-----FQTVSAL 653
Cdd:cd14903 464 QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggaltTTTVGTQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 654 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnasaI 733
Cdd:cd14903 544 FKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF----L 619
|
650 660 670
....*....|....*....|....*....|....*....
gi 153945790 734 PEGQFIDSKKAS--EKLLASIDIDH-TQYKFGHTKVFFK 769
Cdd:cd14903 620 PEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
105-769 |
4.26e-161 |
|
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: 510.77 E-value: 4.26e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 105 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 184
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 185 AGKTVNTKRVIQYFATIavtgekkkdeSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd01385 84 SGKTESTNFLLHHLTAL----------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDIL 342
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 343 GFTPEEKVSIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKlYDQHLGKSANFQKPKvvkgK 575
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----V 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 576 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKS--------------AMKTLASLFSTYASAEADSSAKKGAK 641
Cdd:cd01385 467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSssafvreligidpvAVFRWAVLRAFFRAMAAFREAGRRRA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 642 KKGSSFQ---------------------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNG 700
Cdd:cd01385 547 QRTAGHSltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 701 VLEGIRICRKGFPSRILYGDFKQRYKVLnasaIPEGQfIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01385 627 MLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
104-769 |
8.20e-161 |
|
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: 508.52 E-value: 8.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd01387 3 VLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIAVTGEKKKDEsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKLAS 263
Cdd:cd01387 83 GSGKTEATKLIMQYLAAVNQRRNNLVTE----------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQI------TSNKKPDLIEmllittnPYDYAFVSQG-EITVPSIDDQEELMATD 336
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELlaglpaQLRQKYGLQE-------AEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLQSLNSADLLKALCYPRVKVGN 411
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 412 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 492 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPK 570
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 571 VvkGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYAsAEADSSAKKGAKKKGSSFQ-- 648
Cdd:cd01387 461 M--PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR-AQTDKAPPRLGKGRFVTMKpr 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 649 --TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd01387 536 tpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 153945790 727 VLNASAIPEGQFIDSKKASEKLLASIDIDhTQYKFGHTKVFFK 769
Cdd:cd01387 616 CLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
849-1926 |
1.14e-160 |
|
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: 522.81 E-value: 1.14e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 849 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTER 928
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 929 AEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQ 1008
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1009 TLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEF 1088
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1089 EISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNK 1168
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1169 KREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNL 1248
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1249 EKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKA 1328
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1329 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEHVE 1408
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1409 AVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQ---KY--EETQAELEASQKESRSLSte 1483
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaRYaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1484 lfkVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILR 1563
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1564 IQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESL 1643
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1644 RNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQN 1723
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1724 TSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1803
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1804 EQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKR 1883
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 153945790 1884 QAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVK 1926
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
104-769 |
7.19e-160 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 504.89 E-value: 7.19e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd01379 3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFATIavtgekkkdesGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01379 83 GAGKTESANLLVQQLTVL-----------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKpdLIEMLLITTNPYDYAFVSQGEITVPSIDD--QEELMATD 336
Cdd:cd01379 152 GARISEYLLEKSRVVHQAIGERNFHIFYYIyaglAEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 413 YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd01379 310 TIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlgKSA 564
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 565 NFQKPKvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLAslfstyasaeadssakkgakkkg 644
Cdd:cd01379 463 YYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR----------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 645 ssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 724
Cdd:cd01379 516 ---QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKR 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 153945790 725 YKVL--NASAIPEGqfidSKKASEKLLASIDIDHtqYKFGHTKVFFK 769
Cdd:cd01379 593 YYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
104-769 |
3.11e-157 |
|
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: 498.55 E-value: 3.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd14873 3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 183 SGAGKTVNTKRVIQYFATIAVTGEKKKdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd14873 83 SGAGKTESTKLILKFLSVISQQSLELS--LKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQ-GEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITAMEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14873 240 MQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEEILT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 417 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14873 312 PLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvkgkA 576
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRV----A 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGssfQTVSALFRE 656
Cdd:cd14873 465 VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR---PTVSSQFKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 657 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL-NASAIPE 735
Cdd:cd14873 542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNLALPE 621
|
650 660 670
....*....|....*....|....*....|....
gi 153945790 736 gqfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14873 622 ----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
108-769 |
1.49e-155 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 494.28 E-value: 1.49e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 108 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKpevVAAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 178 LITGESGAGKTVNTKRVIQYFATI--AVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATAskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 335 TDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLQSLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 413 yvTKGQ------TVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14892 320 --ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PLGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 555 LYDQHLGKSANFQKPKVvkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMktlaslfstyasaeads 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 635 sakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 714
Cdd:cd14892 536 -------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPI 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 715 RILYGDFKQRYKVL-------NASAIPEGQFIDSKKASEKLLASIDIDHTQykFGHTKVFFK 769
Cdd:cd14892 597 RRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
104-769 |
2.67e-149 |
|
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: 476.10 E-value: 2.67e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 183 SGAGKTVNTKRVIQYFATIavtgekkkdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL----------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEEL-----MATDS 337
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 338 aIDIL---GFTPEEKVSIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRVKV 409
Cdd:cd14897 232 -TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 410 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCINFT 484
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 485 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDqHLGKS 563
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGES 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 564 ANFQKPKvvKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYasaeadssakkgakkk 643
Cdd:cd14897 464 PRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 644 gssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 723
Cdd:cd14897 524 ----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 724 RYKVL-----NASAIPEGQFIDSKKAsekllASIDidhtQYKFGHTKVFFK 769
Cdd:cd14897 594 RYKEIcdfsnKVRSDDLGKCQKILKT-----AGIK----GYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
104-769 |
2.42e-144 |
|
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: 463.73 E-value: 2.42e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 174
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 175 QSILITGESGAGKTVNTKRVIQYFATIA---------VTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNP--YDYAFVSQGE-I 321
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 322 TVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 400 KALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PLGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 549 TSFKNKLYDQHlgksANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA 628
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 629 SAEADSSAKKGAKKKGSSFqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIC 708
Cdd:cd14907 558 GSQQQNQSKQKKSQKKDKF--LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945790 709 RKGFPSRILYGDFKQRYKVLNasaipegqfidskkasekllasididhTQYKFGHTKVFFK 769
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
104-728 |
6.46e-144 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 460.93 E-value: 6.46e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 168
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 169 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 248 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYqitsnkkpdliEMLLittnpydyafvSQGEITVPSiD 327
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFY-----------EMAI-----------GASEAARKR-D 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 328 DQEELMAtdsAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLQSLNSADLLK 400
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 401 ALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFDFNS 475
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 476 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNK 554
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 555 LYdQHLGKSANFQKPKVVKGKaeAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMktlaslfstyasaeads 634
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ----------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 635 sakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 714
Cdd:cd14900 516 -------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650
....*....|....
gi 153945790 715 RILYGDFKQRYKVL 728
Cdd:cd14900 577 RLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-769 |
3.77e-138 |
|
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: 446.28 E-value: 3.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 180 TGESGAGKTVNTKRVIQYFAtiavtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML-LITTNPYDYAFVSQGEITVPSI--DDQEELMatd 336
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYgLLDPGKYRYLNNGAGCKREVQYwkKKYDEVC--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14889 228 NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 416 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd14889 308 RHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFqkp 569
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYY--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 570 KVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKK------ 643
Cdd:cd14889 461 GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAgsdnfn 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 644 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 723
Cdd:cd14889 540 STRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 153945790 724 RYKVLnasaIPEGQFIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 769
Cdd:cd14889 620 RYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
102-769 |
1.17e-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: 444.77 E-value: 1.17e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAvtgekkkdesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA----------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSANFQKPKVVKgka 576
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 577 eAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyaSAEADSSAKKGAK-KKGSSFQTVSALFR 655
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG---SSEAPSETKEGKSgKGTKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 656 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 735
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|....*
gi 153945790 736 GqfiDSKKASEKLLASIDIDHT-QYKFGHTKVFFK 769
Cdd:cd14904 622 K---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-769 |
6.81e-133 |
|
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: 431.00 E-value: 6.81e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyKPEVvAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 176
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 177 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQG--------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSkkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 249 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 327 DDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLQSLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 403 CYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 561 GKSANFQKPKvVKGKAEAhFSLIHYAGTVDYNITGWLDKNkdplNDTVVglyqksamKTLASLFSTyasaeadssakkga 640
Cdd:cd14891 475 KRHPCFPRPH-PKDMREM-FIVKHYAGTVSYTIGSFIDKN----NDIIP--------EDFEDLLAS-------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 641 kkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGD 720
Cdd:cd14891 527 ----------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 721 FKQRYKVLNASAI------PEGQFIdskkasEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14891 597 LVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
26-828 |
9.66e-130 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 428.29 E-value: 9.66e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 26 RIEAQNKPFDAKTSVFV-------------AEPKESYVKSTIQ-SKEGGKVTVK---TEGGATLTVREDQVF----PMNP 84
Cdd:PTZ00014 16 RRNSNVEAFDKSGNVLKgfyvwtdkapavkEDPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 85 PKYDkieDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR-GKKRQEAPPHIFSISDN 163
Cdd:PTZ00014 96 MTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 164 AYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiavtgekkkDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDN 243
Cdd:PTZ00014 173 ALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS---------SKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 244 SSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITV 323
Cdd:PTZ00014 244 SSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 324 PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-----PDGTEVADKAAYLQSLNSADL 398
Cdd:PTZ00014 323 PGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 399 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:PTZ00014 403 KKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKPLGIFSILEEECMFPKATDTSFK 552
Cdd:PTZ00014 483 LFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 553 NKLYDQhLGKSANFQKPKVVKGKaeaHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaEA 632
Cdd:PTZ00014 557 SSCNTN-LKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF------EG 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 633 DSSAKKGAKKKgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 712
Cdd:PTZ00014 627 VEVEKGKLAKG----QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGF 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 713 PSRILYGDFKQRYKVLNAsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQ---IIT 789
Cdd:PTZ00014 703 SYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVS 781
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 153945790 790 RTQAVcrgfLMRVEYQKMLQRR-EALFCIQYNVRAFMNVK 828
Cdd:PTZ00014 782 VLEAL----ILKIKKKRKVRKNiKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
102-769 |
7.27e-129 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 420.85 E-value: 7.27e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 172 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKM-QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 251 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---TSNKKPDLIEMLLITTN----PYDYAFVSQGEI-T 322
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLlrgGDEEEHEKYEFHDGITGglqlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 323 VPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 400 KALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLE 477
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 478 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFP-KATDTSFKNKL 555
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 556 YDQHL-------GKSANFQKPKVVKGKaeAHFSLIHYAGTVDYNI-TGWLDKNKDPLNdtvvglyqksamKTLASLFSTy 627
Cdd:cd14908 480 YETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIP------------LTADSLFES- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 628 asaeadssakkgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 707
Cdd:cd14908 545 -----------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 708 CRKGFPSRILYGDFKQRYKVLnASAIPE----------------GQFIDSKKA----SEKLLASIDIDHTQYKFGHTKVF 767
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldpqklcVKKMCKDLVkgvlSPAMVSMKNIPEDTMQLGKSKVF 680
|
..
gi 153945790 768 FK 769
Cdd:cd14908 681 MR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
102-726 |
5.07e-128 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 419.68 E-value: 5.07e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP---------VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFML-TD 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 172 RENQSILITGESGAGKTVNTKRVIQYFATIAVT---GEKKKDESGKMQgtleDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDqssTEQEGSDAVEIG----KRILQTNPILESFGNAQTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 249 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEmLLITTNPYDYAFVSQGEIT-----V 323
Cdd:cd14902 157 KFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSfarkrA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 324 PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLQSLNSA 396
Cdd:cd14902 236 VADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 397 DLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAG 467
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 468 FEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKA 546
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 547 TDTSFKNKLYDQHLGksanfqkpkvvkgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS- 625
Cdd:cd14902 471 SNQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAd 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 626 -TYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 704
Cdd:cd14902 536 eNRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEA 615
|
650 660
....*....|....*....|..
gi 153945790 705 IRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14902 616 VRIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
102-769 |
4.79e-122 |
|
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: 402.41 E-value: 4.79e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKpevVAAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 171
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 172 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSS-SKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 252 RIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPD-LIEMLLITTNPYDYAFVSQGEITV-- 323
Cdd:cd14895 157 RMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQrn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 324 PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------------D 385
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 386 KAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY------- 458
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 459 ----FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGI 533
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 534 FSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQ 613
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 614 KSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVS----ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEH 689
Cdd:cd14895 553 KTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSvgigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 690 ELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASaipegQFIDSKKASEkLLASIDIDHTQykFGHTKVFFK 769
Cdd:cd14895 633 AKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
102-769 |
6.41e-122 |
|
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: 400.13 E-value: 6.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAvtgekkkdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAK---------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLESLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14876 231 SMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 416 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 496 MFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQKP 569
Cdd:cd14876 391 VFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFKPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 570 KVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaeadsSAKKGAKKKGSSFQT 649
Cdd:cd14876 464 KV---DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF----------EGVVVEKGKIAKGSL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 650 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 729
Cdd:cd14876 531 IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 153945790 730 AsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14876 611 L-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
102-769 |
9.89e-121 |
|
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: 396.46 E-value: 9.89e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIavtgEKKKDESGKMQgtLEDQIisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKL 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQ--PEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEI-TVPSIDDQEELMATDSAID 340
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLQSlnSADLLKALCYPRVKVGN-EYVTK 416
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQV--PPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 417 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 495 HMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvk 573
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 574 gkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKgakkkgssfqTVSAL 653
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------TLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 654 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAI 733
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*.
gi 153945790 734 PEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14896 611 EA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
104-728 |
1.59e-113 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 376.50 E-value: 1.59e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 179
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 180 TGESGAGKTVNTKRVIQYFATIAVTgeKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS--PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVpsidDQEELMATDSAI 339
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGA-AFSWLPNPERNL----EEDCFEVTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEyvtk 416
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 417 gqtvQQVYNAV----------GALAKAVYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14880 312 ----QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSA 564
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 565 NFQKPKVVKgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyasAEADSSAKKGAKKKG 644
Cdd:cd14880 467 CLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPA---NPEEKTQEEPSGQSR 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 645 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 724
Cdd:cd14880 541 APVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVER 620
|
....
gi 153945790 725 YKVL 728
Cdd:cd14880 621 YKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
104-731 |
2.65e-108 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 363.53 E-value: 2.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTGK 260
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 LASADIETYLLEKSRVTFQL-KAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQ---------- 329
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 330 -----EELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLQSLNSADLLKA 401
Cdd:cd14906 243 ktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 402 LCYPRVKVGNE--YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIAGF 468
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKAT 547
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 548 DTSFKNKLYDQHLGKSANFQKPkvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY 627
Cdd:cd14906 482 EQSLLEKYNKQYHNTNQYYQRT-----LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 628 ASAEADSSAKKGAKKkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 707
Cdd:cd14906 557 ITSTTNTTKKQTQSN------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKV 630
|
650 660
....*....|....*....|....
gi 153945790 708 CRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd14906 631 RKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
108-769 |
1.46e-105 |
|
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: 353.42 E-value: 1.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 108 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYFATIAVTGEKKkdesgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD----------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEI-TVPSIDDQEELMATDSAID 340
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 341 ILgFTPEEKVSIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 418 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-LGIFSILEEECMFPKATDTSFKNKLyDQHLgKSANFqkpkvVKGK- 575
Cdd:cd14886 395 KSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPGKg 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 576 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAkkgakkkgssfQTVSALFR 655
Cdd:cd14886 467 SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG-----------KFLGSTFQ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 656 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL---NASA 732
Cdd:cd14886 536 LSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSS 615
|
650 660 670
....*....|....*....|....*....|....*..
gi 153945790 733 IPEGQfiDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14886 616 QNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
104-726 |
5.48e-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: 5.48e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAY----------RGKKRQEAPPHIFSISDNAYQFMLTDR 172
Cdd:cd14899 3 ILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 173 ENQSILITGESGAGKTVNTKRVIQYFA-------TIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14899 83 RSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 246 RFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNK----KPDLIEMLLITTNPYDYAFVSQGE 320
Cdd:cd14899 163 RFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 321 ITV--PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------DK 386
Cdd:cd14899 243 CSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfTK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 387 AAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL---------------D 451
Cdd:cd14899 323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdvD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 452 TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KP 530
Cdd:cd14899 403 DEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhRP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 531 LGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVG 610
Cdd:cd14899 482 IGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQ 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 611 LYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSAL--------FRENLNKLMTNLRSTHPHFVRCIIPNETK 682
Cdd:cd14899 562 LLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDSH 641
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 153945790 683 TPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14899 642 VGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
104-769 |
1.15e-104 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 351.03 E-value: 1.15e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 180
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFatiavtGEKKKDESGK-MQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14875 83 GESGSGKTENAKMLIAYL------GQLSYMHSSNtSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 256 -GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITV------PSIDD 328
Cdd:cd14875 157 dPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 329 QEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQsLNSADLLKalCYpRVK 408
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LVK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 409 VGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINFT 484
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 485 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKS 563
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 564 ANFQKPkvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASaEADSSakkgakkk 643
Cdd:cd14875 470 PYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKG-LARRK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 644 gssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF-K 722
Cdd:cd14875 538 ----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 723 QRYKVLNASAIPEGQFIDSKKASEKLLAS----IDIDHTQYKFGHTKVFFK 769
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
103-769 |
4.24e-102 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 344.68 E-value: 4.24e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 183 SGAGKTVNTKRVIQYFATIA------VTGEKkkdesgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 256
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAgsvggvLSVEK---------------LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 257 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvsqgeITVPSIDDQE------ 330
Cdd:cd01386 147 QAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF-----GIVPLQKPEDkqkaaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 331 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLQSLNSADLLKALCYPRV 407
Cdd:cd01386 222 AFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 408 KVGNEYVT---------------KGQTVQQvynAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD 472
Cdd:cd01386 299 SGGPQQSTtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 473 FN------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL--------------- 531
Cdd:cd01386 376 HSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedrr 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 532 GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKgKAEA--HFSLIHYAGT--VDYNITGWLDKNK-DPLND 606
Cdd:cd01386 456 GLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 607 TVVGLYQKSAMKTLA----SLFStyasaeadssakkgakkkGSSFQtvsalfrenLNKLMTNLRSTHPHFVRCIIPN--- 679
Cdd:cd01386 534 NATQLLQESQKETAAvkrkSPCL------------------QIKFQ---------VDALIDTLRRTGLHFVHCLLPQhna 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 680 ---ETKTPGAMEHELVLH------QLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL----NASAIPEGQFIDSKKASE 746
Cdd:cd01386 587 gkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVE 666
|
730 740
....*....|....*....|...
gi 153945790 747 KLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01386 667 ELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
104-732 |
1.93e-90 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 306.82 E-value: 1.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvykpEVVAAYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSIL 178
Cdd:cd14898 3 TLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 179 ITGESGAGKTVNTKRVIQYFAtiavtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgtT 258
Cdd:cd14898 74 ISGESGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpdliemLLITTNPYDYAFVSQGEITVpsIDDQEELMATDSA 338
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 339 IDILGFTPEEkvSIYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14898 213 MKSLGIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 419 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKAT--DTSFKNKLYDQHLgksanfqkpkvVKGKA 576
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGF-----------INTKA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGlyqksamktlASLFSTYASAEadssakkgakkkgssfqTVSALFRE 656
Cdd:cd14898 434 RDKIKVSHYAGDVEYDLRDFLDKNREKGQLLIFK----------NLLINDEGSKE-----------------DLVKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 657 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASA 732
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
104-769 |
2.60e-88 |
|
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: 303.28 E-value: 2.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14878 3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATiavtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14878 83 GERGSGKTEASKQIMKHLTC----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 261 -LASADIETYLLEKSRVTFQLKAERSYHIFY----QITSNKKPDLIemlliTTNPYDYAFVSQGE----ITVPSIDDQEE 331
Cdd:cd14878 153 hLTGARIYTYMLEKSRLVSQPPGQSNFLIFYllmdGLSAEEKYGLH-----LNNLCAHRYLNQTMredvSTAERSLNREK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 332 LMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGN 411
Cdd:cd14878 228 LAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 412 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14878 308 DMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 488 LQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANF 566
Cdd:cd14878 388 MHHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 567 QKPKVVKGKAE-------AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyasaeadssakkg 639
Cdd:cd14878 468 VYSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 640 akkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 719
Cdd:cd14878 535 ------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 153945790 720 DFKQRYKVLnASAIPEGQfidsKKASEKLLASIDIDHTQ---YKFGHTKVFFK 769
Cdd:cd14878 609 DFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
104-769 |
5.49e-88 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 301.93 E-value: 5.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEvvaaYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYFatiaVTGEKKKDEsgkMQGTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNE---ISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 344 FTPEEKVSIYKLTGAVMhYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14937 227 MHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 419 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 499 LEQEEYKKEGIEWTFIDFGMDlAACIELIEKPLGIFSILEEECMFPKATDTSfknkLYDQHLGKSANFQKPKVVKGKAEA 578
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLfstYASAEADSSAKKGakkkgssfQTVSALFRENL 658
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL---YEDVEVSESLGRK--------NLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 153945790 739 IDSKKASEKLLASIDIDhtQYKFGHTKVFFK 769
Cdd:cd14937 609 TDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-769 |
8.43e-88 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 303.88 E-value: 8.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 174 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkdesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH----GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 254 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpdliemllittnpydyafVSQGEITVPSIDDQE--E 331
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAV------------------AAATQKSSAGEGDPEstD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 332 LMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLQSLNS----- 395
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 396 -------ADLLKALCYPRVKVGNEYVTKGQTVQQV------YNAVGALA------KAVYEKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVretrsfFDLDGAAAardaacKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 516 FGMDLAAC--------IELIEKP--------------LGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SANFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 569 PKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVvglyqksamKTLASLFSTYASaEADSSAKKGAKKKGSSFQ 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDEL---------ERLFLACSTYTR-LVGSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 649 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 153945790 729 NASAIPEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14887 687 LPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
108-768 |
3.30e-85 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 294.07 E-value: 3.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 108 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYKPEVVAAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 177
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 178 LITGESGAGKTVNTKRVIQYFATIAVTGEKkkdesgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 256
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK---------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 257 TTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFV--SQGEITV--PSIDDQE- 330
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPlgPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 331 --ELMAtdsAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR 406
Cdd:cd14879 237 fqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 407 VKVGNEYVTkgqtvqqVY-NAVGA------LAKAVYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---FNS 475
Cdd:cd14879 314 KLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGNS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 476 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEEC-MFPKATDTSFKN 553
Cdd:cd14879 387 LDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 554 KLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLN-DTVvglyqksamktlaSLFSTyasaea 632
Cdd:cd14879 466 ALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSpDFV-------------NLLRG------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 633 dssakkgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 712
Cdd:cd14879 527 ------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEY 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 713 PSRILYGDFKQRYKvlnasaiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFF 768
Cdd:cd14879 589 VVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
102-717 |
1.13e-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: 267.16 E-value: 1.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 174 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkdeSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRINL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 253 IHFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGE--- 320
Cdd:cd14884 151 LIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 321 ---------ITVPSIDDQEELMATDSA-----IDILGFTPEEKVSI---YKLTGAVMHYGNMKFKQkqreeqaepdgtev 383
Cdd:cd14884 231 krsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 384 adkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN---------QQLDTKQ 454
Cdd:cd14884 297 ---AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDNED 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 455 PRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF--GMDLAACIELIEK 529
Cdd:cd14884 374 IYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 530 PLGIFSILEEECMfpKATDTSFKNKLYD----QHLGK--SANFQKPKVVKGKAEAH------FSLIHYAGTVDYNITGWL 597
Cdd:cd14884 454 RLDDITKLKNQGQ--KKTDDHFFRYLLNnerqQQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 598 DKNKDPLNDTVVGLYQKSAMKTLaslfstyasaeadssAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCII 677
Cdd:cd14884 532 DKNSDKIETSIETLISCSSNRFL---------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFL 596
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 153945790 678 PNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 717
Cdd:cd14884 597 PNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
104-751 |
5.62e-68 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 243.10 E-value: 5.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyKPEVVAAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14881 3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVI-QYFAtiaVTGEKKKDESGKmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKLA 262
Cdd:cd14881 78 GSGKTYASMLLLrQLFD---VAGGGPETDAFK-------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGALY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPD-LIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14881 147 RTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEeRVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLGI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LG--FTpeekvSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLqSLNSADLLKALcYPRVKVgneyvTKGQT 419
Cdd:cd14881 227 LGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----ARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 420 VQQVYNA------VGALAKAVYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14881 295 VKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 489 QQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PLGIFSILEEECMfPKATDTSFKNKLYDQHLGkSANF 566
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-NPRL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 567 QKPKVVKGKAeahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKsamKTLASLFSTYASaeadssakkgakkkgsS 646
Cdd:cd14881 452 FEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCNFGFATHTQ----------------D 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 647 FQTvsalfreNLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14881 510 FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYR 582
|
650 660
....*....|....*....|....*
gi 153945790 727 VLnASAIPEGQFIDSKKASEKLLAS 751
Cdd:cd14881 583 LL-APFRLLRRVEEKALEDCALILQ 606
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
103-728 |
6.06e-67 |
|
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: 239.77 E-value: 6.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 181
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 182 ESGAGKTVNTKRVIQYfatiaVTGEKKKDESGKMQGTLEDqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14874 72 ESGSGKSYNAFQVFKY-----LTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLQSLNSADLLKALCyPRVKVGNEYvtk 416
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 417 gqTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 496 MFVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSAnFQKpk 570
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK-- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 571 vVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADssakkgakkkgsSFQTV 650
Cdd:cd14874 444 -ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSD------------MIVSQ 510
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 651 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14874 511 AQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
108-712 |
1.86e-66 |
|
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: 239.61 E-value: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 108 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 186
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 187 KTVNTKRVIQYFATIAVTGEKkkdesgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 266
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK----------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 267 ETYLLEKSRVTFQLKAERSYHIFYQ----ITSNKKPdliEMLLITTNPYDYaFVSQGEITVPSIDDQEELMATDSAIDIL 342
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQflkgITDEEKA---AYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 343 GFtPEEKVS-IYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKaAYLQSLNsadllKALCYPRVKVGNEYVT-KGQTV 420
Cdd:cd14905 231 DF-PSEKIDlIFKTLSFIIILGNVTFFQKNGK-------TEVKDR-TLIESLS-----HNITFDSTKLENILISdRSMPV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14905 297 NEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 499 LEQEEYKKEGIEW-TFIDFgMDLAACIELIEKplgIFSILEEECMFPKATDTSFKNKLydqhlgksANFQKPKVVKGKAE 577
Cdd:cd14905 374 QEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 578 AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLAS---LFSTYAS-AEADSSAKKGAKKKGSSFQTVSAL 653
Cdd:cd14905 442 NKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATvAELNQMFDAKNTAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 654 FR------ENLNK-----------------------LMTNLRSTHP---------HFVRCIIPNETKTPGAMEHELVLHQ 695
Cdd:cd14905 522 LScgsnnpNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQ 601
|
650
....*....|....*..
gi 153945790 696 LRCNGVLEGIRICRKGF 712
Cdd:cd14905 602 IKSLCLLETTRIQRFGY 618
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
104-769 |
8.85e-66 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 236.56 E-value: 8.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 184 GAGKTVNTKRVIQYfatIAVTGEKKKDESGKmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGDGNRGATGR--------VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 264 ADIETYLLEKSRVTFQLKAERSYHIFYQI--TSNKKPDLIEMLLITTNPYDYAFVSQG-------------EITVPSIDD 328
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFydFIEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 329 QEELMAtdsaidILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:cd14882 232 FEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 409 VGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEecmfpKATDTSFKNKLYDQHLGKS 563
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 564 ANFQKPkvvkgkAEAH-FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyasaeadssakkgakK 642
Cdd:cd14882 457 SQFVKK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------S 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 643 KGSSFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 718
Cdd:cd14882 516 QVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 719 GDFKQRYKVLnasAIPEGQFIDSKKASEKLLAsIDIDHTQYKFGHTKVFFK 769
Cdd:cd14882 596 QEFLRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-726 |
9.32e-66 |
|
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: 239.10 E-value: 9.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 105 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 175 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGK--MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGAsgVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 253 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK--PDLIEMLLITTNPYDYAFVSQG--EITVPSID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 328 -DQEELMATDSAIDIlgfTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYL-----QSLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 400 KAlcYPRV------------KVGNEYVT--KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 528 E-KPLGIFSILEEECMFPKATDTSFKNKLY--DQHLG------KSANFQKPKVVKGKA-EAHFSLIHYAGTVDYNITGWL 597
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglsrpnMGADTTNEYLAPSKDwRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 598 DKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSSAKKGAKKKGSSFQTVSALFRENLN--------------K 660
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaaASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 661 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-253 |
3.69e-62 |
|
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: 209.89 E-value: 3.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 124 FCVTVNPYKWLPVYKPEVV-AAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 203 VTGEKKKDESG-----KMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 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 ... |
102-767 |
1.02e-43 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 171.94 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 181 GESGAGKTVNTKRVIQYFATIAVTGE-------------KKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRrlptnlndqeednIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 248 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 328 DQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 384
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 385 DKAAYLQS-LNSADLLKALCYPRVK-VGNEYV-TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLLACkLLSFDIETFVKYFTTNyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 537 LEEECMfPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSA 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 617 MKTLASLFSTYasaEADSSAKKGAKKKGSSFQTVSALF---------------RENLNKLMTNLRSTHPHFVRCIIPNET 681
Cdd:cd14938 557 NEYMRQFCMFY---NYDNSGNIVEEKRRYSIQSALKLFkrrydtknqmavsllRNNLTELEKLQETTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 682 KTP-GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAsaipegqfiDSKKASEKLLASIDIDHTQYK 760
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 153945790 761 FGHTKVF 767
Cdd:cd14938 705 IGNNMIF 711
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1144-1912 |
2.30e-28 |
|
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: 125.18 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1144 RELEEISERLEEAggatsaQVELNKKREaEFQKLRRDLEEAtlqhEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKE 1223
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1224 KSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQ-QRLINDLTAQRARLQTEAGEYSRQLDEKDALVS 1302
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1303 QLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRalskansEVAQWRTKYEtDA 1382
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1383 IQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErsnaacaALDKKQRNFDKVLSEWKQK 1462
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1463 YEETQAELEASQKESRSLSTELfkvknvyeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIH----ELEKIKKQVeQ 1538
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVLKASIQGVHgtvaQLGSVGERY-A 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1539 EKCEIQAALEEAEASLEHEEGKILRIQ------------LELNQVKSE-VDRKIAEKDE---------EIDQLKRN---- 1592
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGvigfavdlvEFDPKYEPafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1593 ---HTRVVETMQS-----------TLDAEI-----------RSRNDALRVKKKMEGDLNEMEIQLnhanrlaaESLRNYR 1647
Cdd:TIGR02169 619 vfgDTLVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPAELQRLRERL--------EGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1648 NT-QGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSL 1726
Cdd:TIGR02169 691 SSlQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1727 INTKKKLENDVSQL-----QSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD 1801
Cdd:TIGR02169 771 EEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1802 E--AEQLALKGGKK----QIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQ 1875
Cdd:TIGR02169 851 SieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
810 820 830
....*....|....*....|....*....|....*..
gi 153945790 1876 AKVKSYKRQAEEAEEQSNANLSkFRKLQHELEEAEER 1912
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1259-1936 |
1.54e-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: 122.47 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1259 VSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDekdalvsqlSRSKQAS-TQQIEELKHQLEEetkaknalahalq 1337
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLK---------SLERQAEkAERYKELKAELRE------------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1338 ssrHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASL 1417
Cdd:TIGR02168 225 ---LELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1418 EKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQ 1497
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1498 LETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLE--------LN 1569
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1570 QVKSEVDRKIAEKDEEIDQLKRNHTR------VVETMQSTLDAEIRSRNDALRVKKKMEGDLN--------------EME 1629
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaAIE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1630 IQL-NHANRLAAESLRNYRNTQGILKETQLH------------------------------------------------- 1659
Cdd:TIGR02168 541 AALgGRLQAVVVENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgndreilkniegflgvakdlvkfdpklrkalsy 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1660 ----------LDDALRGQEDLKEQLAIV------------------ERRANLL--QAEIEELWATLEQTERSRKIAEQEL 1709
Cdd:TIGR02168 621 llggvlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaKTNSSILerRREIEELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1710 LDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL 1789
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1790 EQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQD 1869
Cdd:TIGR02168 781 EAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1870 LVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISA 1936
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
952-1750 |
9.80e-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: 119.78 E-value: 9.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 952 ELKKDIDDLELTLAKVEKEKHatENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLE 1031
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEEL--REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1032 QQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKI 1111
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1112 KELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLE----EAGGATSAQVELNKKR-EAEFQKLRRDLEEATL 1186
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqqEIEELLKKLEEAELKElQAELEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1187 QHEAMVAALRKKhADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLeDQVSELKTKE 1266
Cdd:TIGR02168 455 ELERLEEALEEL-REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL-GVLSELISVD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1267 EEQQRLINdlTAQRARLQTEAGEysrqldEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLL 1346
Cdd:TIGR02168 533 EGYEAAIE--AALGGRLQAVVVE------NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1347 REQYEEEQEGKA-------------ELQRALSKANSEVAQWR---------------TKYETDAIQRTEELEEAKKKLAQ 1398
Cdd:TIGR02168 605 KDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggviTGGSAKTNSSILERRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1399 RLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESR 1478
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1479 SLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEK-------IKKQVEQEKCEIQAALEEAE 1551
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlreRLESLERRIAATERRLEDLE 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1552 ASLEHEEGKILRIQLELNQVKSEVDrKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQ 1631
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1632 LNHANRLAAESLRNYRNTQGILKET-QLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWA-TLEqtersrkiAEQEL 1709
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvNLA--------AIEEY 995
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 153945790 1710 LDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQE 1750
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1592 |
1.60e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 119.02 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 843 LKSAETEKEMAtmkEEFQKTKDELAKSEA-----KRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLKEKREYEGyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 918 LEAKIKEVTERAEEE-EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLS 996
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 997 KEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDK 1076
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1077 QQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLS------------- 1143
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggraveevl 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1144 -----------RELEEISER----LEEAGGATSAQV----ELNKKREAEFQKlRRDLEEAT-LQHEAMVAALRKKHADSM 1203
Cdd:TIGR02169 517 kasiqgvhgtvAQLGSVGERyataIEVAAGNRLNNVvvedDAVAKEAIELLK-RRKAGRATfLPLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1204 AELGEQIDNLQRVKQKLEKEKS--------------------ELKMET--DDLSSNAEAI---SKAKGNLEKMCRSLEDQ 1258
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKyvfgdtlvvedieaarrlmgKYRMVTleGELFEKSGAMtggSRAPRGGILFSRSEPAE 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1259 VSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQS 1338
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1339 SRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLE 1418
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1419 KTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQL 1498
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1499 ETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIK------KQVEQEKCEIQAALEEAE-----ASLEHEEGKILRIQLE 1567
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDELK 992
|
810 820
....*....|....*....|....*.
gi 153945790 1568 LNQVKSEVDRK-IAEKDEEIDQLKRN 1592
Cdd:TIGR02169 993 EKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1148-1935 |
9.83e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.31 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1148 EISERLEEAGGATSAQ--VELNKKREAefqkLRRDLEEATLQHEAMVAALRKKHADsMAELGEQIDNLQRVKQKLEKEKS 1225
Cdd:TIGR02168 217 ELKAELRELELALLVLrlEELREELEE----LQEELKEAEEELEELTAELQELEEK-LEELRLEVSELEEEIEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1226 ELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALvsqls 1305
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE----- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1306 rsKQASTQQIEELKHQLEEETKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQR 1385
Cdd:TIGR02168 367 --LEELESRLEELEEQLETLRSKVAQLELQIAS-------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1386 TEELEEAKKKLaqrLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFdkvlsewkQKYEE 1465
Cdd:TIGR02168 438 LQAELEELEEE---LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL--------EGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1466 TQAELEASQKE---SRSLSTELFKVKNVYEESldqLETLRREnkNLQQEISDlteqiaeggkqihelekikkqveqekcE 1542
Cdd:TIGR02168 507 GVKALLKNQSGlsgILGVLSELISVDEGYEAA---IEAALGG--RLQAVVVE---------------------------N 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1543 IQAALEEAEASLEHEEGKilRIQLELNQVKSevdrkiaekdeeiDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKME 1622
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGR--VTFLPLDSIKG-------------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1623 GDLNEMEI--QLNHANRLAAESLRNYRNtqgILKETQLHLDDALRGQEDLKEQLAIVERRANL--LQAEIEELWATLEQT 1698
Cdd:TIGR02168 620 YLLGGVLVvdDLDNALELAKKLRPGYRI---VTLDGDLVRPGGVITGGSAKTNSSILERRREIeeLEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1699 ERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDT 1778
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1779 SAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTE 1858
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1859 EDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKIS 1935
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1611 |
2.37e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.15 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 846 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEV 925
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 926 TERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQET 1005
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1006 hqqtlddLQAEEDKVNILTKAKTKLEQQVDDLEGSLE--QEKKLRMDLERAKRKLEGdlklAQESTMDMENDKQQLDEKL 1083
Cdd:TIGR02168 402 -------IERLEARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEE----LQEELERLEEALEELREEL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1084 EKKEfeisnliSKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISER------LEEAG 1157
Cdd:TIGR02168 471 EEAE-------QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyeaaIEAAL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1158 GATSAQVELNKKREA--EFQKLRRDLEEATLQHEAMVAALRKKHADSMAELgEQIDNLQRVKQKLEKEKSELKMETDDLS 1235
Cdd:TIGR02168 544 GGRLQAVVVENLNAAkkAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL-KNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1236 SN-------AEAISKAKGNLEKMC-------------------RSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGE 1289
Cdd:TIGR02168 623 GGvlvvddlDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1290 YSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANS 1369
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1370 EVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQ 1449
Cdd:TIGR02168 783 EIEELE--------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1450 RNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHEL 1529
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1530 E-KIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-------------KIAEKDEEIDQLKRNHTR 1595
Cdd:TIGR02168 935 EvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeyeELKERYDFLTAQKEDLTE 1014
|
810
....*....|....*....
gi 153945790 1596 VVETMQST---LDAEIRSR 1611
Cdd:TIGR02168 1015 AKETLEEAieeIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
952-1806 |
1.25e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.85 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 952 ELKKDIDDLELTLakVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKaktkle 1031
Cdd:TIGR02169 215 ALLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1032 qqvddlEGSLEQEKKLRmDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKI 1111
Cdd:TIGR02169 287 ------EEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1112 KELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEAtlqhEAM 1191
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1192 VAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLssnaeaiskakgnlekmcRSLEDQVSELktkeeeqQR 1271
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY------------------DRVEKELSKL-------QR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1272 LINDLTAQRARLQTEAGEYSRQLDEKDA-------LVSQLSRSKQastqqieelKHQLEEETKAKNALAHALQSSRHDCD 1344
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGE---------RYATAIEVAAGNRLNNVVVEDDAVAK 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1345 LLREQYEEEQEGKAELQrALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNakcaSLEkTKQRL 1424
Cdd:TIGR02169 562 EAIELLKRRKAGRATFL-PLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE----DIE-AARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1425 QNEVEDLMLD---VERSNAACAALDKKQRNFDKVLSEwKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETL 1501
Cdd:TIGR02169 636 MGKYRMVTLEgelFEKSGAMTGGSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1502 RRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-KIA 1580
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIP 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1581 EKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEG---DLNEMEIQLNHANRLAAESLRNYRNTQGILKETQ 1657
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1658 LHLddalrgqEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDV 1737
Cdd:TIGR02169 875 AAL-------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1738 SQLQSevEEVIQESRNAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQL 1806
Cdd:TIGR02169 948 EEELS--LEDVQAELQRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1168-1831 |
4.10e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1168 KKREAEfQKLrrdleEATLQHEAMVAALRkkhadsmAELGEQIDNLQRVKQKLEKEKsELKMETDDLSSNAEAISKakgn 1247
Cdd:COG1196 173 RKEEAE-RKL-----EATEENLERLEDIL-------GELERQLEPLERQAEKAERYR-ELKEELKELEAELLLLKL---- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1248 lekmcRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETK 1327
Cdd:COG1196 235 -----RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1328 AKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWrtkyETDAIQRTEELEEAKKKLAQRLQEAEEHV 1407
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA----EAELAEAEEALLEAEAELAEAEEELEELA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1408 EAVnakcASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELfkv 1487
Cdd:COG1196 386 EEL----LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1488 knvyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRiqle 1567
Cdd:COG1196 459 ----EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI---- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1568 lnqvkseVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAeirsrndALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYR 1647
Cdd:COG1196 531 -------GVEAAYEAALEAALAAALQNIVVEDDEVAAAA-------IEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1648 NTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAeiEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1727
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1728 NTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLA 1807
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
650 660
....*....|....*....|....
gi 153945790 1808 LKGGKKQIQKLEARVRELEGEVEN 1831
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1315-1923 |
2.41e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1315 IEELKHQLEE-ETKAKNAL-AHALQSSRHDCD--LLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRtEELE 1390
Cdd:COG1196 195 LGELERQLEPlERQAEKAErYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-EELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1391 EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAEL 1470
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1471 EASQKESRSLSTELfkvknvyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEA 1550
Cdd:COG1196 354 EEAEAELAEAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1551 EASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRnhtrvvetmqstLDAEIRSRNDALRVKKKMEGDLNEMEI 1630
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE------------LLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1631 QLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKiaeQELL 1710
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---AAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1711 DASERVQLlhtqntSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLE 1790
Cdd:COG1196 572 GRATFLPL------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1791 QTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAvkgLRKHERRVKELTYQTEEDRKNVLRLQDL 1870
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE---LEEALLAEEEEERELAEAEEERLEEELE 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1871 VDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHE----LEEAEERADIAESQVNKL 1923
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1432 |
7.26e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 842 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAK 921
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 922 IKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKA 1001
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1002 LQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDE 1081
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1082 KLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQ--RSDLSRELEEISERLEEAGGA 1159
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvlIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1160 TSAQVELNKKREAEFQKlRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAE 1239
Cdd:COG1196 551 IVVEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1240 AISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEysRQLDEKDALVSQLSRSKQASTQQIEELK 1319
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA--ELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1320 HQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALskansevaqwrtKYETDAIQRTEELEEAKKKLAQR 1399
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA------------LEELPEPPDLEELERELERLERE 775
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 153945790 1400 LQE-------AEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1432
Cdd:COG1196 776 IEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1100-1750 |
1.45e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1100 EQAVEIQLQKKIKELQARIEELGEEieaeRASRAKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRR 1179
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLREL----EAELEELEAELEELEAELEELEAELAEL--------------EAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1180 DLEEATLQHEAMVAALRKKHAdSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQV 1259
Cdd:COG1196 275 ELEELELELEEAQAEEYELLA-ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1260 SELKTKEEE-QQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQAStQQIEELKHQLEEETKAKNALAHALQS 1338
Cdd:COG1196 354 EEAEAELAEaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1339 SRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDA---IQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCA 1415
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1416 SLEKTKQRLQNEVEDLMLDVERS------NAACAALDKKQRNFDKVLS---EWKQKYEETQAELEASQKESRSLSTELFK 1486
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAyeaaleAALAAALQNIVVEDDEVAAaaiEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1487 VKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQL 1566
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1567 ELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAEslrny 1646
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL----- 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1647 rntqgilketqlhLDDALRGQEDLKEQLAIVERRANLLQAEIEELWAtleqtersrkI---AEQELLDASERVQLLHTQN 1723
Cdd:COG1196 748 -------------LEEEALEELPEPPDLEELERELERLEREIEALGP----------VnllAIEEYEELEERYDFLSEQR 804
|
650 660
....*....|....*....|....*..
gi 153945790 1724 TSLINTKKKLENDVSQLQSEVEEVIQE 1750
Cdd:COG1196 805 EDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-714 |
4.07e-22 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 104.44 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 292 ITS--NKKP--------------DLIEMLLITTNPYDYA-FVSQGEITVPSIDDQEELMatdSAIDILGFTPEEKVSIYK 354
Cdd:cd14894 329 MVAgvNAFPfmrllakelhldgiDCSALTYLGRSDHKLAgFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 355 LTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLQSLNSADLL-KALCYPRVKVGNEYVTKGQTVQ--QVYNAVG 428
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 429 ALAKAVYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLqqF 491
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--Y 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 492 FNHHMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPLGIFSILEEECMFPKATDTSF-----KNKLYDQHL--GKSA 564
Cdd:cd14894 564 AREEQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 565 NFQKPKVVKGKAEAH---------FSLIHYAGTVDYNITGWLDKNKDPL-NDTVVGLYQKSAMKTLASLFSTYA---SAE 631
Cdd:cd14894 638 RLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQlgwSPN 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 632 ADSSAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 711
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNS 797
|
...
gi 153945790 712 FPS 714
Cdd:cd14894 798 SSS 800
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1431 |
8.19e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.60 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 844 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 924 EVTERAEEeeeinaeltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQ 1003
Cdd:TIGR02168 425 ELLKKLEE---------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1004 ethqQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRK-------------------------- 1057
Cdd:TIGR02168 496 ----RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrlqavvvenlnaakkaiaflkqnelg 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1058 ----LEGDLKLAQESTMDMENDKQQLDE------KLEKKEFEISNLIS------KIEDEQAVEIQLQKKIKElQARIEEL 1121
Cdd:TIGR02168 572 rvtfLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSyllggvLVVDDLDNALELAKKLRP-GYRIVTL 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1122 GEEIEAERASRAKAEKQR--SDLSR--ELEEISERLEEAGG-ATSAQVELNKKR------EAEFQKLRRDLEEATLQHEA 1190
Cdd:TIGR02168 651 DGDLVRPGGVITGGSAKTnsSILERrrEIEELEEKIEELEEkIAELEKALAELRkeleelEEELEQLRKELEELSRQISA 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1191 M---VAALRKKH----------ADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLED 1257
Cdd:TIGR02168 731 LrkdLARLEAEVeqleeriaqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1258 QVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQ 1337
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1338 SSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASL 1417
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
650
....*....|....
gi 153945790 1418 EKTKQRLQNEVEDL 1431
Cdd:TIGR02168 971 RRRLKRLENKIKEL 984
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
966-1866 |
2.23e-21 |
|
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: 102.36 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 966 KVEKEKHATENKVKNLTEEMAGLDETIaklsKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEK 1045
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKR----KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1046 KLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEI 1125
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1126 EAErasRAKAEKQRSDLSRELEEISERLEEAggatSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAE 1205
Cdd:pfam02463 299 KSE---LLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1206 LGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQrARLQT 1285
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK-LTEEK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1286 EAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALS 1365
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1366 KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAAL 1445
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1446 DKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKN-----VYEESLDQLETLRRENKNLQQEISDLTEQIA 1520
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLeeglaEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1521 EGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrvVETM 1600
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK----EEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1601 QSTLDAEIRSRndalrvkKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERR 1680
Cdd:pfam02463 767 SELSLKEKELA-------EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1681 ANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEveevIQESRNAEEKAKK 1760
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL----EEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1761 AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAV 1840
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890 900
....*....|....*....|....*.
gi 153945790 1841 KGLRKHERRVKELTYQTEEDRKNVLR 1866
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
868-1431 |
2.88e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 868 KSEAKRKELEEkmvtLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLE 947
Cdd:COG1196 219 KEELKELEAEL----LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 948 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAK 1027
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1028 TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQL 1107
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1108 QKKIKELQARIEELGEEIEAERASRAKAE------KQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDL 1181
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLeelaeaAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1182 EEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAE---AISKAKGNLEKMCRSLEDQ 1258
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALargAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1259 VSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQS 1338
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1339 SRHdcDLLREQYEEEQEGKAELQRALSKANSEVAQwRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAvnakcASLE 1418
Cdd:COG1196 695 LEE--ALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEEELLEEEALEELPEPPDL-----EELE 766
|
570
....*....|...
gi 153945790 1419 KTKQRLQNEVEDL 1431
Cdd:COG1196 767 RELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
915-1536 |
1.47e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 915 KIQLEAKIKEVT---ERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 991
Cdd:COG1196 217 ELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 992 IAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMD 1071
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1072 MENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISE 1151
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1152 RLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMET 1231
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1232 DDLSSNAEAISKAKGNLEKMcRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQAS 1311
Cdd:COG1196 537 EAALEAALAAALQNIVVEDD-EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1312 TQQIEELKHQLEEETKAKNALAhalqssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEE 1391
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALR------------RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1392 AKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELE 1471
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1472 ASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQV 1536
Cdd:COG1196 764 ELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
833-1517 |
2.73e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 833 MKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLI 912
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 913 KNKIQLEAKikevteraeeeeeinaelTAKKRKLEDECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETI 992
Cdd:PTZ00121 1342 KKAAEAAKA------------------EAEAAADEAEAAEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 993 AKLSKEKKALQETHQQTLDDLQAEEdkvnilTKAKTKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEGDLKlaqestmdM 1072
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKK--------A 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1073 ENDKQQLDEKLEKKEfeisnLISKIEDEQAVEiQLQKKIKELQARieelgeeieAERASRAKAEKQRSDLSRELEEISE- 1151
Cdd:PTZ00121 1460 EEAKKKAEEAKKADE-----AKKKAEEAKKAD-EAKKKAEEAKKK---------ADEAKKAAEAKKKADEAKKAEEAKKa 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1152 ----RLEEAGGATSAQVELNKKREAEFQKLR--RDLEEATLQHEAMVAALRKKHADSMAELGEQIDNlQRVKQKLEKEKS 1225
Cdd:PTZ00121 1525 deakKAEEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEE 1603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1226 ELKMETDDLSSNAEAISKAKgnlekmcrsledqvsELKtKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLS 1305
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAE---------------ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1306 RSKQASTQQIEELKHQLEEETKAKNALAHALQSSRhDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQR 1385
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KK 1745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1386 TEEL---EEAKKKLAQRLQEAEEHVEAVNAKCASLekTKQRLQNEVEDLMLDVER------SNAACAALDKKQRNFdkVL 1456
Cdd:PTZ00121 1746 AEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKkikdifDNFANIIEGGKEGNL--VI 1821
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1457 SEWKQKYEETQAELEASQ----KESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTE 1517
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKnmqlEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1599 |
4.87e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 856 KEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvQSEADSLADAEERCEQLIK----NKIQLEAKIKEVTERAEE 931
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDAR---KAEAARKAEEERKAEEARKaedaKKAEAVKKAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 932 EEEINaeltaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlTEEMAGLDEtiAKLSKEKKALQETHQQTLD 1011
Cdd:PTZ00121 1242 AKKAE-----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADE--AKKAEEKKKADEAKKKAEE 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1012 DLQAEEDKVNI------LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEK--- 1082
Cdd:PTZ00121 1314 AKKADEAKKKAeeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkka 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1083 --LEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAT 1160
Cdd:PTZ00121 1394 deAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1161 SAQVELNKKREAEfqKLRRDLEEATLQ-HEAMVAALRKKHADSMAELGEQidnlqrvKQKLEKEKSELKMETDDLsSNAE 1239
Cdd:PTZ00121 1474 EAKKKAEEAKKAD--EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEA-KKAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1240 AISKAkgnlEKMCRSLEDQVSELKTKEEEQQRlindlTAQRARLQTEAGEYSRQLDEKdALVSQLSRSKQASTQQIEELK 1319
Cdd:PTZ00121 1544 EKKKA----DELKKAEELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAK 1613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1320 HqlEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL----EEAKKK 1395
Cdd:PTZ00121 1614 K--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKA 1690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1396 LAQRLQEAEE--HVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSnaacaaldKKQRNFDKVLSEWKQKYEETQAELEAS 1473
Cdd:PTZ00121 1691 AEALKKEAEEakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1474 QKESRSLSTELFKVKN-VYEESLDQLETLRR-ENKNLQQEISDLTEQIAEGGKQIHELekIKKQVEQEKCEIQAALEEAE 1551
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEaVIEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKN 1840
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 153945790 1552 ASLEhEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVET 1599
Cdd:PTZ00121 1841 MQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1535 |
6.62e-20 |
|
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: 97.43 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 844 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 924 EVTERAEEEEEINAELTAKKRKLEDECSELKKDIDdleltlakvEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQ 1003
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1004 ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMdlerAKRKLEGDLKLAQESTMDMENDKQQLDEKL 1083
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK----NQSGLSGILGVLSELISVDEGYEAAIEAAL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1084 EKKefeISNLISKIEDEQAVEIQLQKKIKELQARI----EELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG- 1158
Cdd:TIGR02168 544 GGR---LQAVVVENLNAAKKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSy 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1159 -------ATSAQVELNKKREAEFQKL------------------RRDLEEATLQHEAMVAALRKKhadsMAELGEQIDNL 1213
Cdd:TIGR02168 621 llggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREIEELEEK----IEELEEKIAEL 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1214 QRVKQKLEKEKSELKMETDDLSSNAEAIS-------KAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTE 1286
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSrqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1287 AGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSK 1366
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1367 ANSEVAQWRTKYETdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALD 1446
Cdd:TIGR02168 857 LAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1447 KK-QRNFDKVLSEWK-------QKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQ 1518
Cdd:TIGR02168 936 VRiDNLQERLSEEYSltleeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEA 1015
|
730
....*....|....*..
gi 153945790 1519 IAEGGKQIHELEKIKKQ 1535
Cdd:TIGR02168 1016 KETLEEAIEEIDREARE 1032
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1458 |
1.29e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 844 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 924 EVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEK---- 999
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGerya 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1000 KALQETHQQTLDDLQAEEDKV-----NILTKAK---------TKLEQQVDDLE-GSLEQEKKLRMDLERAKRKLEGDLKL 1064
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVakeaiELLKRRKagratflplNKMRDERRDLSiLSEDGVIGFAVDLVEFDPKYEPAFKY 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1065 AQESTM---DMENDKQQLDE----KLEKKEFEISNLIS----KIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRA 1133
Cdd:TIGR02169 619 VFGDTLvveDIEAARRLMGKyrmvTLEGELFEKSGAMTggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1134 KAEKQR-------SDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLE--EATLQH--------EAMVAALR 1196
Cdd:TIGR02169 699 RIENRLdelsqelSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvKSELKElearieelEEDLHKLE 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1197 KKHADSMAELG-EQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLIND 1275
Cdd:TIGR02169 779 EALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1276 LTAQRARLQTEAGEYSRQLDEKDALVSQLSRskqastqQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQE 1355
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKK-------ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1356 GKAELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDL---- 1431
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleri 1009
|
650 660
....*....|....*....|....*...
gi 153945790 1432 -MLDVERSNAACAALDKKQRNFDKVLSE 1458
Cdd:TIGR02169 1010 eEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1536 |
6.13e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 90.90 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 846 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEK--------MVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 918 LEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSK 997
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQT---LDDLQAE----EDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqestm 1070
Cdd:TIGR02169 407 ELDRLQEELQRLseeLADLNAAiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD------- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1071 DMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIK---------------------------------ELQAR 1117
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataievaagnrlnnvvvEDDAV 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1118 IEELGEEIEAERASRA------KAEKQRSDLSRELEEiserleEAGGATSAQVELNKKREAEFQKLRRD------LEEA- 1184
Cdd:TIGR02169 560 AKEAIELLKRRKAGRAtflplnKMRDERRDLSILSED------GVIGFAVDLVEFDPKYEPAFKYVFGDtlvvedIEAAr 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1185 ---------TLQHE------AMVAALRK---------KHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEA 1240
Cdd:TIGR02169 634 rlmgkyrmvTLEGElfeksgAMTGGSRAprggilfsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1241 ISK-----------AKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQteagEYSRQLDE-KDALVSQLSRSK 1308
Cdd:TIGR02169 714 ASRkigeiekeieqLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE----ELEEDLHKlEEALNDLEARLS 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1309 QASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEE 1388
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1389 LEEAKKKLAQ---RLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:TIGR02169 870 LEELEAALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1466 T------QAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAeggkqihELEKIKKQV 1536
Cdd:TIGR02169 950 ElsledvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE-------EYEKKKREV 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1020-1628 |
1.17e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 89.71 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1020 VNILTKAKTKLEQQVDDlegSLEQEKKLRMDLERAkrkleGDLKLAQEstmDMENDKQqldEKLEKKEFEIsnliskied 1099
Cdd:PRK02224 140 VNKLINATPSDRQDMID---DLLQLGKLEEYRERA-----SDARLGVE---RVLSDQR---GSLDQLKAQI--------- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1100 EQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqvelnKKREAEFQKLRR 1179
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-----------ETLEAEIEDLRE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1180 DLEEATLQHEamvaalrkkhadsmaELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQV 1259
Cdd:PRK02224 266 TIAETERERE---------------ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1260 SELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSS 1339
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1340 RHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQEAEEH 1406
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1407 VEAVNAKCASLEKTK------QRLQNEVEDL--MLD-----VERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEAS 1473
Cdd:PRK02224 491 VEEVEERLERAEDLVeaedriERLEERREDLeeLIAerretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1474 QKESRSLSTELFKVKNVYEeSLDQLETLRRENKNLQQEISDLTEQIaeggKQIHELEKIKKQVEQEKCEIQAALEEA--E 1551
Cdd:PRK02224 571 REEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKR----EALAELNDERRERLAEKRERKRELEAEfdE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1552 ASLEHEEGKILRIQLELNQVKSEVDRKIAEKD-------------EEIDQLKRNHTRV-------------VETMQST-- 1603
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQVEEKLDELREERDdlqaeigavenelEELEELRERREALenrvealealydeAEELESMyg 725
|
650 660
....*....|....*....|....*.
gi 153945790 1604 -LDAEIRSRNDAlrvkkKMEGDLNEM 1628
Cdd:PRK02224 726 dLRAELRQRNVE-----TLERMLNET 746
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1914 |
2.67e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.04 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1239 EAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRsKQASTQQIEEL 1318
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1319 KHQleEETKAKNALAHALQSSRHDcdllrEQYEEEQEGKAELQRALSKAN--SEVAQWRTKYETDAIQRTEEL----EEA 1392
Cdd:PTZ00121 1170 RKA--EDAKKAEAARKAEEVRKAE-----ELRKAEDARKAEAARKAEEERkaEEARKAEDAKKAEAVKKAEEAkkdaEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1393 KKklAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:PTZ00121 1243 KK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1473 SQK--ESRSLSTELfkvKNVYEESLDQLETLRRENKNLQQEisdlteqiAEGGKQIHELEKIKKQVEQEKCEiqAALEEA 1550
Cdd:PTZ00121 1321 KKKaeEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKAEAAEKKKEEAKKKAD--AAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1551 EASLEHEEgkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALrvKKKMEGDLNEMEI 1630
Cdd:PTZ00121 1388 EEKKKADE---AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA--KKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1631 QLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAE---- 1706
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakka 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1707 QELLDASE---RVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQ-ESRNAEEKAKKAITDAAMMAEELKKEQDTSAHL 1782
Cdd:PTZ00121 1543 EEKKKADElkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1783 ERMKK------NLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGE--------VENEQKRNAEAVKGLRKHER 1848
Cdd:PTZ00121 1623 EELKKaeeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeakkAEEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1849 RVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAE---EQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1076-1804 |
2.89e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 88.64 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1076 KQQLDEKLEKKEFEISNLISKIEDEQAV----EIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISE 1151
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELhekqKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1152 RLEeagGATSAQVELNKKREAEFQKLRRDLeeatLQHEAMVAALRKKHADSMAELGEQI---DNL------------QRV 1216
Cdd:pfam15921 153 ELE---AAKCLKEDMLEDSNTQIEQLRKMM----LSHEGVLQEIRSILVDFEEASGKKIyehDSMstmhfrslgsaiSKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1217 KQKLEKEKSELKMETDDLSSNAEAI-SKAKGNLEKMCRSLEDQVSELKTKEEEQ-----------QRLINDLTAQRARLQ 1284
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEVEitgltekassaRSQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1285 TEA----GEYSRQLDEKDALVSQ----LSRSKQASTQQIEELKHQL----EEETKAKNALAHALQSSRHDCD----LLRE 1348
Cdd:pfam15921 306 EQArnqnSMYMRQLSDLESTVSQlrseLREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDqlqkLLAD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1349 QYEEEQEGKAELQRALSKANSEVAQWRT----KYETD----AIQRTEELEEAKKKLAQ--------RLQEAEEHVEAVNA 1412
Cdd:pfam15921 386 LHKREKELSLEKEQNKRLWDRDTGNSITidhlRRELDdrnmEVQRLEALLKAMKSECQgqmerqmaAIQGKNESLEKVSS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1413 KCASLEKTKQRLQNEVEDLM---LDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKN 1489
Cdd:pfam15921 466 LTAQLESTKEMLRKVVEELTakkMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1490 VYEESlDQLETLRRENKN----LQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQ 1565
Cdd:pfam15921 546 VQTEC-EALKLQMAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1566 -----LELNQVK-----SEVDRKIAEKDEEIDQLKRNHTRVVETMQS-TLDAEIRSRNdaLRVK-KKMEGDLNEMEIQLN 1633
Cdd:pfam15921 625 arvsdLELEKVKlvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlSEDYEVLKRN--FRNKsEEMETTTNKLKMQLK 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1634 HANrlaaESLRNYRNTQGILKETQLHlddALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDAS 1713
Cdd:pfam15921 703 SAQ----SELEQTRNTLKSMEGSDGH---AMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1714 ERVQLLHTQntslintKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmkknleqtv 1793
Cdd:pfam15921 776 QELSTVATE-------KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK---------- 838
|
810
....*....|.
gi 153945790 1794 kdLQHRLDEAE 1804
Cdd:pfam15921 839 --LQHTLDVKE 847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1027-1610 |
3.09e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.43 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1027 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESTMDMENDKQQLDEklekkefeisnLISKIEDEQAve 1104
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA-- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1105 iqlQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGAT---------SAQVELNKKRE--AE 1173
Cdd:COG4913 287 ---QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlereieRLERELEERERrrAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1174 FQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNL----- 1248
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparll 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1249 ---EKMCRSLEDQVSEL---------KTKEEEQQ----RLINDltaQRARLQTEAGEYSRQLdekdALVSQLSRSKQAST 1312
Cdd:COG4913 444 alrDALAEALGLDEAELpfvgelievRPEEERWRgaieRVLGG---FALTLLVPPEHYAAAL----RWVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1313 QQIEELKHQLEEETKAKNALAHALQSSRHDC-DLLREQYEEEQ-----EGKAELQRA--------LSKANSEVAQ----- 1373
Cdd:COG4913 517 ERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrr 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1374 -WRTKYET--DAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMLDVERSNAACAALDKK 1448
Cdd:COG4913 597 rIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1449 QRNFDK---VLSEWKQKYEETQAELEASQKESRSLSTELFKVknvyEESLDQLETLRRENKNLQQEISDL--TEQIAEGG 1523
Cdd:COG4913 677 LERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRL----EKELEQAEEELDELQDRLEAAEDLarLELRALLE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1524 KQIHELeKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQV----KSEVDRKIAE------------------ 1581
Cdd:COG4913 753 ERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESlpeylalldrleedglpe 831
|
650 660 670
....*....|....*....|....*....|
gi 153945790 1582 -KDEEIDQLKRNHTRVVETMQSTLDAEIRS 1610
Cdd:COG4913 832 yEERFKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1074-1922 |
3.18e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.04 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1074 NDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARieeLGEEIEAERASRAKAEKQRSDLSRELEEI---- 1149
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK---KTETGKAEEARKAEEAKKKAEDARKAEEArkae 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1150 -SERLEEAGGATSAQVELNKKREAEFQKLR--RDLEEATLQHEAMVA-ALRKKHADSMAELGEQIDNLQRVKQKLEKEKS 1225
Cdd:PTZ00121 1138 dARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAARKAeEVRKAEELRKAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1226 ElKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQrlINDLTAQRARLQTEAGEYSRQLDEKDALVSQLS 1305
Cdd:PTZ00121 1218 R-KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1306 RSKQASTQQIEELKHQLEEETKAKNALAHAlQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQR 1385
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1386 TEE---LEEAKKKLAQ--RLQEAEEHVEAVNAKCASLEKtKQRLQNEVEDLMLDVERSNAACAAldKKQRNFDKVLSEWK 1460
Cdd:PTZ00121 1374 EEAkkkADAAKKKAEEkkKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1461 QKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQiAEGGKQIHELEKIKKQVEQEK 1540
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKK 1529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1541 CEIQAALEEAEASLEHEEGKILRIQLELNqvKSEVDRKIAEKDEEiDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKK 1620
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1621 MEGDlnemEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQT-- 1698
Cdd:PTZ00121 1607 MKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkk 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1699 --ERSRKIAEQELLDASErvqllhtqntslintKKKLEndvsqlqsEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQ 1776
Cdd:PTZ00121 1683 aeEDEKKAAEALKKEAEE---------------AKKAE--------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1777 DTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVK--------GLRKHER 1848
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFdnfaniieGGKEGNL 1819
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1849 RVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEEraDIAESQVNK 1922
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE--EIEEADEIE 1891
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1258-1924 |
3.43e-17 |
|
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: 88.31 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1258 QVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQ-------------ASTQQIEELKHQLEE 1324
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElcaeaeemrarlaARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1325 ETKAKNALAHALQSSR----HDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQRL 1400
Cdd:pfam01576 83 RLEEEEERSQQLQNEKkkmqQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS-KLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1401 QEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSL 1480
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1481 STELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGK 1560
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1561 ILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAA 1640
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1641 ESLRNYRNTQGILKETQLHLDDALRGQEDLKEqlaiverRANLLQAEIEELWATLEQTE----RSRK---IAEQELLDAS 1713
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgkniKLSKdvsSLESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1714 ERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTV 1793
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1794 KDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVEN---EQKRNAEAVKGLRKHERRVKELtyqTEEDRKNVLRLQDL 1870
Cdd:pfam01576 555 EALTQQLEEKAA--------AYDKLEKTKNRLQQELDDllvDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEE 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1871 VDKLQAkvksykrqaeEAEEQSNANLSkfrkLQHELEEAEERADIAESQVNKLR 1924
Cdd:pfam01576 624 RDRAEA----------EAREKETRALS----LARALEEALEAKEELERTNKQLR 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
857-1856 |
5.60e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 87.87 E-value: 5.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 857 EEFQKTKDELAKSEAKRKELEEKMVTLLKEKN-DLQLQVQS---EADSLADA---EERCEQLIKNKIQ-----LEAKIKE 924
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSViDLQTKLQEmqmERDAMADIrrrESQSQEDLRNQLQntvheLEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 925 VTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH------------ATENKVKNLTEEMAGLDETI 992
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDsmstmhfrslgsAISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 993 AKLSKEKKALQETHQQTLDDL-QAEEDKVNILTKaktklEQQVDdLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESTmd 1071
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLlQQHQDRIEQLIS-----EHEVE-ITGLTEKASSARSQANSIQSQLE----IIQEQA-- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1072 mENDKQQLDEKLEKKEFEISNLISKIEDEQAVeiqLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISE 1151
Cdd:pfam15921 309 -RNQNSMYMRQLSDLESTVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1152 RLEEAGGATSAQVELNKK-------REAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEK 1224
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1225 S---ELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALv 1301
Cdd:pfam15921 465 SltaQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHL- 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1302 sqlsRSKQAstqQIEELKHQLEEETKAknalahalqssrhdCDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkYETD 1381
Cdd:pfam15921 544 ----RNVQT---ECEALKLQMAEKDKV--------------IEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKE 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1382 AIQRTEELEEAK----------KKLAQRLQEAE-EHVEAVNAKCASLEKTKQrLQNEVEDLMLDVERSNAACAALDKK-- 1448
Cdd:pfam15921 599 INDRRLELQEFKilkdkkdakiRELEARVSDLElEKVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNELNSLSEDye 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1449 --QRNF-------DKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQI 1519
Cdd:pfam15921 678 vlKRNFrnkseemETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1520 AEGGKQIHELEKIKKQVEQ-------EKCEIQAALEEAEASLEHEEGKILRIQLELNQVK---SEVDRKIAEKDEEIDQL 1589
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQelstvatEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfAECQDIIQRQEQESVRL 837
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1590 KRNHTRVVETMQS---TLDAEIRSRNdalrvkkkmegdLNEMEIQLNHANRLAAESLRNYRNTQGiLKETQLHLDDALRG 1666
Cdd:pfam15921 838 KLQHTLDVKELQGpgyTSNSSMKPRL------------LQPASFTRTHSNVPSSQSTASFLSHHS-RKTNALKEDPTRDL 904
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1667 QEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQeLLDASERVQLLHTQNTSLINTKKKLENDVSQlqsevEE 1746
Cdd:pfam15921 905 KQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDC-IIESSLRSDICHSSSNSLQTEGSKSSETCSR-----EP 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1747 VIQESRNAEEKAkKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDL---------QHR----------LDEAEQLA 1807
Cdd:pfam15921 979 VLLHAGELEDPS-SCFTFPSTASPSVKNSASRSFHSSPKKSPVHSLLTSSaegsigsssQYRsaktihspdsVKDSQSLP 1057
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 153945790 1808 LKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQ 1856
Cdd:pfam15921 1058 IETTGKTCRKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1625-1926 |
1.11e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1625 LNEMEIQLNHANRlAAESLRNYRNTQGILKETQLHLddALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKI 1704
Cdd:COG1196 195 LGELERQLEPLER-QAEKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1705 AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1784
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1785 MKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEgEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNV 1864
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 1865 LRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVK 1926
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
975-1592 |
1.30e-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: 86.23 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 975 ENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILtkaktklEQQVDDLEGSLEQEKKLRMDLERA 1054
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL-------EQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1055 KRKLEGDLKlaqestmdmeNDKQQLDekleKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAK 1134
Cdd:TIGR04523 105 LSKINSEIK----------NDKEQKN----KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1135 AEKQRSDLSRELEEISERLEEaggatsaqveLNKKREAEFQKLRrDLEEATLQHeamvaalrKKHADSMAELGEQIDNLQ 1214
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDK----------IKNKLLKLELLLS-NLKKKIQKN--------KSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1215 RVKQKLEKEKSELKMEtddLSSNAEAISKAKGNLEKMCRSLEDQVSELktkeEEQQRLINDLTAQRARLQTEAGEYSRQL 1294
Cdd:TIGR04523 232 DNIEKKQQEINEKTTE---ISNTQTQLNQLKDEQNKIKKQLSEKQKEL----EQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1295 DEKdaLVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQW 1374
Cdd:TIGR04523 305 EQD--WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1375 RtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDK 1454
Cdd:TIGR04523 383 K--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1455 VLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKK 1534
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1535 QVEQEKCEIQAALEEAEASLEHE--EGKILRIQLELNQVKSE---VDRKIAEKDEEIDQLKRN 1592
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEKE 597
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1211-1910 |
2.85e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.41 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1211 DNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLiNDLTAQRARLQTEAGEY 1290
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1291 SRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEEtkaknALAHALQSSrhdcdllREQYEEEQEGKAELQRALSKANSE 1370
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRARKAAPLAAHIK-----AVTQIEQQA-------QRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1371 VAQwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTK-------QRLQNEVEDLMLDVERSNAACA 1443
Cdd:TIGR00618 334 VKQ-------------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1444 ALDKKQRNFDKVLSEwKQKYEETQAELEASQKESRsLSTELFKVKNVYEESLDQLETLR-RENKNLQQEISDLTEQIAEg 1522
Cdd:TIGR00618 401 ELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKEREQQLQT- 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1523 GKQIHELEKIKKQVEQEKCEIQAALE-EAEASLEHEEGK-------------ILRIQLELNQVKSEVDRKIAEKDEEIDQ 1588
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1589 LKRNHTRVVETMQSTLDAEI---RSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALR 1665
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1666 GQEDLKEQLAIVERRANLLQAEIEELW-ATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLENDVSQLQSEV 1744
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHAlSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1745 EEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ---IQKLEAR 1821
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAEIQFF 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1822 VRELEgEVENEQKRNAEAVKGLRKHERRVKELT-YQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFR 1900
Cdd:TIGR00618 791 NRLRE-EDTHLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
730
....*....|
gi 153945790 1901 KLQHELEEAE 1910
Cdd:TIGR00618 870 KIIQLSDKLN 879
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1377 |
8.75e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 8.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 840 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvqSEADSLADAEERCEQLIKNKIQLE 919
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 920 AKIKEVTERAEEEEEINAELTAKKRKLE------DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 993
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 994 KLSKEKKALQEthqqTLDDLQAEEDKVNILTKAKTKLEQ--QVDDLEGSLEQEKKLRM--DLERAKRKLEGDLKLAQEST 1069
Cdd:PRK03918 339 RLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1070 MDMENDKQQLD---EKLEKKEFEISNLISKIEDEQAVEI--QLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSR 1144
Cdd:PRK03918 415 GELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1145 --ELEEISERLEEAGGATSA-QVELNKKREAEFQKLRRDLEEATLQHEAMvaalrKKHADSMAELGEQIDNLQRVKQKLE 1221
Cdd:PRK03918 495 liKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSL-----KKELEKLEELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1222 KEKSELKMETDDLS-SNAEAISKAKGNLEKMCR---SLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEK 1297
Cdd:PRK03918 570 EELAELLKELEELGfESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1298 DALVSQLSRSKQastQQIEELKHQLEEETKAKNALAHALQSSRH----DCDLLREQYEEEQEGKAELQRaLSKANSEVAQ 1373
Cdd:PRK03918 650 EELEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREeikkTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
....
gi 153945790 1374 WRTK 1377
Cdd:PRK03918 726 LREK 729
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1071-1803 |
1.21e-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: 83.15 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1071 DMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAeraSRAKAEKQRSDLSRELEEIS 1150
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK---NKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1151 ERleeaggatsaqVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADsMAELGEQIDNLQRVKQKLEKEKSELKME 1230
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1231 TDDLSSNaeaISKAKGNLEKmcrsLEDQVSELKTKEEEQQRL---INDLTAQRARLQTEAGEYSRQLDEKDALVSQlsrs 1307
Cdd:TIGR04523 182 KLNIQKN---IDKIKNKLLK----LELLLSNLKKKIQKNKSLesqISELKKQNNQLKDNIEKKQQEINEKTTEISN---- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1308 kqaSTQQIEELKhqlEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEvaqWRTKYETDAIQRTE 1387
Cdd:TIGR04523 251 ---TQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1388 ELEEAKKKLAQrlqeAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQ 1467
Cdd:TIGR04523 322 KLEEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1468 AELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAAL 1547
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1548 EEAEASLEHEEGKILRIQ---LELNQVKSEVDRKIAEKDEEIDQLKRNhTRVVETMQSTLDAEIRSRNDALrVKKKMEGD 1624
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1625 LNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKI 1704
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1705 AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKA----KKAIT------DAAMMAEELKK 1774
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELslhyKKYITrmirikDLPKLEEKYKE 715
|
730 740
....*....|....*....|....*....
gi 153945790 1775 EQDTSAHLERMKKNLEQTVKDLQHRLDEA 1803
Cdd:TIGR04523 716 IEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1080-1598 |
1.27e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1080 DEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGA 1159
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1160 TSAQVELNKKREAEFQKLR------RDLEEATLQHEAMVAALR--KKHADSMAELGEQIDNLQRVKQKLEKEKSELKMET 1231
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1232 DDLS---SNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRlINDLTAQRARLQTEAGEYSrqLDEKDALVSQLSRSK 1308
Cdd:PRK03918 324 NGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLT--PEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1309 QASTQQIEEL---KHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEG--KAELQRALSKANSEVAQWRTKyETDAI 1383
Cdd:PRK03918 401 EEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEK-ERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1384 QRTEELEEA---------KKKLAQRLQEAEEHVEAVN-----AKCASLEKTKQR---LQNEVEDLMLDVERSNA---ACA 1443
Cdd:PRK03918 480 KELRELEKVlkkeselikLKELAEQLKELEEKLKKYNleeleKKAEEYEKLKEKlikLKGEIKSLKKELEKLEElkkKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1444 ALDKKQRNFDKVLSEWKQKYEE----TQAELEASQKESRSLSTELFKVKNV---YEESLDQLETLRRENKNLQQEISDLT 1516
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1517 EQIAEGGKQIHELEKI-----KKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDrKIAEKDEEIDQLKR 1591
Cdd:PRK03918 640 KRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEK 718
|
....*..
gi 153945790 1592 NHTRVVE 1598
Cdd:PRK03918 719 ALERVEE 725
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
868-1587 |
1.37e-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: 82.76 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 868 KSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLiKNKIQ-LEAKIKEVTERAEEEEEINAELTAKKRKL 946
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 947 EDECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDK 1019
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1020 VNILTKAKTKLEQQVDDLEGSLEQEKKLR---MDLERAKRKLEGDLKLAQestmdmeNDKQQLDEKLEKKEFEISNLISK 1096
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1097 IEDEQAveiQLQKKIKELQarieelgeeieaerasraKAEKQRSDLSRELEEISERLEEAGgaTSAQVELNKKREAEFQK 1176
Cdd:TIGR04523 262 QNKIKK---QLSEKQKELE------------------QNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1177 LRRDLEEATLQheamvaalRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLE 1256
Cdd:TIGR04523 319 QEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1257 DQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEkdalvsqLSRSKQASTQQIEELKHQLEEETKAKNALAHAL 1336
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1337 QSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCAS 1416
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK--------LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1417 LEKTKQRLQNEVEDLMLDVERSNaacaaLDKKQRNFDKVLSEWKQkyeeTQAELEASQKESrslstelfkvknvyEESLD 1496
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQ----TQKSLKKKQEEK--------------QELID 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1497 QLETlrrENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHeegkilrIQLELNQVK---S 1573
Cdd:TIGR04523 593 QKEK---EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ-------IKETIKEIRnkwP 662
|
730
....*....|....
gi 153945790 1574 EVDRKIAEKDEEID 1587
Cdd:TIGR04523 663 EIIKKIKESKTKID 676
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
948-1431 |
1.86e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 948 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKkALQETHQQTLDDLQAEedkvniltkak 1027
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREE----------- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1028 tkLEQQVDDLEGSLEQEkklRMDLERAKRKLEGdlklAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQL 1107
Cdd:PRK02224 319 --LEDRDEELRDRLEEC---RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1108 QKKIKELQARIEelgeeieaerasrakaekqrsDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEAtlq 1187
Cdd:PRK02224 390 EEEIEELRERFG---------------------DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA--- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1188 hEAMVAALR----------KKHADSMAELGEQIDnlqrvkqKLEKEKSELKMETDDLSSNAEAISKAKgNLEKMCRSLED 1257
Cdd:PRK02224 446 -EALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1258 QVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAH--- 1334
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirt 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1335 ---ALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEHVEAVN 1411
Cdd:PRK02224 597 llaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELR 673
|
490 500
....*....|....*....|
gi 153945790 1412 AKCASLEKTKQRLQNEVEDL 1431
Cdd:PRK02224 674 EERDDLQAEIGAVENELEEL 693
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
840-1703 |
2.19e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.71 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 840 KPLLKSAETEKEMATMKEefqktKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQliKNKIQLE 919
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRL-----KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL--KEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 920 AKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEK 999
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1000 KALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSL-----------EQEKKLRMDLERAKRKLEGDLKLAQES 1068
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELkeleikreaeeEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1069 TMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEE 1148
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1149 ISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLE--KEKSE 1226
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGvaVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1227 LKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQ-------RARLQTEAGEYSRQLDEKDA 1299
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidpiLNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1300 LVSQLSRSKQASTQQIEELKhQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1379
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAK-AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1380 TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErsnaacaALDKKQRNFDKVLSEW 1459
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1460 KQKYEETQAELEASQKESRSLSTEL-FKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQ 1538
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1539 EKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTL--DAEIRSRNDALR 1616
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEerIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1617 VKKKMEGDLNEMEIQLNHANRLAAEsLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLE 1696
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
....*..
gi 153945790 1697 QTERSRK 1703
Cdd:pfam02463 1014 ETCQRLK 1020
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1146-1806 |
5.08e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.24 E-value: 5.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1146 LEEISERleeAGGATSAQVELNKKREAEFQKLRRDLE--EATLQHEAmVAALRKKhadsMAELGEQIDNLQRVKQKLEKE 1223
Cdd:PRK02224 164 LEEYRER---ASDARLGVERVLSDQRGSLDQLKAQIEekEEKDLHER-LNGLESE----LAELDEEIERYEEQREQARET 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1224 KSELKMETDDLSSNAEAISKAKGNLEKmcrsLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQ 1303
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1304 LSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE---- 1379
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEelee 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1380 --TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQN---EVEDLM---------LDVERSNAACAal 1445
Cdd:PRK02224 392 eiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveEAEALLeagkcpecgQPVEGSPHVET-- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1446 dkkqrnfdkvLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ 1525
Cdd:PRK02224 470 ----------IEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1526 IHELEKIKKQVEQEkceiqAALEEAEASLEHEEGKILRIQLelnqvkSEVDRKIAEKDEEIDQLKRnhtrvVETMQSTLd 1605
Cdd:PRK02224 539 AEELRERAAELEAE-----AEEKREAAAEAEEEAEEAREEV------AELNSKLAELKERIESLER-----IRTLLAAI- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1606 AEIRSRNDALRVKKKmegDLNEMEiqlnhanrlaaeslrnyrntqgilketqlhlddalrgqEDLKEQLAIVERRANLLQ 1685
Cdd:PRK02224 602 ADAEDEIERLREKRE---ALAELN--------------------------------------DERRERLAEKRERKRELE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1686 AEIEElwATLEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLENDVSQLQSEVEEViqesrnaeekakkaitda 1765
Cdd:PRK02224 641 AEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREE-------RDDLQAEIGAVENELEEL------------------ 693
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 153945790 1766 ammaEELKKEQDTsahlermkknLEQTVKDLQHRLDEAEQL 1806
Cdd:PRK02224 694 ----EELRERREA----------LENRVEALEALYDEAEEL 720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1294-1912 |
1.21e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1294 LDEKDalVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQ 1373
Cdd:COG4913 218 LEEPD--TFEAADALVEHFDDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1374 wrTKYETdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMLDVERSNAACAALDKKQR 1450
Cdd:COG4913 288 --RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1451 NFDKVLSEWKQKYEETQAELEASQKESRSLSTELfkvknvyEESLDQLETLRREnknLQQEISDLTEQIAEGGKQIHELE 1530
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEAL-------EEELEALEEALAE---AEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1531 KIKKQVEQEKCEIQAALEEAeASLEHEEgkiLRIQLELNQVKSE--------------------VD-RKIAEKDEEIDQL 1589
Cdd:COG4913 433 RRKSNIPARLLALRDALAEA-LGLDEAE---LPFVGELIEVRPEeerwrgaiervlggfaltllVPpEHYAAALRWVNRL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1590 KRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNH--ANRLA------AESLRNYRntQGILKETQLH-- 1659
Cdd:COG4913 509 HLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKgn 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1660 -----LDDALRGQEDL------KEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQ---------ELLDASERVQLL 1719
Cdd:COG4913 587 gtrheKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1720 HTQNTSLINTKKKLEN---DVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELkkeqdtsahlermkKNLEQTVKDL 1796
Cdd:COG4913 667 EREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--------------EQAEEELDEL 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1797 QHRLDEAEQLALKGgkkQIQKLEARVRELEGE------VENEQKRNAEAVKGLRKHERRVKEL--TYQTE---------- 1858
Cdd:COG4913 733 QDRLEAAEDLARLE---LRALLEERFAAALGDaverelRENLEERIDALRARLNRAEEELERAmrAFNREwpaetadlda 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1859 --EDRKNVLR-LQDLV-DKLQAKVKSYKRQAEEAEEQSNANLSkfRKLQHELEEAEER 1912
Cdd:COG4913 810 dlESLPEYLAlLDRLEeDGLPEYEERFKELLNENSIEFVADLL--SKLRRAIREIKER 865
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1076-1934 |
1.68e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.63 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1076 KQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQK-KIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLE 1154
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1155 EAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMvAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDL 1234
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ-EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1235 SSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQL----SRSKQA 1310
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelkSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1311 STQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQE-----GKAELQRALSKANSEVAQWRTKYETDAIQR 1385
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEelekqELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1386 TEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1466 TQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQA 1545
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1546 ALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDL 1625
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1626 NEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIA 1705
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1706 EQELldaSERVQLLHTQNTSLINTKKKLEndvsqlqSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 1785
Cdd:pfam02463 807 EEEL---KEEAELLEEEQLLIEQEEKIKE-------EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1786 KKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVL 1865
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1866 RLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKI 1934
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1518 |
2.08e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.45 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 843 LKSAETEKEmatmkeefqktkdelakseakRKELEEKMvtllkekNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKI 922
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 923 KEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKAL 1002
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1003 QETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegDLKLAQESTMDMEN--DKQQLD 1080
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKAISARYaeERDRAE 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1081 EKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLE----EA 1156
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEeledEL 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1157 GGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQidnlQRVKQKLEKEKSELKMETDDLSS 1236
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE----RKQRAQAVAAKKKLELDLKELEA 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1237 NAEAISKAKGNLEKMCRSLEDQVSELktkeeeqQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLS-------RSKQ 1309
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDL-------QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQedlaaseRARR 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1310 ASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKY--ETDAIQRTE 1387
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSE 937
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1388 ----ELEEAKKKLAQRLQEAEEHVEA-VNAKCASLEKTKQRLQNEVEdlMLDVERSNAAcaaldKKQRNFDKVLSEWKQK 1462
Cdd:pfam01576 938 sarqQLERQNKELKAKLQEMEGTVKSkFKSSIAALEAKIAQLEEQLE--QESRERQAAN-----KLVRRTEKKLKEVLLQ 1010
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1463 YEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQ 1518
Cdd:pfam01576 1011 VEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1375-1888 |
3.43e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1375 RTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVN-------AKCASLEKTKQRLQ---NEVEDLMLDVERSNAACAA 1444
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselpelrEELEKLEKEVKELEelkEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1445 LDKKQRNFDKVLSEWKQKYEETQaELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGK 1524
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1525 QIHELEKIKKQVEqekcEIQAALEEAEASLEHEEgKILRIQLELNQVKSEV-DRKIAEKDEEIDQLKRNHTRV------V 1597
Cdd:PRK03918 336 KEERLEELKKKLK----ELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIeeeiskI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1598 ETMQSTLDAEIRSRNDALRVKKKMEGD--LNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDA------------ 1663
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLrkelrelekvlk 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1664 ----LRGQEDLKEQLAIVERRANLLQAE-IEELWATLEQT-ERSRKIAEQ--ELLDASERVQLLHTQNTSLINTKKKLEN 1735
Cdd:PRK03918 491 keseLIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLkEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1736 DVSQLQ-----------SEVEEVIQESRNAEEK---AKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLD 1801
Cdd:PRK03918 571 ELAELLkeleelgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1802 EAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDL------VDKLQ 1875
Cdd:PRK03918 648 ELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekalerVEELR 727
|
570
....*....|...
gi 153945790 1876 AKVKSYKRQAEEA 1888
Cdd:PRK03918 728 EKVKKYKALLKER 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1537 |
1.25e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 901 LADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKhateNK 977
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEV----KE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 978 VKNLTEEMAGLDETIAKLSKEKKALQEthqqtldDLQAEEDKVNILTKAKTKLEQQVDDLEgSLEQEKKLRMDLERAKrk 1057
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFY-- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1058 legdlklaqestmdmendkqqldEKLEKKEFEISNLISKIEDEqaveiqlqkkIKELQARIeelgeeieaerasrakaeK 1137
Cdd:PRK03918 303 -----------------------EEYLDELREIEKRLSRLEEE----------INGIEERI------------------K 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1138 QRSDLSRELEEISERLEEaggaTSAQVELNKKREAEFQKLRRDLEEATlqheamvaALRKKHAD-SMAELGEQIDNLQRV 1216
Cdd:PRK03918 332 ELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELE--------RLKKRLTGlTPEKLEKELEELEKA 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1217 KQKLEKE-------KSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQ---------VSELKTKEEEQQRLINDLTAQR 1280
Cdd:PRK03918 400 KEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelleeyTAELKRIEKELKEIEEKERKLR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1281 ARLqteageysRQLDEKDALVSQLSRSKQAStQQIEELKHQLE----EETKAKNALAHALQSS----RHDCDLLREQYEE 1352
Cdd:PRK03918 480 KEL--------RELEKVLKKESELIKLKELA-EQLKELEEKLKkynlEELEKKAEEYEKLKEKliklKGEIKSLKKELEK 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1353 EQE---GKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEakkklaqRLQEAE----EHVEAVNAkcaslEKTKQRLQ 1425
Cdd:PRK03918 551 LEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEE-------RLKELEpfynEYLELKDA-----EKELEREE 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1426 NEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYeetqaeleaSQKESRSLSTELFKVKNVYEESLDQLETLRREN 1505
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY---------SEEEYEELREEYLELSRELAGLRAELEELEKRR 689
|
650 660 670
....*....|....*....|....*....|..
gi 153945790 1506 KNLQQEISDLTEQIAEGGKQIHELEKIKKQVE 1537
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1387-1921 |
2.10e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1387 EELEEAKKKLaQRLQEAEEHVEAVNAKCASLEKTKQRLQ-NEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:COG4913 235 DDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1466 TQAELEASQKESRSLSTELfkvknvYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQA 1545
Cdd:COG4913 314 LEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1546 ALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRV---VETMQSTLDAEIRSRNDALRVKkkme 1622
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAELPFV---- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1623 GDLneMEIQLNHAN-RLAAES-LRNYRNTqgILKETQlHLDDALRgqedlkeqlaIVERRAnlLQAEIeelwatleQTER 1700
Cdd:COG4913 464 GEL--IEVRPEEERwRGAIERvLGGFALT--LLVPPE-HYAAALR----------WVNRLH--LRGRL--------VYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1701 SRKIAEQELLDASERVQLLHtqntslintkkKLENDVSQLQSEVEEVIQES------RNAEE--KAKKAITDAAMMaeel 1772
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEElrRHPRAITRAGQV---- 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1773 kkeqdtsahlermKKNLEQTVKDLQHRLDE--------AEQLALKggKKQIQKLEARVRELEGEVE---------NEQKR 1835
Cdd:COG4913 584 -------------KGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLEaleaeldalQERRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1836 NAEAVKGLRKHERRVKELTY---QTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEER 1912
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
....*....
gi 153945790 1913 ADIAESQVN 1921
Cdd:COG4913 729 LDELQDRLE 737
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
943-1589 |
7.10e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.23 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 943 KRKLEDECSELKKDidDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQE--THQQTLDDLQAEEDKV 1020
Cdd:TIGR00618 195 KAELLTLRSQLLTL--CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEqlKKQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1021 N----ILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISK 1096
Cdd:TIGR00618 273 RaqeaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1097 IEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNK-----KRE 1171
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlahaKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1172 AEFQKLRRDLEEATLQHEAMVAALRKKHADSMAE-LGEQIDNLQRVKQKLEKEK-------------SELKMETDDLSSN 1237
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQsLKEREQQLQTKEQIHLQETrkkavvlarllelQEEPCPLCGSCIH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1238 AEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQA---STQQ 1314
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1315 IEELKHQLEEETKAKNALAhalqssrhdcDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1394
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLA----------CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1395 KLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA-- 1472
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML----AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAre 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1473 -----SQKESRSLSTELFKVK-NVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAA 1546
Cdd:TIGR00618 739 dalnqSLKELMHQARTVLKARtEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 153945790 1547 LEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQL 1589
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL 861
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1040-1933 |
9.76e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.93 E-value: 9.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1040 SLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEiSNLISKIEDEQAVEIQLQKKIKELQARIE 1119
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1120 ELGEEIEaeraSRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREA-EFQKLRRDLEEATLQHEAMVAALRKK 1198
Cdd:TIGR00606 266 KLDNEIK----ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1199 HADSMAELGE-----QIDNLQRVKQKLEKEKSELKMETDDLSSNAE-------AISKAKGNLEKMCRSLEDQVSELKTKE 1266
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFserqiknFHTLVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1267 EEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLL 1346
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1347 REQYeeEQEGKAELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQEAE-EHVEAVNAKCA------SLEK 1419
Cdd:TIGR00606 502 EVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1420 TKQRLQNEVEDLMLDVERSNAACAALDKKQ---RNFDKVLSEWKQKYEETQAELEASQ-------------KESRSLSTE 1483
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQdeesdlerlkeeiEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1484 LFKVKNVYEESLDQL-----------ETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKceiqaalEEAEA 1552
Cdd:TIGR00606 658 LAGATAVYSQFITQLtdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR-------DEMLG 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1553 SLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQL 1632
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1633 NHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWA---TLEQTERSRKIAEQEL 1709
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQL 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1710 LDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESrnaEEKAKKAITDAAMMAEELKK--------EQDTSAH 1781
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDG 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1782 LERMKKNLEQTVKDLQHRLDEAEQlalkgGKKQIQKlEARVRELEGEVENEQKRNAEAVKGLRKHERRVKEL-----TYQ 1856
Cdd:TIGR00606 968 KDDYLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHL 1041
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1857 TEEDRKNVLRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1929
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
....
gi 153945790 1930 VHTK 1933
Cdd:TIGR00606 1122 IYYK 1125
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1387-1929 |
1.23e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 73.61 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1387 EELEEAKKKLAQRLQEAEE-HveavnakcaslEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNElH-----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1466 TQAELEASqkesRSLSTELFKVKNVyeeSLDQLETLRRENKNLQQEISDLTEQIAEG-GKQIHELEKIKK-QVEQEKCEI 1543
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEIRSILVDFEEAsGKKIYEHDSMSTmHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1544 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIaekdeeiDQLKRNHTRVVETMQSTLDAEIRSRND-ALRVKKKME 1622
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI-------ELLLQQHQDRIEQLISEHEVEITGLTEkASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1623 GDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDlkeqlaiverranllqaEIEELwatleqtERSR 1702
Cdd:pfam15921 296 SIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED-----------------KIEEL-------EKQL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1703 KIAEQELLDAservqllhtqntslintkkklendvsqlQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHL 1782
Cdd:pfam15921 352 VLANSELTEA----------------------------RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1783 ERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRK 1862
Cdd:pfam15921 404 WDRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1863 nvlRLQDLVDKLQAK---VKSYKR----------QAEEAEEQSNANLSKFR--------KLQHeLEEAEERADIAESQVN 1921
Cdd:pfam15921 476 ---MLRKVVEELTAKkmtLESSERtvsdltaslqEKERAIEATNAEITKLRsrvdlklqELQH-LKNEGDHLRNVQTECE 551
|
....*...
gi 153945790 1922 KLRVKSRE 1929
Cdd:pfam15921 552 ALKLQMAE 559
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
35-79 |
1.29e-12 |
|
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: 63.60 E-value: 1.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 153945790 35 DAKTSVFVAEPKESYVKSTIQSKEGGKVTVKTEGGATLTVREDQV 79
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1175-1700 |
1.35e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1175 QKLRRDLEEAtlqHEAMVAALRK--------KHADSMAELGEQIDNLQRVKQKLEKEKSELKMETddlssNAEAISKAKG 1246
Cdd:COG4913 231 VEHFDDLERA---HEALEDAREQiellepirELAERYAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1247 NLEKmcrsLEDQVSELKTKEEEQQRLINDLTAQRArlqteageysrqldekdalvsqlsrskQASTQQIEELKHQLEEET 1326
Cdd:COG4913 303 ELAR----LEAELERLEARLDALREELDELEAQIR---------------------------GNGGDRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1327 KAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE---- 1402
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiasl 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1403 -------AEEHVEAVNAKCASLEKTKQRL----------------QNEVE--------DLMLDVERSNAACAALDK---K 1448
Cdd:COG4913 432 errksniPARLLALRDALAEALGLDEAELpfvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1449 QR-NFDKVlsewkqkyEETQAELEASQKESRSLSTELFKVKNVYEESLDQL-------------ETLRRENK-------- 1506
Cdd:COG4913 512 GRlVYERV--------RTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRaitragqv 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1507 ------------------------------NLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEH 1556
Cdd:COG4913 584 kgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1557 EegkilriqlelnqvksEVDRKIAEKDEEIDQLKRNHTrVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHAN 1636
Cdd:COG4913 664 A----------------SAEREIAELEAELERLDASSD-DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1637 RLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRanlLQAEIEELWATLEQTER 1700
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN---LEERIDALRARLNRAEE 787
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1653-1937 |
2.34e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1653 LKETQLHLD--DALRGQedLKEQLAIVERranllQAEIEELWATLEQTERSRKIAEQ--ELLDASERVQLLHTQNTSLIN 1728
Cdd:COG1196 181 LEATEENLErlEDILGE--LERQLEPLER-----QAEKAERYRELKEELKELEAELLllKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1729 TKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlAL 1808
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-EL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1809 KGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEA 1888
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 153945790 1889 EEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1388 |
2.62e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 843 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKM--VTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEA 920
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 921 KIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV-EKEKHATENKVKNLTEemagLDETIAKLSKEK 999
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKeELERLKKRLTGLTPEK----LEKELEELEKAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1000 KALqethqqtlddlqaeEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLK--LAQESTMDM---EN 1074
Cdd:PRK03918 401 EEI--------------EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRkeLLEEYTAELkriEK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1075 DKQQLDEKLEKKEFEISNLISKIEDEQAV--EIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSD-LSRELEEISE 1151
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIkLKGEIKSLKK 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1152 RLEEAGGATSAQVELNKKR---EAEFQKLRRDLEEATLQHEAMVaalrKKHADSMAELGEQIDNLQRVKQKLEKEKSELK 1228
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLdelEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1229 METDDLSSNAEAISKAKGNLEKmcrsLEDQVSELKTK--EEEQQRLINDLTaqrarlqteagEYSRQLDEKDALVSQLSR 1306
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEE----LRKELEELEKKysEEEYEELREEYL-----------ELSRELAGLRAELEELEK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1307 SKQASTQQIEELKHQLEEETKAKNALaHALQSSRHDCDLLREQY-----EEEQEGKAELQRALSKANSEVAQwrTKYETD 1381
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGV 764
|
....*..
gi 153945790 1382 AIQRTEE 1388
Cdd:PRK03918 765 RVKAEEN 771
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1189-1598 |
3.88e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1189 EAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMcrsleDQVSELKTKEEE 1268
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1269 QQRLINDLTAQRARLQTEAGEYsRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEE-TKAKNALAHALQSSRHDCDLLR 1347
Cdd:COG4717 127 LLPLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1348 EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQrtEELEEAK---------------------------------- 1393
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1394 -------KKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQkyEET 1466
Cdd:COG4717 284 gllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1467 QAELEASQKESRSLsteLFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKI--KKQVEQEKCEIQ 1544
Cdd:COG4717 362 ELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1545 AALEEAEASLEHEEGKILRIQLELNQVKSevDRKIAEKDEEIDQLKRNHTRVVE 1598
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAE 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1292-1923 |
6.21e-12 |
|
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: 71.25 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1292 RQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDcdllREQYEEEQEGKAELQ------RALS 1365
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKReyegyeLLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1366 KANSEVAQWRTKYETDAIQRT-EELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQ-RLQNEVEDLMLDVERSNAACA 1443
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEElEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1444 A-------LDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLT 1516
Cdd:TIGR02169 312 EkereledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1517 EQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILriqlELNQVKSEVDRKIAEKDEEIDQLKRnhtrv 1596
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN----ELEEEKEDKALEIKKQEWKLEQLAA----- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1597 vetMQSTLDAEIRSRNDALRvkkKMEGDLNEMEIQLNHANrlaaESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAI 1676
Cdd:TIGR02169 463 ---DLSKYEQELYDLKEEYD---RVEKELSKLQRELAEAE----AQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1677 VERR---------ANLLQA---EIEELWATLEQTERSRKIAEQELL------DASERVQLLHTQNT-----SLINTKKKL 1733
Cdd:TIGR02169 533 VGERyataievaaGNRLNNvvvEDDAVAKEAIELLKRRKAGRATFLplnkmrDERRDLSILSEDGVigfavDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1734 ENDVSQL--QSEVEEVIQESRN-----------------------AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1788
Cdd:TIGR02169 613 EPAFKYVfgDTLVVEDIEAARRlmgkyrmvtlegelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1789 LEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQ 1868
Cdd:TIGR02169 693 LQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1869 DLVDKLQAKVKS-YKRQAEEAEEQSNANLSKFRKlqhELEEAEERADIAESQVNKL 1923
Cdd:TIGR02169 772 EDLHKLEEALNDlEARLSHSRIPEIQAELSKLEE---EVSRIEARLREIEQKLNRL 824
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1181-1817 |
7.49e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.02 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1181 LEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLssnAEAISKAKGNLEKMCRSLEDQVS 1260
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW---KEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1261 ELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHalqssr 1340
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK------ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1341 hdcDLLREQYEEEQEGKAELQRALSKANSEvaqWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKT 1420
Cdd:pfam12128 397 ---DKLAKIREARDRQLAVAEDDLQALESE---LREQLE----AGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1421 KQ------RLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA---------------------- 1472
Cdd:pfam12128 467 ENfderieRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpqagtllhflrkeapd 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1473 -SQKESRSLSTELF---------------KVKNVY-----------EESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ 1525
Cdd:pfam12128 547 wEQSIGKVISPELLhrtdldpevwdgsvgGELNLYgvkldlkridvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1526 iheLEKIKKQVEqekcEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEK-----------DEEIDQLKRNHT 1594
Cdd:pfam12128 627 ---LVQANGELE----KASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkdsanerlnslEAQLKQLDKKHQ 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1595 RVVETMQSTLDAEIRSRNDALRVkkkMEGDLNEMEIQLNHAnrLAAESLRNYRNTQGIlkETQLHLDDALRGqedlkeql 1674
Cdd:pfam12128 700 AWLEEQKEQKREARTEKQAYWQV---VEGALDAQLALLKAA--IAARRSGAKAELKAL--ETWYKRDLASLG-------- 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1675 aIVERRANLLQAEIEELWATLEQTERSRKIAeqelldASERVQLLHT---QNTSLINTKKKLENDVSQLQSEVEEVIQES 1751
Cdd:pfam12128 765 -VDPDVIAKLKREIRTLERKIERIAVRRQEV------LRYFDWYQETwlqRRPRLATQLSNIERAISELQQQLARLIADT 837
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1752 --RNAE-EKAKKAITDAAMMA-EELKKEQDTSAHLERMK--KNLEQTVKDLQHRLDEAEQLALK--GGKKQIQK 1817
Cdd:pfam12128 838 klRRAKlEMERKASEKQQVRLsENLRGLRCEMSKLATLKedANSEQAQGSIGERLAQLEDLKLKrdYLSESVKK 911
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
863-1429 |
8.17e-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: 70.43 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 863 KDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAK 942
Cdd:TIGR04523 88 NDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 943 KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNL---TEEMAGLDETIAKLSKEKKALQETHQQTLDDLQaeeDK 1019
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN---EK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1020 VNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKkefeisNLISKIED 1099
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK------ELKSELKN 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1100 EQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRR 1179
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1180 DLEEATLQHEamvaalrkkhadsmaELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQV 1259
Cdd:TIGR04523 399 KIQNQEKLNQ---------------QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1260 SELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQS- 1338
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDl 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1339 ----SRHDCDLLREQYEEEQEGK-------AELQRALSKANSEVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQEAE 1404
Cdd:TIGR04523 544 edelNKDDFELKKENLEKEIDEKnkeieelKQTQKSLKKKQEEKQELIDQKEKekkDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580
....*....|....*....|....*
gi 153945790 1405 EHVEAVNAKCASLEKTKQRLQNEVE 1429
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1750 |
1.06e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 70.46 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 850 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKnDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERA 929
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 930 EEEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDETIAKLSKEKKALQETH--- 1006
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1007 --QQTLDDLQAEEDKVNILTKAKTKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLD 1080
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1081 EKLEKKEFEISNLISKIEDEQAVeiqLQKKIKELQARIEELGEEIeaerASRAKAEKQRSDLSRELEEISeRLEEaggat 1160
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQQLE----GSSDRILELDQELRKAERELS-KAEK----- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1161 SAQVELNKKREAEFQKLRRDLEEAtlqheamvaalRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEA 1240
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRK-----------LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1241 ISKAKGNLEKMcRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSR------SKQASTQQ 1314
Cdd:TIGR00606 562 LTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1315 IEELKHQLEEETKAKNALAHALQssrhdcdlLREQYEEEQEGKaelqralSKANSEVAQwrtkyetDAIQRTEELEEAKK 1394
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1395 KLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELE--- 1471
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtim 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1472 ASQKESRSLSTELFKVKNVYEEsldqletLRRENKNLQQEISDLteQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAE 1551
Cdd:TIGR00606 779 PEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1552 ASLEHEEGKILRIQLELNQVKSEvDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQ 1631
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1632 LNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKeqlaivERRANLLQAEIEELWATLEQTERSRKIAEQELLD 1711
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRL 1002
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 153945790 1712 ASERVQLLHTQNTSLIN--TKKKLENDVSQLQSEVEEVIQE 1750
Cdd:TIGR00606 1003 MRQDIDTQKIQERWLQDnlTLRKRENELKEVEEELKQHLKE 1043
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
850-1330 |
2.05e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 69.28 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 850 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEkndlqlqVQSEADSLADAEERCEQLIKNKIQLE---------- 919
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELEnelnllekek 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 920 -------AKIKEVTERAEEEEEINAELTAKKRKLEDECSELKK--------------DIDDLELTLAKVE---------- 968
Cdd:TIGR04523 183 lniqkniDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKqnnqlkdniekkqqEINEKTTEISNTQtqlnqlkdeq 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 969 -----------KEKHATENKVKNLTEEMAGLDETIAKLSKEKKalQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDL 1037
Cdd:TIGR04523 263 nkikkqlsekqKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1038 EGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQAR 1117
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1118 IEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQ---HEAMVAA 1194
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElksKEKELKK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1195 LRKKHADS---MAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNaeaISKAKGNLEKmcRSLEDQVSELKTKEEEQQR 1271
Cdd:TIGR04523 501 LNEEKKELeekVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE---LNKDDFELKK--ENLEKEIDEKNKEIEELKQ 575
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1272 LINDLTAQRARLQTEAGEYSrqlDEKDALVSQLSrskqASTQQIEELKHQLeEETKAKN 1330
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKE---KEKKDLIKEIE----EKEKKISSLEKEL-EKAKKEN 626
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
834-1507 |
2.31e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 69.31 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 834 KLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSE--AKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAE------ 905
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 906 ERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 978
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 979 KNLTEEMAGLDETI------AKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLE 1052
Cdd:TIGR00606 615 ESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1053 RAKRKLEGDLKLAqestmdmENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASR 1132
Cdd:TIGR00606 695 EFISDLQSKLRLA-------PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1133 AKAEKQRSDLSRELEEISERLEEAGGATSAQVELnKKREAEFQKLRRDLEEATLqhEAMVAALRKKHADSMAEL---GEQ 1209
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdtvVSK 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1210 IDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEdqvselkTKEEEQQRLINDLTAQRARLQTEAGE 1289
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-------ELSTEVQSLIREIKDAKEQDSPLETF 917
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1290 YSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSrhdCDLLREQYEEEQEGKA----ELQRALS 1365
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLKQKETELNTVNaqleECEKHQE 994
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1366 KANSEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQEAEEhveavnAKCASLEKTKQRLQNEVEDLML 1433
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLIKR 1068
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1434 DVERSNAACAALDKKQRNFDKVLSEWK-QKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKN 1507
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
943-1567 |
2.44e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 943 KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDETIAKLSKEKKALQ-ETHQQTLDDLQAEEDK 1019
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1020 vniLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqestMDMENDKQQLDEKLEKKEFEISNLISKIED 1099
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1100 ----EQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLeeaggatsAQVELNKKR-EAEF 1174
Cdd:COG4913 371 lglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI--------ASLERRKSNiPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1175 QKLRRDLEEATLQHE---------------------AMVAALR---------KKHADSMAELGEQIDNLQRVK-QKLEKE 1223
Cdd:COG4913 443 LALRDALAEALGLDEaelpfvgelievrpeeerwrgAIERVLGgfaltllvpPEHYAAALRWVNRLHLRGRLVyERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1224 KSELKMETDDLSSNAE----AISKAKGNLEKM---------CRSLED------------QVSELKTKEEEQ--------- 1269
Cdd:COG4913 523 LPDPERPRLDPDSLAGkldfKPHPFRAWLEAElgrrfdyvcVDSPEElrrhpraitragQVKGNGTRHEKDdrrrirsry 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1270 ------QRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQ----------------QIEELKHQLEEETK 1327
Cdd:COG4913 603 vlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaerEIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1328 AKNALAhALQSSRHDCDLLREQYEEEqegKAELQRALSKANSEVAQWRTkyETDAIQRTEELEEAKKKLAQRlQEAEEHV 1407
Cdd:COG4913 683 SSDDLA-ALEEQLEELEAELEELEEE---LDELKGEIGRLEKELEQAEE--ELDELQDRLEAAEDLARLELR-ALLEERF 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1408 EAVNAKcASLEKTKQRLQNEVEDLMldversnaacAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSlstelfkv 1487
Cdd:COG4913 756 AAALGD-AVERELRENLEERIDALR----------ARLNRAEEELERAMRAFNREWPAETADLDADLESLPE-------- 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1488 knvYEESLDQLET----------LRRENKNLQQEISDLTEQIAEggkqihELEKIKKQVEqekcEIQAALEEaeasLEHE 1557
Cdd:COG4913 817 ---YLALLDRLEEdglpeyeerfKELLNENSIEFVADLLSKLRR------AIREIKERID----PLNDSLKR----IPFG 879
|
730
....*....|
gi 153945790 1558 EGKILRIQLE 1567
Cdd:COG4913 880 PGRYLRLEAR 889
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1007-1427 |
3.77e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1007 QQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESTMDMENDKQQLdEKLEKK 1086
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERL-EELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1087 EFEISNLISKIEDEQAVEIQLQKKIKEL--------QARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGG 1158
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1159 ATSAQVELNKKREAE-----------FQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSEL 1227
Cdd:COG4717 235 ELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1228 KMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRS 1307
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1308 KQAS--TQQIEELKHQLEEETKAKNALAHAlqssrHDCDLLREQYEEEQEGKAELQRALSKANSEVAqwRTKYETDAIQR 1385
Cdd:COG4717 395 EEYQelKEELEELEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 153945790 1386 TEELEEAKKKLAQRLQEAEEHVEAVNAKCAS---LEKTKQRLQNE 1427
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAALKLAlelLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1144-1624 |
4.67e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1144 RELEEISERLEEAggatSAQVELNKKREAEFQKLRRDLEEATLQhEAMVAALRKKHA-DSMAELGEQIDNLQRVKQKLEK 1222
Cdd:COG4913 235 DDLERAHEALEDA----REQIELLEPIRELAERYAAARERLAEL-EYLRAALRLWFAqRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1223 EKSELKMETDDLSSNAEAISKA--------KGNLEKMCRSLEDQVSELKTKEEEQQRLINDL-----------TAQRARL 1283
Cdd:COG4913 310 ELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1284 QTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLE-----------EETKAKNALAHALQSSRHD----CDLLRE 1348
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrksnipaRLLALRDALAEALGLDEAElpfvGELIEV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1349 QYEEEQ-EGKAE----------------LQRALSKANS----------EVAQWRTKYETDAIQR---TEELE----EAKK 1394
Cdd:COG4913 470 RPEEERwRGAIErvlggfaltllvppehYAAALRWVNRlhlrgrlvyeRVRTGLPDPERPRLDPdslAGKLDfkphPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1395 KLAQRLQEAEEHVeavnaKCASLEKTKQ-----------------------------------------RLQNEVEDLML 1433
Cdd:COG4913 550 WLEAELGRRFDYV-----CVDSPEELRRhpraitragqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1434 DVERSNAACAALDKKQRNFDKVLSEWK--QKYEETQAELEASQKESRSLSTELFKVknvyEESLDQLETLRRENKNLQQE 1511
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1512 ISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKR 1591
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 153945790 1592 NH----TRVVETMQ----------STLDAEIRSRNDALRVKKKMEGD 1624
Cdd:COG4913 781 RLnraeEELERAMRafnrewpaetADLDADLESLPEYLALLDRLEED 827
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1447-1937 |
4.93e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1447 KKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVY---EESLDQLETLRRENKNLQQEISDLTEQIAEGG 1523
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1524 KQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKIlriqlELNQVKSEVDRKIAEKDEEIDQLKRnhtrvvetmqst 1603
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-----EYLDELREIEKRLSRLEEEINGIEE------------ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1604 ldaEIRSRNDALRVKKKMEGDLNEMEIQLNHANrlaaESLRNYRNTQGILKETQ-LHLDDALRGQEDLKEQLAIVERRAN 1682
Cdd:PRK03918 329 ---RIKELEEKEERLEELKKKLKELEKRLEELE----ERHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1683 LLQAEIEELW---ATLEQTERSRKIAEQELLDASERVQLLHTQNTSliNTKKKLENDVSQLQSEVEEVIQESRNAEEKAK 1759
Cdd:PRK03918 402 EIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1760 KAitdaammAEELKKEQDTSAHLERMKKNLEQtVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENeQKRNAEA 1839
Cdd:PRK03918 480 KE-------LRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1840 VKGLRKHERRVKELTYQTEEDRKNVLR---------LQDLVDKLQAKVKSYKR--QAEEAEEQSNANLSKFRKLQHELEE 1908
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDK 630
|
490 500
....*....|....*....|....*....
gi 153945790 1909 AEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1427 |
5.41e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 844 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 924 EvteraeeeeeinaeltakkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQ 1003
Cdd:PRK02224 311 A---------------------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1004 ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDD----LEGSLEQEKKLRMDLERAKRK---LEGDLKLAQESTmdmeNDK 1076
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREReaeLEATLRTARERV----EEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1077 QQLDEKLEKKEFEisnliSKIEDEQAVEiqlqkkikelqarieelgeEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1156
Cdd:PRK02224 446 EALLEAGKCPECG-----QPVEGSPHVE-------------------TIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1157 GGATSAQVELNKKREAefqklRRDLEEATLQHEAMVAALRKKhadsMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSS 1236
Cdd:PRK02224 502 EDLVEAEDRIERLEER-----REDLEELIAERRETIEEKRER----AEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1237 NAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRlINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQAStqQIE 1316
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIADAEDE-IERLREKREALAELNDERRERLAEKRERKRELEAEFDEA--RIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1317 ELKhqlEEETKAKNALAHAlqssrhdcdllREQYEEEQEGKAELQRALSKANSEvaqwrtkyetdaIQRTEELEEAKKKL 1396
Cdd:PRK02224 650 EAR---EDKERAEEYLEQV-----------EEKLDELREERDDLQAEIGAVENE------------LEELEELRERREAL 703
|
570 580 590
....*....|....*....|....*....|.
gi 153945790 1397 AQRLqeaeEHVEAVNAKCASLEKTKQRLQNE 1427
Cdd:PRK02224 704 ENRV----EALEALYDEAEELESMYGDLRAE 730
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
849-1539 |
6.29e-11 |
|
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: 67.69 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 849 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMV--TLLKEKNDLQLQVQSEADSLADAEERCEQLIKnKIQLEAKIKEVT 926
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLKQLRARIEELRAQEAVLEETQERINRARK-AAPLAAHIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 927 ERAEEEEEINAELTAKKRKLEDE---CSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEtiaKLSKEKKALQ 1003
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIRE---ISCQQHTLTQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1004 ETHQQTlDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKL 1083
Cdd:TIGR00618 380 HIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1084 EKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERasraKAEKQRSDLSRELEEISERleeagGATSAQ 1163
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC----PLCGSCIHPNPARQDIDNP-----GPLTRR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1164 VELNKKREAEFQKlrrdlEEATLQHEamVAALRKKhadsMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISK 1243
Cdd:TIGR00618 530 MQRGEQTYAQLET-----SEEDVYHQ--LTSERKQ----RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1244 AKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLE 1323
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1324 EetkaknALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRLQEA 1403
Cdd:TIGR00618 679 Q------LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSS----LGSDLAAREDALNQSLKEL 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1404 EEhvEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcAALDKKQRNFDKVLSEWKQKYEETQAELEASQKEsRSLSTE 1483
Cdd:TIGR00618 749 MH--QARTVLKARTEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI-LNLQCE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1484 LFkvknvyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQE 1539
Cdd:TIGR00618 825 TL------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1081-1734 |
7.48e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.44 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1081 EKLEKKEFEISNLISKIEDEQAVEIQLQKKIK-ELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGA 1159
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKvSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1160 TSAQVELNKKREAEFQKLRRDLE---EATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMEtddLSS 1236
Cdd:pfam05483 143 NKDLIKENNATRHLCNLLKETCArsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1237 NAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAqrarLQTEAGEYSRQLDEKDALVS----QLSRSKQAST 1312
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1313 QQIEELKHQLEEETKAKNALAHALQ-SSRHDCDLLRE---QYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEE 1388
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQiATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1389 LEEAKKKLAQRLQ----EAEEHVEAVNAKCASLEKTKQRLqNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYE 1464
Cdd:pfam05483 375 NEDQLKIITMELQkkssELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1465 ETQAELEASQ-------KESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLT-------EQIAEGGKQIHELE 1530
Cdd:pfam05483 454 DLEIQLTAIKtseehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTlelkkhqEDIINCKKQEERML 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1531 KIKKQVEQEKCEIQAALEEAEASL--EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEI 1608
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1609 RSRNDALRVKKKMEG--------DLNEMEIQLNHANRLAAESLRNYR-----------NTQGILKETQLHLDDA------ 1663
Cdd:pfam05483 614 HQENKALKKKGSAENkqlnayeiKVNKLELELASAKQKFEEIIDNYQkeiedkkiseeKLLEEVEKAKAIADEAvklqke 693
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1664 --LRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKiaEQELLDASERVQLLHTQNtSLINTKKKLE 1734
Cdd:pfam05483 694 idKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQ--EQSSAKAALEIELSNIKA-ELLSLKKQLE 763
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1274 |
7.58e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 838 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 918 LEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatENKVKnlTEEMAGLDETIAKLSK 997
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDK- 1076
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKk 1758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1077 -QQLDEKLEKKEFEIsnlisKIEDEQAVEIQLQKKikelqarieelgeeieaERASRAKAEKQRSDLSRELEEISERLEE 1155
Cdd:PTZ00121 1759 iAHLKKEEEKKAEEI-----RKEKEAVIEEELDEE-----------------DEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1156 AGGATSAQVEL---NKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETD 1232
Cdd:PTZ00121 1817 GNLVINDSKEMedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 153945790 1233 DLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLIN 1274
Cdd:PTZ00121 1897 DIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1298-1937 |
7.84e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 7.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1298 DALVSQLSRSKQASTQQIEELKHQLEEETKAkNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrtK 1377
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKA-EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK---K 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1378 YETDAIQRTEELEEAKKKL--------AQRLQEAEEHVEAVNAKCASLEKTKQRLQN----EVEDLMLDVERSNAACAAL 1445
Cdd:PTZ00121 1106 TETGKAEEARKAEEAKKKAedarkaeeARKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1446 DKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTE--LFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGG 1523
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1524 KQIH---ELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETM 1600
Cdd:PTZ00121 1266 ARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1601 QSTLDAEIRSRNDALRVKKKMEGDLNEMEiqlnhANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAiVERR 1680
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKE-----EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA-AKKK 1419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1681 ANLLQAEIEELwatlEQTERSRKIAEQEllDASERVQLLHTQNTSLINTKKKLENdvSQLQSEVEEVIQESRNAEEKAKK 1760
Cdd:PTZ00121 1420 ADEAKKKAEEK----KKADEAKKKAEEA--KKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKK 1491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1761 A-----ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEaRVRELEGEVENEQKR 1835
Cdd:PTZ00121 1492 AeeakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAK 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1836 NAEAVKGLRkhERRVKELTYQTEEDRKNVLRLQDLVDKLQA----KVKSYKRQAEE---AEEQSNANLSKFRKLQHELEE 1908
Cdd:PTZ00121 1571 KAEEDKNMA--LRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670
....*....|....*....|....*....|
gi 153945790 1909 AEE-RADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:PTZ00121 1649 AEElKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1282 |
1.25e-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: 65.56 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1065 AQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSR 1144
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1145 ELEEISERLEE-------AGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKhadsMAELGEQIDNLQRVK 1217
Cdd:COG4942 98 ELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1218 QKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAR 1282
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1492-1914 |
2.30e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1492 EESLDQLETL--RRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEheegkilriqlELN 1569
Cdd:PRK02224 186 RGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1570 QVKSEVDrKIAEKDEEIDQLKRNHTRVVETMQSTLDaEIRSRNDALRVKKKMEG----DLNEMEIQLNHANRLAAESLRN 1645
Cdd:PRK02224 255 TLEAEIE-DLRETIAETEREREELAEEVRDLRERLE-ELEEERDDLLAEAGLDDadaeAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1646 YRNTQGILKETQlhldDALRGQ-EDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNT 1724
Cdd:PRK02224 333 CRVAAQAHNEEA----ESLREDaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1725 SLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAIT--------------DAAMMAEELKKEQDTSAHLERMKKNLE 1790
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1791 QTVKDLQHRLDEAEQLAlkggkkqiqKLEARVRELEGEVENEQKRNAEavkglrKHERrvkeltyqTEEDRKNVLRLQDL 1870
Cdd:PRK02224 489 EEVEEVEERLERAEDLV---------EAEDRIERLEERREDLEELIAE------RRET--------IEEKRERAEELRER 545
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 153945790 1871 VDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
941-1536 |
2.54e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 65.69 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 941 AKKRKLEDECSELKKdIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKV 1020
Cdd:PRK01156 149 AQRKKILDEILEINS-LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1021 NILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEIS---NLISKI 1097
Cdd:PRK01156 228 NNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINdyfKYKNDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1098 EDEQAVEIQLQKKIKELQArIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEfqkl 1177
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHA-IIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY---- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1178 rrdleeatlqheamvaalRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLED 1257
Cdd:PRK01156 383 ------------------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1258 QVSELKTK-----------EEEQQRLINDLTAQRARLQTEAGEYSRQ---LDEK--------DALVSQLSRSKQASTQQI 1315
Cdd:PRK01156 445 NMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEvkdIDEKivdlkkrkEYLESEEINKSINEYNKI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1316 EELKHQLEEETKAKNALAHAlqssrHD-CDLLREQYEEEQEGKAELQR-ALSKANSEvaqwRTKYETDAIQ-RTEELEEA 1392
Cdd:PRK01156 525 ESARADLEDIKIKINELKDK-----HDkYEEIKNRYKSLKLEDLDSKRtSWLNALAV----ISLIDIETNRsRSNEIKKQ 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1393 KKKLAQRLQEAEEHVEAVNAkcaSLEKTKQRLQNEVEDL---MLDVERSNAACAALDKKQRNFDKVLSEwKQKYEETQAE 1469
Cdd:PRK01156 596 LNDLESRLQEIEIGFPDDKS---YIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKE 671
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1470 LEASQKESrslSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQV 1536
Cdd:PRK01156 672 ITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1311 |
3.09e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1065 AQESTMDMENDKQQLDEKLEkkefEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSR 1144
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1145 ELEEISERLEEaggatsaqvelnkkREAEFQKLRRDLEEATLQHEAMVAAlrkkHADSMAELGEQIDNLQRVKQKLEKEK 1224
Cdd:COG4942 91 EIAELRAELEA--------------QKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1225 SELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQL 1304
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*..
gi 153945790 1305 SRSKQAS 1311
Cdd:COG4942 233 EAEAAAA 239
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
847-1662 |
3.90e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.45 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 847 ETEKEMATMKEEFQKTKDELAKSEAKRK-------ELEEKMVTLL----KEKNDLQLQVQSEADSLADAEERCEQLIKnK 915
Cdd:TIGR00606 252 NRLKEIEHNLSKIMKLDNEIKALKSRKKqmekdnsELELKMEKVFqgtdEQLNDLYHNHQRTVREKERELVDCQRELE-K 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 916 IQLEAKIKEVTERAEEEEEINAELTA-------KKRKLEDECSELKKDIDDLE--------------LTLAKVEKEKHAT 974
Cdd:TIGR00606 331 LNKERRLLNQEKTELLVEQGRLQLQAdrhqehiRARDSLIQSLATRLELDGFErgpfserqiknfhtLVIERQEDEAKTA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 975 ENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERA 1054
Cdd:TIGR00606 411 AQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1055 KRKLEGDLKLAQEstMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKK------IKELQARIEELGEEIEAE 1128
Cdd:TIGR00606 491 EKNSLTETLKKEV--KSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKmdkdeqIRKIKSRHSDELTSLLGY 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1129 RASRAKAEKQRSDLSRELEEISERLeeaggatsAQVELNKKREAEFQKLRRDLEEatlQHEAMVAALRKKHADSMAELGE 1208
Cdd:TIGR00606 569 FPNKKQLEDWLHSKSKEINQTRDRL--------AKLNKELASLEQNKNHINNELE---SKEEQLSSYEDKLFDVCGSQDE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1209 QIDnLQRVKQKLEKEKSELKM-------------ETDDLSSN----AEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQR 1271
Cdd:TIGR00606 638 ESD-LERLKEEIEKSSKQRAMlagatavysqfitQLTDENQSccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTES 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1272 LINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSR---HDCDLLRE 1348
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvclTDVTIMER 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1349 QYEEEQEGKAELQRALSKANSeVAQWRTKYETDaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEV 1428
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQG-SDLDRTVQQVN--QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1429 EDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNL 1508
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1509 QQEISDLTEQIAEGgkqiheLEKIKKQVEQEKCEIQAALEEAEASLE----------------HEEGKILRIQLELNQVK 1572
Cdd:TIGR00606 954 HGYMKDIENKIQDG------KDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmrqdidtqKIQERWLQDNLTLRKRE 1027
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1573 S---EVDRKIAEKDEEIDQLKRNHTR-VVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESlrNYRN 1648
Cdd:TIGR00606 1028 NelkEVEEELKQHLKEMGQMQVLQMKqEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYRE 1105
|
890
....*....|....
gi 153945790 1649 TQGILKETQLHLDD 1662
Cdd:TIGR00606 1106 MMIVMRTTELVNKD 1119
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1010-1521 |
3.90e-10 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.21 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1010 LDDLQAEEDKVNILTKAKtkLEQQVDDLEGSLEQEKKLRMDLERAKRKLegdLKLAQESTMDMENDK-----QQLDEKLE 1084
Cdd:PRK10246 200 LEKLQAQASGVALLTPEQ--VQSLTASLQVLTDEEKQLLTAQQQQQQSL---NWLTRLDELQQEASRrqqalQQALAAEE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1085 KKEFEISNLI------------SKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASrakAEKQRSDLSRELEEISER 1152
Cdd:PRK10246 275 KAQPQLAALSlaqparqlrphwERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHH---AAKQSAELQAQQQSLNTW 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1153 LEEAGGATSAQVELNKKReAEFQKLRRDLEEATLQHEAMVAALRKKHA----------DSMAELGEQIDNLQRVKQKLEK 1222
Cdd:PRK10246 352 LAEHDRFRQWNNELAGWR-AQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltaDEVAAALAQHAEQRPLRQRLVA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1223 EKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEE---------EQQRLINDLTAQRARLQT-------- 1285
Cdd:PRK10246 431 LHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcg 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1286 -------------EAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQL-----------EEE---TKAKNALAHALQS 1338
Cdd:PRK10246 511 stshpaveayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLqrdeseaqslrQEEqalTQQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1339 SRHDCD----LLREQYEEEQE-----GKAELQRALSKANSEVAQWRTKYETDAIQRTEELEE----------------AK 1393
Cdd:PRK10246 591 TLQPQDdiqpWLDAQEEHERQlrllsQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1394 KKLAQRLQEAEEHVEAVNAKCASLEKTKQRL------QNEVEDLMLDVERS-NAACAALDKKQRNFDKVLSEWKQKYEET 1466
Cdd:PRK10246 671 QQEAQSWQQRQNELTALQNRIQQLTPLLETLpqsddlPHSEETVALDNWRQvHEQCLSLHSQLQTLQQQDVLEAQRLQKA 750
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1467 QAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAE 1521
Cdd:PRK10246 751 QAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQ 805
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1074-1299 |
3.92e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1074 NDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERL 1153
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1154 EEaggatsaQVELNKKREAEFQKL-RRDLEEATLQHEAMVAALRKKH--ADSMAELGEQIDNLQRVKQKLEKEKSELKME 1230
Cdd:COG4942 100 EA-------QKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1231 TDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDA 1299
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
850-1258 |
4.37e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 850 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDL--QLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTE 927
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 928 RAEEEEEINAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLS 996
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 997 KEKKALQE-----------THQQTLDDLQAEEDKV---------------NILTKAKTKLEQQVDDLEGSLEQEKKLRMD 1050
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1051 LERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEfeisnliskiedEQAVEIQLQKKIKELQARIEELGEEIEAERA 1130
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE------------ELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1131 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKR--EAEFQKLRRDLEEATLQHEAMVAALRKKHADsMAELGE 1208
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELAELEAE-LEQLEE 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 153945790 1209 QiDNLQRVKQKLEKEKSELKMETDDlssnAEAISKAKGNLEKMCRSLEDQ 1258
Cdd:COG4717 468 D-GELAELLQELEELKAELRELAEE----WAALKLALELLEEAREEYREE 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1518 |
4.43e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 838 KIKPLLKSAETEKEMATMKEEFQKTKDElaksEAKRKELEEKMVTLLKEKNDlqlQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAE---EDKKKADELKKAAAAKKKADEAKKK 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 918 LEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLSK 997
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQTLDDLQAEEDKvniltkaKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQEstMDMENDKQ 1077
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--LKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1078 QLDEKleKKEFEISNLISKIEDEQAveiQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAg 1157
Cdd:PTZ00121 1565 KAEEA--KKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL- 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1158 gatsAQVELNKKREAEfqKLRRDLEEATLQHEamvaalrkkhadsmaelgeqidNLQRVKQKLEKEKSELKMETDDLSSN 1237
Cdd:PTZ00121 1639 ----KKKEAEEKKKAE--ELKKAEEENKIKAA----------------------EEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1238 AEAISKAKGNLEKmcrsledqVSELKTKEEEQQRlindltaqrarlqtEAGEYSRQLDEKDALVSQLSRSKQASTQQIEE 1317
Cdd:PTZ00121 1691 AEALKKEAEEAKK--------AEELKKKEAEEKK--------------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1318 LKHQLEEETK----AKNALAHALQSSRHDCDLLREQYEEEQEG-KAELQRAL--SKANSEVAQWRTKYETDAIQRTEELE 1390
Cdd:PTZ00121 1749 AKKDEEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEME 1828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1391 EAKKKlaqrlqeaeehvEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNaacaaldkKQRNFDK---VLSEWKQKYEETQ 1467
Cdd:PTZ00121 1829 DSAIK------------EVADSKNMQLEEADAFEKHKFNKNNENGEDGN--------KEADFNKekdLKEDDEEEIEEAD 1888
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1468 AELEASQKE-SRSLSTELFKVKN--VYEESLDQLETLRRENKNLQQEISDLTEQ 1518
Cdd:PTZ00121 1889 EIEKIDKDDiEREIPNNNMAGKNndIIDDKLDKDEYIKRDAEETREEIIKISKK 1942
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
859-1515 |
6.58e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.47 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 859 FQKTKDELAKSEAK---RKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIknkIQLEAKIKEVTERAEEEEEI 935
Cdd:pfam12128 236 IMKIRPEFTKLQQEfntLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL---RTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 936 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEMagldetiaklSKEKKALQETHQQTLDDLQA 1015
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ---LPSWQSELENL----------EERLKALTGKHQDVTAKYNR 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1016 EEDKVNiltkaktklEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlAQESTMDMENDKQQLDEKLEKKEFE--ISNL 1093
Cdd:pfam12128 380 RRSKIK---------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1094 ISKIEDEQAV-EIQLQKKIKelQARIEELGEEIEAERASR-------AKAEKQRSDLSRELEEISERLEEAGGATSAQVE 1165
Cdd:pfam12128 450 KLRLNQATATpELLLQLENF--DERIERAREEQEAANAEVerlqselRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1166 ------------LNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRV--------KQKLEKEKS 1225
Cdd:pfam12128 528 qlfpqagtllhfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIdvpewaasEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1226 ELKMETDDLSSNAEAISK----AKGNLEKMCRSLEDQVSELKTKEEEQQRLINDltaqrarlqteageysrQLDEKDALV 1301
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEqlvqANGELEKASREETFARTALKNARLDLRRLFDE-----------------KQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1302 SQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETD 1381
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1382 AIQrteelEEAKKKLAQRLQEaeehveavnakcaslEKTKQRLQNEVEDLMLDVERsnaaCAALDKKQRNFDKVLSE-WK 1460
Cdd:pfam12128 751 ALE-----TWYKRDLASLGVD---------------PDVIAKLKREIRTLERKIER----IAVRRQEVLRYFDWYQEtWL 806
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1461 QKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDL 1515
Cdd:pfam12128 807 QRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1214-1836 |
1.29e-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: 63.50 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1214 QRVKQKLEKEKSELK---METDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLqteAGEY 1290
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI---NSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1291 SRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAhalqSSRHDCDLLREQYEEEQEGKAELQRALSKANSE 1370
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1371 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQR 1450
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1451 NFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLD-----QLETLRRENKNLQQEISDLTEQIAEGGKQ 1525
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1526 IHELEKIKKQVEQEKCEIQAALEEAEASLEHE----EGKILRIQlELNQVKSEVDRKIaEKDEEIDQLKRNHTRVVETMQ 1601
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIK-NLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1602 STLDAEIRSRNDALRVKKKMEGDLNEMEIQLNhanrLAAESLRNYRntqgilketqlhlddalrgqEDLKEQLAIVERra 1681
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKE----LIIKNLDNTR--------------------ESLETQLKVLSR-- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1682 nllqaEIEELWATLEQTERSRKIAEQELLDaservqlLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKA 1761
Cdd:TIGR04523 476 -----SINKIKQNLEQKQKELKSKEKELKK-------LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1762 ITDAAMMAEELKKE---------QDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENE 1832
Cdd:TIGR04523 544 EDELNKDDFELKKEnlekeidekNKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKKDLIKEIEEKEKKISSLEKELEKA 622
|
....
gi 153945790 1833 QKRN 1836
Cdd:TIGR04523 623 KKEN 626
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
994-1629 |
1.37e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.20 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 994 KLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKlrmdlerAKRKLEGDLKLAQESTMDME 1073
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRD-------KANQLEEKTKLQDENLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1074 NDKQQLDEKLEKKEFEISNLISKiedEQAVEIQLQKKIKElqarIEELGEEIEAERASRAKAEKQRSDLSRELEEISERL 1153
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMST---QKALEEDLQIATKT----ICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1154 EEAGGATSAQVELNkkrEAEFQKLRRDLEEATLQHEAMVAALRKKHADSmaelgEQIDNLQRVKQKLEKEKSELKMETDD 1233
Cdd:pfam05483 362 EELLRTEQQRLEKN---EDQLKIITMELQKKSSELEEMTKFKNNKEVEL-----EELKKILAEDEKLLDEKKQFEKIAEE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1234 LSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLtaqRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQ 1313
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL---KTELEKEKLKNIELTAHCDKLLLENKELTQEASD 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1314 QIEELKHQLEEETKAKNALAHALQssrhdcdllreQYEEEQEGKAELQRALSKANsevaqwrtkyetdaiqrtEELEEAK 1393
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLK-----------QIENLEEKEMNLRDELESVR------------------EEFIQKG 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1394 KKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNaacaaldkkqrnfdkvlsewkQKYEETQAELEAS 1473
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKN---------------------KNIEELHQENKAL 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1474 QKESRSLSTELfkvkNVYEESLDQLETLRRENKNLQQEISDLTEQIAEgGKQIHElEKIKKQVEQEKCEIQAALEEAEAS 1553
Cdd:pfam05483 621 KKKGSAENKQL----NAYEIKVNKLELELASAKQKFEEIIDNYQKEIE-DKKISE-EKLLEEVEKAKAIADEAVKLQKEI 694
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1554 LEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDqLKRNHTRVVETMQSTLDAEIRS-RNDALRVKKKMEGDLNEME 1629
Cdd:pfam05483 695 DKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKE 770
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1076-1540 |
1.49e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1076 KQQLDEkLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEE--LGEEIEAERASRAKAEKQRSDLSRELEEISERL 1153
Cdd:COG4717 77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1154 EEaggaTSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDD 1233
Cdd:COG4717 156 EE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1234 LSSNAEAISKAKgnlekmcrsledqvselktKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDAL----------VSQ 1303
Cdd:COG4717 232 LENELEAAALEE-------------------RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1304 LSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAI 1383
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1384 QrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcaaldkkqrnfdkvlsEWKQKY 1463
Cdd:COG4717 373 A--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE----------------ELEEEL 434
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1464 EETQAELEASQKESRSLSTELFKVKNVYE--ESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEK 1540
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1470-1917 |
1.51e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1470 LEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEe 1549
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1550 aeasleheegkilriQLELNQVKSEVDRKIAEKDEEIDQLKRnhtrvvetmqstldaEIRSRNDALRVKKKMEGDLNEME 1629
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1630 IQLNHANRLAAESLRNYrntqgiLKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQEL 1709
Cdd:COG4717 177 EELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1710 LDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKK 1787
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1788 NLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRN-----------AEAVKGLRKHERRVKELTYQ 1856
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvedeeelraaLEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1857 TEEDRKNVLRLQDLVDK--LQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAE 1917
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
949-1521 |
1.75e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.82 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 949 ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKT 1028
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1029 KL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLiSKIEDEQAVE 1104
Cdd:pfam05483 328 QLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1105 IQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKreaEFQKLRRDLEEA 1184
Cdd:pfam05483 407 LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK---EVEDLKTELEKE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1185 TLQHeamvaalrkkhadsmAELGEQIDNLQRVKQKLEKEKSELKMEtddLSSNAEAISKAKGNLEKMCRSLEdqvselkT 1264
Cdd:pfam05483 484 KLKN---------------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKKQEERMLKQIE-------N 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1265 KEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCD 1344
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1345 LLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRL 1424
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1425 QNEVEDLMldversnaacAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRE 1504
Cdd:pfam05483 699 QHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
570
....*....|....*..
gi 153945790 1505 NKNLQQEISDLTEQIAE 1521
Cdd:pfam05483 769 KEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1106-1340 |
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 153945790 1106 QLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRRDLEEAT 1185
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1186 LQheamVAALRKKHADSMAELGEQIDNLQRVKQKLE-------KEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQ 1258
Cdd:COG4942 90 KE----IAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1259 VSELKTKEEEQQRLINDLTAQRARLQteageysRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQS 1338
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
..
gi 153945790 1339 SR 1340
Cdd:COG4942 239 AA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1654-1937 |
2.82e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1654 KETQLHLDDAlrgQEDLKeqlaiverRANLLQAEIEELWATL----EQTERSRKI-AEQELLDASERVQLLHTQNTSLin 1728
Cdd:COG1196 175 EEAERKLEAT---EENLE--------RLEDILGELERQLEPLerqaEKAERYRELkEELKELEAELLLLKLRELEAEL-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1729 tkKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEQTVKDLQHRLDEAEQLAl 1808
Cdd:COG1196 242 --EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELE- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1809 kggkKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEA 1888
Cdd:COG1196 316 ----ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 153945790 1889 EEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1229-1702 |
3.25e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1229 METDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSK 1308
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1309 QAST--QQIEELKHQLEEETKAKNALAHALQSSRHdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRT 1386
Cdd:COG4717 126 QLLPlyQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1387 EELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQ--NEVEDLMLDVERSNAACAALDKKQRNFDKV--------- 1455
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1456 ---LSEWKQKYEETQAELEASQKESRSLSTELFKVKNvyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKI 1532
Cdd:COG4717 282 vlgLLALLFLLLAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1533 KKQVEQEKC--EIQAALEEAEASLEHE---EGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRvvetmqSTLDAE 1607
Cdd:COG4717 360 EEELQLEELeqEIAALLAEAGVEDEEElraALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE------EELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1608 IRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRnyrntqgilketqlhLDDALRGQEDLKEQLAIVERRANLLQAE 1687
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWAALKLA 498
|
490
....*....|....*
gi 153945790 1688 IEELWATLEQTERSR 1702
Cdd:COG4717 499 LELLEEAREEYREER 513
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1217-1853 |
3.32e-09 |
|
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: 62.08 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1217 KQKLEKEKSELKMETDDLSSNAEAISK--------AKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAG 1288
Cdd:pfam07111 22 ERRLDTQRPTVTMWEQDVSGDGQGPGRrgrsleleGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1289 EYSRQL-------DEKDALVSQLSRSKQASTQQIEELKHQLEE-ETKAKNALAHALQSSRHDCDLLREQYE--EEQEGKA 1358
Cdd:pfam07111 102 ELDALAvaekagqAEAEGLRAALAGAEMVRKNLEEGSQRELEEiQRLHQEQLSSLTQAHEEALSSLTSKAEglEKSLNSL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1359 ELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-------AEEHVEAVNAKCASLEKTKQRLQNEVEDL 1431
Cdd:pfam07111 182 ETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKyvgeqvpPEVHSQTWELERQELLDTMQHLQEDRADL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1432 MLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEasqKESRSLstelfkVKNVYEESLDQLETLRRENKNLQQE 1511
Cdd:pfam07111 262 QATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFP---KKCRSL------LNRWREKVFALMVQLKAQDLEHRDS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1512 ISDLTEQIAEGGKQIhelekikKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKr 1591
Cdd:pfam07111 333 VKQLRGQVAELQEQV-------TSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1592 nhtRVVETMQSTLDaeirsrndalrvkkKMEGDLNEME---IQLNHANRLAAESLRNYRNTQGILKE----TQLHLDD-- 1662
Cdd:pfam07111 405 ---FVVNAMSSTQI--------------WLETTMTRVEqavARIPSLSNRLSYAVRKVHTIKGLMARkvalAQLRQEScp 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1663 ----ALRGQEDLKEQLAIVERRANLLQAEIeELWATLEQTERSRKIAEQElldaSERVQllhtqntsLINTKKKLENDVS 1738
Cdd:pfam07111 468 ppppAPPVDADLSLELEQLREERNRLDAEL-QLSAHLIQQEVGRAREQGE----AERQQ--------LSEVAQQLEQELQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1739 QLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAH-----LERMKKNLEQTVKDLQHRLDEA--EQLALKGG 1811
Cdd:pfam07111 535 RAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVS 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 153945790 1812 KKQIQKLEARVRELEGEVE--NEQKRNAEAvkglRKHERRVKEL 1853
Cdd:pfam07111 615 LRQIQHRATQEKERNQELRrlQDEARKEEG----QRLARRVQEL 654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
857-1354 |
3.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 857 EEFQKTKDELAKSEAKRKELE----EKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEE 932
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNlkelKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 933 EeinaeLTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDD 1012
Cdd:COG4717 129 P-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1013 LQAEedkVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMendKQQLDEKLEKKEFEISN 1092
Cdd:COG4717 204 LQQR---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA---LLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1093 LI-SKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKRE 1171
Cdd:COG4717 278 VLfLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1172 AEFQKLRRDLEEATLQheamvAALRKKHADSMAELGEQIDNLQRvKQKLEKEKSELKMETDDLSSNAEAISkAKGNLEkm 1251
Cdd:COG4717 358 ELEEELQLEELEQEIA-----ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELL-EALDEE-- 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1252 crSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEageySRQLDEKDALVSQLsrskqastQQIEELKHQLEEETKAKNA 1331
Cdd:COG4717 429 --ELEEELEELEEELEELEEELEELREELAELEAE----LEQLEEDGELAELL--------QELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|...
gi 153945790 1332 LAHALQSSRHdcdlLREQYEEEQ 1354
Cdd:COG4717 495 LKLALELLEE----AREEYREER 513
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
842-1329 |
3.47e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.15 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 842 LLKSAETEKEMATMK-----EEFQKTKDELAKSEAKRKE-----LEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQL 911
Cdd:pfam10174 264 LLHTEDREEEIKQMEvykshSKFMKNKIDQLKQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 912 iknkiqlEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 991
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 992 IAKLSKEKKALQE------THQQTLDDLQAEEDKV-NILTKAKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKL 1064
Cdd:pfam10174 417 LAGLKERVKSLQTdssntdTALTTLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1065 AQESTMDMENDKQQLDEKLEKKEFEISNLiskiedeqavEIQLQKKIKELQARIEELGEEIEAERASRAKAEkqRSDLSR 1144
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSL----------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE--INDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1145 ELEEISERLEEAGGATSAQVE--LNKKREAEFQKLRRDLEeatlqheamVAALRKKHADSMAELGEQIDNLQRVKQKLEK 1222
Cdd:pfam10174 562 LLEQEVARYKEESGKAQAEVErlLGILREVENEKNDKDKK---------IAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1223 EKSEL----KMETDDLSSNAE--AISKAKGNLEKMCRSLEDQVSELKTKE---EEQQRLINDLTAQRARLQTEAGEYSRQ 1293
Cdd:pfam10174 633 KGAQLleeaRRREDNLADNSQqlQLEELMGALEKTRQELDATKARLSSTQqslAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1294 -----LDEKDALVS--QLSRSKQASTQ--------QIEELKHQLEEETKAK 1329
Cdd:pfam10174 713 allaaISEKDANIAllELSSSKKKKTQeevmalkrEKDRLVHQLKQQTQNR 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1200-1416 |
3.90e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1200 ADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVS----ELKTKEEEQQRLIND 1275
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1276 LTAQRARLQTEAGEYSR--QLDEKDALVS-----QLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLRE 1348
Cdd:COG4942 99 LEAQKEELAELLRALYRlgRQPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1349 QYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCAS 1416
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
890-1134 |
4.14e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 890 LQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK 969
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 970 EKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAktkLEQQVDDLEGSLEQEKKLRM 1049
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1050 DLERAKRKLEGDLKLAQESTMDME---NDKQQLDEKLEKKEFEISNLISKIEDEQAveiQLQKKIKELQARIEELGEEIE 1126
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEalkAERQKLLARLEKELAELAAELAELQQEAE---ELEALIARLEAEAAAAAERTP 244
|
....*...
gi 153945790 1127 AERASRAK 1134
Cdd:COG4942 245 AAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
857-1148 |
4.88e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 857 EEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLqlqVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEIN 936
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 937 AELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQT 1009
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDkseenarSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1010 LDDLQAEEDKVNI----LTKAKTKLEQQVDDLEGSLE----QEKKLRMDLERAKRKLEGDLKLAQESTMD---------- 1071
Cdd:pfam05483 628 NKQLNAYEIKVNKleleLASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemva 707
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1072 -MENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEE 1148
Cdd:pfam05483 708 lMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1491-1912 |
5.77e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1491 YEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEAsleheegkilriqlELNQ 1570
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE--------------ELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1571 VKSEVdRKIAEKDEEIDQLKRnHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLnhanrlaaESLRNYRNTQ 1650
Cdd:PRK03918 226 LEKEV-KELEELKEEIEELEK-ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--------KELKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1651 GILKETQLHLDDALRgqeDLKEQLAIVERRANLLQAEIEELW---ATLEQTERSRKIAEQELLDASERVQLLHTQNTSL- 1726
Cdd:PRK03918 296 IKLSEFYEEYLDELR---EIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKe 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1727 ----------INTKKKLENDVSQLQSEVEEVIQESRNAEEKA---KKAITDAAMMAEELKKEQD---------TSAHLER 1784
Cdd:PRK03918 373 elerlkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1785 MKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELEGEVENEQK--RNAEAVKGLRKHERRVKELTYQT-EEDR 1861
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKA 524
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1862 KNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNanlsKFRKLQHELEEAEER 1912
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1668-1935 |
6.94e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1668 EDLKEQLAIVERRANLLQAEIEELWATLE--QTERSRKIAEQELLDASERVQLlhtqnTSLINTKKKLENDVSQLQSEVE 1745
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1746 EVIQEsrnaeekakkaITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQhRLDEAEQLALKGG----KKQIQKLEAR 1821
Cdd:TIGR02169 248 SLEEE-----------LEKLTEEISELEKR------LEEIEQLLEELNKKIK-DLGEEEQLRVKEKigelEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1822 VRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRK 1901
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270
....*....|....*....|....*....|....
gi 153945790 1902 LQHELEEAEERADIAESQVNKLRVKSREVHTKIS 1935
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
840-1406 |
7.19e-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: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 840 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRK--ELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLI----- 912
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRleLLEAELEELRAELARLEAELERLEARLDALREELDELEaqirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 913 ---KNKIQLEAKIKEvteraeeeeeinaeLTAKKRKLEDECSELKKDIDDLELTLAKVEKE----KHATENKVKNLTEEM 985
Cdd:COG4913 335 nggDRLEQLEREIER--------------LERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEEL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 986 AGLDETIAKLSKEKKALQETHQQTLDDLQA-EEDKVNI---LTKAKTKLEQQVDDLEGSL----------EQEKKLRMDL 1051
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASlERRKSNIparLLALRDALAEALGLDEAELpfvgelievrPEEERWRGAI 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1052 ERA-----------------------KRKLEGDL-----KLAQESTMDMENDKQQLDEKLEKKEFEISNLIS-------- 1095
Cdd:COG4913 481 ERVlggfaltllvppehyaaalrwvnRLHLRGRLvyervRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEaelgrrfd 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1096 --KIEDEQAVE-----IQLQKKIKELQARieelgEEIEAERASRAK------AEKQRSDLSRELEEISERLEEAggatSA 1162
Cdd:COG4913 561 yvCVDSPEELRrhpraITRAGQVKGNGTR-----HEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEA----EE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1163 QVELNKKREAEFQKLRRDLEEATLQHEAMVaalrkkhadSMAELGEQIDNLQRVKQKLEKEKSELkmetddlssnaeais 1242
Cdd:COG4913 632 RLEALEAELDALQERREALQRLAEYSWDEI---------DVASAEREIAELEAELERLDASSDDL--------------- 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1243 kakgnlekmcRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDE-KDALVSQLSRSKQASTQQIEELKHQ 1321
Cdd:COG4913 688 ----------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1322 LEEETKAKnALAHALQSSRHDCDLLREQYEEEQEGKaeLQRALSKANSEVAQWRTKYET----DAI---QRTEELEEAKK 1394
Cdd:COG4913 758 ALGDAVER-ELRENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEE 834
|
650
....*....|..
gi 153945790 1395 KLAQRLQEAEEH 1406
Cdd:COG4913 835 RFKELLNENSIE 846
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
980-1196 |
7.60e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 980 NLTEEMAGLDETIAKLSKEKKALQ---ETHQQTLDDLQAEEDKVNILTKAKTkLEQQVDDLEGSLEQEKKLRMDLERAKR 1056
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRkelEEAEAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1057 KLEGDLKLAQESTMDMENDK--QQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAE-RASRA 1133
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASlEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1134 KAEKQRSDLSRELEEISERLEEAGgatsaqvelnkKREAEFQKLRRDLEEATLQHEAMVAALR 1196
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELP-----------ELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1192-1920 |
8.22e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1192 VAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNL---EKMCRSLEDqVSELKTKEEE 1268
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALrqqEKIERYQED-LEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1269 QQRLINDLTAQRARLQTEAGeysRQLDEKDALVSQLSRSKQA-STQQIEELKHQleeetKAKNALAHAlqssRHDCDL-- 1345
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLE---AAEEEVDSLKSQLADYQQAlDVQQTRAIQYQ-----QAVQALEKA----RALCGLpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1346 ------------LREQYEEEQEGKAELQRALSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKKLAQ--RLQEAEEH 1406
Cdd:COG3096 434 ltpenaedylaaFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1407 VEAVNAKCASLEKTKQRLQNevedlmldVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRslstelfk 1486
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV-------- 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1487 vknvyeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHE-EGKILRIQ 1565
Cdd:COG3096 578 ---------EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERErEATVERDE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1566 LElnQVKSEVDRKIAE-------KDEEIDQLKrnhtrvvETMQSTLDAEIRSrndalrvkkkmegdlnemEIQLNHANRL 1638
Cdd:COG3096 649 LA--ARKQALESQIERlsqpggaEDPRLLALA-------ERLGGVLLSEIYD------------------DVTLEDAPYF 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1639 AAE--SLRN---YRNTQGILKetqlhlddALRGQEDLKEQLAIVERRANLLQA---EIEEL----WATLEQTE-RSRKIA 1705
Cdd:COG3096 702 SALygPARHaivVPDLSAVKE--------QLAGLEDCPEDLYLIEGDPDSFDDsvfDAEELedavVVKLSDRQwRYSRFP 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1706 EQELLD--ASE-RVQLLHTQNTSLINTKKKLENDVSQLQSeveevIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHL 1782
Cdd:COG3096 774 EVPLFGraAREkRLEELRAERDELAEQYAKASFDVQKLQR-----LHQAFSQFVGGHLAVAFAPDPEAELAALRQRRSEL 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1783 ERMKKNLEQTVKDLQHRLDeaeqlALKGGKKQIQKL------------EARVRELEGEVENEQkrnaEAVKGLRKHERRV 1850
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLD-----QLKEQLQLLNKLlpqanlladetlADRLEELREELDAAQ----EAQAFIQQHGKAL 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1851 KELtyqteEDRKNVLR--------LQDLVDKLQAKVKSYKRQA---------------EEAEEQSNANLSKFRKLQHELE 1907
Cdd:COG3096 920 AQL-----EPLVAVLQsdpeqfeqLQADYLQAKEQQRRLKQQIfalsevvqrrphfsyEDAVGLLGENSDLNEKLRARLE 994
|
810
....*....|...
gi 153945790 1908 EAEERADIAESQV 1920
Cdd:COG3096 995 QAEEARREAREQL 1007
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1089-1331 |
9.69e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1089 EISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsaqvelnk 1168
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1169 kREAEFQKLRRDLEEATLQHEAMVAALrkkHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNL 1248
Cdd:COG3883 84 -RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1249 EKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKA 1328
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
...
gi 153945790 1329 KNA 1331
Cdd:COG3883 240 AAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1663-1894 |
1.26e-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: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1663 ALRGQEDLKEQLaivERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQS 1742
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1743 EVEEVIQESRNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1816
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1817 KLEARVRELEGEVENEQKRNAEAVKglrKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNA 1894
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1106-1333 |
1.26e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1106 QLQKKIKELQARIeelgeeieaerasrAKAEKQRSDLSRELEEISERLEEAggatsaQVELNKKrEAEFQKLRRDLEEAT 1185
Cdd:COG3883 20 AKQKELSELQAEL--------------EAAQAELDALQAELEELNEEYNEL------QAELEAL-QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1186 LQHEAMVAALrKKHADSMAELGEQIDNLQRVkqkLEKEkselkmETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTK 1265
Cdd:COG3883 79 AEIEERREEL-GERARALYRSGGSVSYLDVL---LGSE------SFSDFLDRLSALSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1266 EEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALA 1333
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1348-1585 |
1.35e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1348 EQYEEEQEGKAELQRALSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNE 1427
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1428 vedlmldversnaacaaLDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKN 1507
Cdd:COG4942 99 -----------------LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1508 LQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEE 1585
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1276 |
1.80e-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: 59.65 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 858 EFQKTKDELAKSEAKRKELEEKMVTLLKEK-----NDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEE 932
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 933 EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDD 1012
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1013 LQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqestmdmendkqQLDEKLEKKEFEISN 1092
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE--------------QKQKELKSKEKELKK 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1093 LISKIedeqaveIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEeaggatsaqvelNKKREA 1172
Cdd:TIGR04523 501 LNEEK-------KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK------------KENLEK 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1173 EFQKLRRDLEEATLQHEAMVAA------LRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKG 1246
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKqeekqeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN 641
|
410 420 430
....*....|....*....|....*....|
gi 153945790 1247 NLEKMCRSLEDQVSELKTKEEEQQRLINDL 1276
Cdd:TIGR04523 642 KLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1024-1248 |
2.19e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1024 TKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAV 1103
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1104 EIQLQKKIKEL---------QARIEELGEEIEAERASRA-----KAEKQRSDLSRELEEISERLEEAGGATSAQVELNKK 1169
Cdd:COG4942 99 LEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1170 REAEFQKLRRDLEEATLQHEAMVAALRKK---HADSMAELGEQIDNLQRVKQKLEKEKSELKMETddlssNAEAISKAKG 1246
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAAAAERT-----PAAGFAALKG 253
|
..
gi 153945790 1247 NL 1248
Cdd:COG4942 254 KL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
870-1212 |
2.33e-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: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 870 EAKRKELEEKMVTLLKEKNDLQLQvQSEADSLADAEERCEQLIKNKIQLEAkikevteraeeeeeinaeltakkrkLEDE 949
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAE-LDALQERREALQRLAEYSWDEIDVAS-------------------------AERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 950 CSELKKDIDDLELT---LAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKA 1026
Cdd:COG4913 670 IAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1027 KtkLEQQVDDLEGSlEQEKKLRMDLERAKRKLEGDLKLAQESTMDmendkqQLDEKLEKKEFEISNLISKIEDEQAVEIQ 1106
Cdd:COG4913 750 L--LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER------AMRAFNREWPAETADLDADLESLPEYLAL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1107 LQK----KIKELQARIEELGEeieaeRASRAKAEKQRSDLSRELEEISERLEEA---------GGATSAQVELNKKREAE 1173
Cdd:COG4913 821 LDRleedGLPEYEERFKELLN-----ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPE 895
|
330 340 350
....*....|....*....|....*....|....*....
gi 153945790 1174 FQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDN 1212
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1391-1618 |
2.45e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1391 EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAEL 1470
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1471 EASQKESRSLSTELFKVKNVYEESL----DQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQ-- 1544
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEal 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1545 -AALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVK 1618
Cdd:COG4942 180 lAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1388-1830 |
2.54e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 58.93 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1388 ELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSE--------- 1458
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEEnfrletard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1459 -WKQKYEE----------TQAELEASQKESRSLSTELFKVKN-------------VYEESLDQLETLRRENKNLQQEISD 1514
Cdd:pfam05622 84 dYRIKCEElekevlelqhRNEELTSLAEEAQALKDEMDILREssdkvkkleatveTYKKKLEDLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1515 LTEQIAEGGKQIHELEKIKKQVEQEKCEIQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEVDRKIAEKD---E 1584
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1585 EIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAaeSLRNYRNTQGILKETQLHLDDAL 1664
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKML--RLGQEGSYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1665 RGQEDLKEQLAIVERRANLLQAEIEELWATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLENDVSQLQSEV 1744
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1745 EEVIQESRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLEQ---TVKDLQHRLDEAEQLALKGGKKQIQ 1816
Cdd:pfam05622 377 SELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLL 456
|
490
....*....|....
gi 153945790 1817 KLEARVRELEGEVE 1830
Cdd:pfam05622 457 EKDKKIEHLERDFE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1217-1444 |
3.36e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1217 KQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDE 1296
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1297 KDALVSQLSRSKQASTQQiEELKHQLEEETkaKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRT 1376
Cdd:COG4942 102 QKEELAELLRALYRLGRQ-PPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1377 KYETDAIQRtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAA 1444
Cdd:COG4942 179 LLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1253-1473 |
3.51e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1253 RSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNAL 1332
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1333 AHALQssrhdcDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQ 1401
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 1402 EAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEAS 1473
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1445-1879 |
4.98e-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: 58.11 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1445 LDKKQRNFDKVLSEWKQKYEETQAELEASQKESRS-------LSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTE 1517
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNdkeqknkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1518 QIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQ-------------LELNQVKSEVDRKIAEKDE 1584
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiqknkslesqiSELKKQNNQLKDNIEKKQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1585 EIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKME---GDLNEMEIQLNHANrlAAESLRNYRNTQGILKETQLHLD 1661
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLK--SEISDLNNQKEQDWNKELKSELK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1662 DALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQ 1741
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1742 SEVEEVIQESRNAEEKAKKAITDAAMMAEELKKeqdtsahLERMKKNLEQTVKDLQHRlDEAEQLALKGGKKQIQKLEAR 1821
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-------LKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETQ 469
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1822 VRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVK 1879
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1390-1591 |
5.04e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1390 EEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcaaLDKKQRNFDKVLSEWKQKYEETQAE 1469
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1470 LEASQKESRSLS--TELFKVKNVyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAAL 1547
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESF-SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153945790 1548 EEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKR 1591
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1461-1930 |
5.26e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 57.92 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1461 QKYEETQ-AELEASQKE--SRSLSTELFKVK--NVYEESLDQLETLRRENknlqQEISdlTEQIAEGGKQIHELE----- 1530
Cdd:PRK04778 24 RKRNYKRiDELEERKQEleNLPVNDELEKVKklNLTGQSEEKFEEWRQKW----DEIV--TNSLPDIEEQLFEAEelndk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1531 -KIKKqveqekceIQAALEEAEASLEHEEGKILRIQLELNQ-VKSEvdrkiAEKDEEIDQLKRNHtrvvETMQSTLDAEI 1608
Cdd:PRK04778 98 fRFRK--------AKHEINEIESLLDLIEEDIEQILEELQElLESE-----EKNREEVEQLKDLY----RELRKSLLANR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1609 RSRNDALrvkKKMEGDLNEMEIQLNHANRLAAESlrNYRNTQGILKETQLHLDDAlrgQEDLKEQLAIVERRANLLQAEI 1688
Cdd:PRK04778 161 FSFGPAL---DELEKQLENLEEEFSQFVELTESG--DYVEAREILDQLEEELAAL---EQIMEEIPELLKELQTELPDQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1689 EELWATLEQ-TERSRKIAEQELLdasERVQLLHTQNTSLINTKKKLE-NDVSQLQSEVEEVIQ---ESRNAEEKAKKait 1763
Cdd:PRK04778 233 QELKAGYRElVEEGYHLDHLDIE---KEIQDLKEQIDENLALLEELDlDEAEEKNEEIQERIDqlyDILEREVKARK--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1764 daammaeELKKEQDT-SAHLERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNA 1837
Cdd:PRK04778 307 -------YVEKNSDTlPDFLEHAKEQNKELKEEIDRvkqsyTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1838 EAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAE---EQSN------ANLSKFRKLQHELEE 1908
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKrylEKSNlpglpeDYLEMFFEVSDEIEA 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 153945790 1909 AEER--------------ADIAESQVNKLRVKSREV 1930
Cdd:PRK04778 460 LAEEleekpinmeavnrlLEEATEDVETLEEETEEL 495
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1079-1703 |
6.32e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1079 LDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEElgeeieaerasrakAEKQRSDLSRELEEISERLEEAGG 1158
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN--------------AMDDYNNLKSALNELSSLEDMKNR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1159 ATSAQVELNKKREAEFQKLRRdLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKmETDDLSSNA 1238
Cdd:PRK01156 254 YESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEIN-KYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1239 EAISKAKGNLEKMCRSLED---QVSELKTKEEEQQRLINDLTAQRARLQteagEYSRQLDEKDALVSQLSRSKQASTqqi 1315
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIE----EYSKNIERMSAFISEILKIQEIDP--- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1316 EELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQralskANSEVAQWRTKYETDAIQR-TEELEEAKK 1394
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN-----GQSVCPVCGTTLGEEKSNHiINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1395 KLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEvedlmlDVERSNAACAALDKKQRNFDKVL-SEWKQKYEETQAEleAS 1473
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE------EINKSINEYNKIESARADLEDIKiKINELKDKHDKYE--EI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1474 QKESRSLStelfkvknvyeesLDQLETLRRENKNLQQEISDLteqiaeggkqihELEKIKKQVEqekcEIQAALEEAEAS 1553
Cdd:PRK01156 552 KNRYKSLK-------------LEDLDSKRTSWLNALAVISLI------------DIETNRSRSN----EIKKQLNDLESR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1554 LEHeegkilrIQLELNQVKSEVDRKIAEKDEEIDQL--KRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQ 1631
Cdd:PRK01156 603 LQE-------IEIGFPDDKSYIDKSIREIENEANNLnnKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSR 675
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 1632 LNHANRLaaeslrnyrntqgiLKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRK 1703
Cdd:PRK01156 676 INDIEDN--------------LKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1347-1911 |
7.19e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1347 REQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQEAEEHVEAVNAKCASLEKTKQRLQN 1426
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1427 EVEDLMLDVERSNAACAALdkKQRNFDKVLSEWKQKYEETQAELeasQKESRSLSTELFKVKNVYEESLDQLETLRRENK 1506
Cdd:TIGR00618 275 QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTEL---QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1507 NLQQE--ISDLTEQ----IAEGGKQIHELEKIKKQVEQEKCEIQA--ALEEAEASLEHEEGKILRIQLELN--QVKSEVD 1576
Cdd:TIGR00618 350 LHSQEihIRDAHEVatsiREISCQQHTLTQHIHTLQQQKTTLTQKlqSLCKELDILQREQATIDTRTSAFRdlQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1577 RKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKET 1656
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1657 QLHLDDALRG---QEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKL 1733
Cdd:TIGR00618 510 CIHPNPARQDidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1734 ENDVSQLQSEVEEviqesrNAEEKAKKAitdAAMMAEELKKEQdtSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKK 1813
Cdd:TIGR00618 590 QNITVRLQDLTEK------LSEAEDMLA---CEQHALLRKLQP--EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1814 QIQKLEARVRELEGEVENEQKRNaeavkgLRKHERRVKELTYqteeDRKNVLRLQDLVDKLQAKVKSYKRQAEEaeeQSN 1893
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLA------LQKMQSEKEQLTY----WKEMLAQCQTLLRELETHIEEYDREFNE---IEN 725
|
570
....*....|....*...
gi 153945790 1894 ANLSKFRKLQHELEEAEE 1911
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQ 743
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1302-1521 |
1.02e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1302 SQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetd 1381
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1382 aiqrtEELEEAKKKLAQRLQEAE--------------EHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDK 1447
Cdd:COG4942 97 -----AELEAQKEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1448 KQrnfdKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEEsldQLETLRRENKNLQQEISDLTEQIAE 1521
Cdd:COG4942 172 ER----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAA 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1506-1932 |
1.11e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.14 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1506 KNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALE-EAEASLEHEEGKILRIQLELNQVK-SEVDRKIAEKD 1583
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1584 EEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKME---GDLNEMEIQLnHANRLAAESLRNYRNtqgilketqlhl 1660
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKLETLTNQNS------------ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1661 dDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQL 1740
Cdd:pfam10174 321 -DCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1741 QSEVEEVIQESRNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EQTVKDLQHRLDEAEQL--ALKG 1810
Cdd:pfam10174 400 QKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1811 GKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQakvksykrQAEEAEE 1890
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVR 551
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 153945790 1891 QSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1932
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
940-1163 |
1.16e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 940 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQethqQTLDDLQAEEDK 1019
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE----AELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1020 VNI-LTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEIS 1091
Cdd:COG4942 95 LRAeLEAQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 1092 NLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1163
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
842-1319 |
1.20e-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: 57.04 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 842 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRK-------ELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKN 914
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 915 KIQL----EAKIKEVTERAEEEEEINAELTAKKRKLED----ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMA 986
Cdd:pfam05483 326 ICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 987 GLDETIAKLSKEKKALQETHQ--QTLDDLQAEEDKVNILTKAKTK------------------LEQQVDDLEGSLEQEKK 1046
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeihdleiqltaiktseehYLKEVEDLKTELEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1047 LRMDLERAKRKLE-GDLKLAQE-STMDMENDKQQLDEKLEKKEFEisNLISKIEDEQAVEIQLQKKIK-----------E 1113
Cdd:pfam05483 486 KNIELTAHCDKLLlENKELTQEaSDMTLELKKHQEDIINCKKQEE--RMLKQIENLEEKEMNLRDELEsvreefiqkgdE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1114 LQARIEELGEEIEAERASRAKAEKQR-------SDLSRELEEISERLEEAGGATSAqveLNKKREAEFQKLRrdleeatl 1186
Cdd:pfam05483 564 VKCKLDKSEENARSIEYEVLKKEKQMkilenkcNNLKKQIENKNKNIEELHQENKA---LKKKGSAENKQLN-------- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1187 QHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRS------------ 1254
Cdd:pfam05483 633 AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHkiaemvalmekh 712
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1255 -------LEDQVSEL---KTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELK 1319
Cdd:pfam05483 713 khqydkiIEERDSELglyKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1330-1881 |
1.26e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1330 NALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQEAEEHV 1407
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1408 EAVNAKCASLEKTKQRLqNEVEDLMLDVERSNAACAALDKKQ-RNFDKVLSEWK---QKYEETQAELEASQKESrslste 1483
Cdd:PRK01156 266 SMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIKKLSVLQKDY------ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1484 lfkvknvyeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILR 1563
Cdd:PRK01156 339 ------------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1564 IQLELNQVKSEVDR---KIAEKDEEIDQLKRNHTRVVETMQ------------STLDAEI--RSRNDALRVKKKMEGDLN 1626
Cdd:PRK01156 407 IKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgTTLGEEKsnHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1627 EMEIQLNHAN-----------RLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQA-EIEELWAT 1694
Cdd:PRK01156 487 EIEIEVKDIDekivdlkkrkeYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1695 LE--------------QTERSRKI-AEQELLDASERVQLLHTQ----NTSLINTKKKLENDVSQLQSEVEEvIQESRNAE 1755
Cdd:PRK01156 567 RTswlnalavislidiETNRSRSNeIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKYNE-IQENKILI 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1756 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAeQLALKGGKKQIQKLEARVRELEGEVeNEQKR 1835
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA-KANRARLESTIEILRTRINELSDRI-NDINE 723
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 153945790 1836 NAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSY 1881
Cdd:PRK01156 724 TLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKY 769
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1316-1700 |
1.33e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.44 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1316 EELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEgkaELQRALSKANSEVAQwrtkYETDAIQRTEELEEAKKK 1395
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDRE---QWERQRRELESRVAE----LKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1396 LAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE---TQAELEA 1472
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1473 SQKESRSLSTELFKVKNvyeeSLDQLETlrrENKNLQQEISDLTEQIAEGGKQIHELEKIKKqveqekcEIQAALEEAEA 1552
Cdd:pfam07888 183 TEEELRSLSKEFQELRN----SLAQRDT---QVLQLQDTITTLTQKLTTAHRKEAENEALLE-------ELRSLQERLNA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1553 SLEHEEGkilrIQLELNQVKSEVDRKIAEkdeeidqLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQL 1632
Cdd:pfam07888 249 SERKVEG----LGEELSSMAAQRDRTQAE-------LHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1633 NHANRLAAESLRNYRNTQGILKETQ--------------LHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQT 1698
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREklevelgrekdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQL 397
|
..
gi 153945790 1699 ER 1700
Cdd:pfam07888 398 EQ 399
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
654-678 |
1.35e-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: 1.35e-07
10 20
....*....|....*....|....*
gi 153945790 654 FRENLNKLMTNLRSTHPHFVRCIIP 678
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1456-1912 |
1.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1456 LSEWKQKYEETQAELEASQKESRSLSTELfkvknVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQ 1535
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1536 VEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDAL 1615
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1616 RVkkkmegDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATL 1695
Cdd:COG4717 252 LL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1696 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEndVSQLQSEVEEVIQESRNAEEKakkaitDAAMMAEELKKE 1775
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEE------ELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1776 QDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERrvkelty 1855
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELEEELEELREELAELEAELEQLEE------- 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1856 qteedrknvlrlQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEER 1912
Cdd:COG4717 468 ------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1456-1924 |
1.72e-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: 56.65 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1456 LSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQ 1535
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1536 VEQEKCEIQAALEEAEASLEHeegkiLRIQLElnQVKSEVDRKIAEKDEEIDQLKRNHTRVV---ETMQSTLDAEIRSRN 1612
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1613 DALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQ----GILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEI 1688
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1689 EElwatleQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAiTDAAMM 1768
Cdd:pfam05483 334 EA------QMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFK-NNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1769 AEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLaLKGGKKQIQKLEAR--------------VRELEGEVENEQK 1834
Cdd:pfam05483 407 LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL-LQAREKEIHDLEIQltaiktseehylkeVEDLKTELEKEKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1835 RNAE---------------------AVKGLRKHERRVKELTYQTEEDRKNVLRLQD----LVDKLQAKVKSYKRQAEEAE 1889
Cdd:pfam05483 486 KNIEltahcdklllenkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVK 565
|
490 500 510
....*....|....*....|....*....|....*
gi 153945790 1890 EQSNANLSKFRKLQHELEEAEERADIAESQVNKLR 1924
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1016-1493 |
1.82e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1016 EEDKVNILTKAKTKLEQQVDDLEgSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLIS 1095
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1096 KIEDEQaveiqLQKKIKELQARIeelgEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVelnkkrEAEFQ 1175
Cdd:COG4717 131 YQELEA-----LEAELAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT------EEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1176 KLRRDLEEATLQHEAMVAALRKKHADsMAELGEQIDNLQRVKQKLEKEKS---------------ELKMETDDLSSNAEA 1240
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEE-LEELEEELEQLENELEAAALEERlkearlllliaaallALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1241 I------------------SKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVS 1302
Cdd:COG4717 275 IagvlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1303 QLSR-SKQASTQQIEELKHQLEEETKAKN--ALAHALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1379
Cdd:COG4717 355 EAEElEEELQLEELEQEIAALLAEAGVEDeeELRAALE--------QAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1380 TDAiqrteeleeakkkLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErsnaacaaldkkqrnfdkvLSEW 1459
Cdd:COG4717 427 EEE-------------LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-------------------LAEL 474
|
490 500 510
....*....|....*....|....*....|....
gi 153945790 1460 KQKYEETQAELEASQKESRSLSTELFKVKNVYEE 1493
Cdd:COG4717 475 LQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1296-1778 |
1.85e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1296 EKDALVSQLSRSKQASTQQIEELKHQLEEetkaknalahaLQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWR 1375
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKE-----------AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1376 TKYET-DAIQRTEELEEAKKKLAQRLQEAEEHVEAVnakcASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQrnfdk 1454
Cdd:COG4717 123 KLLQLlPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEE----- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1455 vLSEWKQKYEETQAELEASQKEsrslstelfkvknvyeesldqLETLRRENKNLQQEISDLTEQiaeggkqiHELEKIKK 1534
Cdd:COG4717 194 -LQDLAEELEELQQRLAELEEE---------------------LEEAQEELEELEEELEQLENE--------LEAAALEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1535 QVEQEK---------CEIQAALEEAEASLEHEEGK------ILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVET 1599
Cdd:COG4717 244 RLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1600 MQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRlAAESLRNYRNTQGILKETQLHLDDALRG-------QEDLKE 1672
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQLEELEQEIAALLAEAGVEDEEELRAaleqaeeYQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1673 QLAIVERRANLLQAEIEELWATLEQTERSRKIA--EQELLDASERVQLLHTQNTSLINTKKKLEND--VSQLQSEVEEVI 1748
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEALDEEELEEELEelEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELK 482
|
490 500 510
....*....|....*....|....*....|
gi 153945790 1749 QESRNAEEKAKKAITDAAMMAEELKKEQDT 1778
Cdd:COG4717 483 AELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1129-1745 |
1.86e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1129 RASRAKAEKQRSDLSRELE--EISERleeaggatSAQVELNKKREAEFQKLRRDLEEaTLQHEAMVAALRKKHADSMAEL 1206
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKqmELEHK--------RARIELEKKASALKRQLDRESDR-NQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1207 GEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLindltaqrarlqte 1286
Cdd:pfam05557 72 REQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1287 ageySRQLDEKDALVSQLSRSKQASTQQIEELKhqlEEETKAKNaLAHALQSSRHDCDLLREQyEEEQEGKAELQRALSK 1366
Cdd:pfam05557 138 ----QERLDLLKAKASEAEQLRQNLEKQQSSLA---EAEQRIKE-LEFEIQSQEQDSEIVKNS-KSELARIPELEKELER 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1367 ANSEVAQWRTKYETDAIQRtEELEEAKKKLaqrlqeaeEHVEAVNAKCASLEKTKQRLQNEvedlmldversnaacaald 1446
Cdd:pfam05557 209 LREHNKHLNENIENKLLLK-EEVEDLKRKL--------EREEKYREEAATLELEKEKLEQE------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1447 kkqrnfdkvLSEWKQKYEETQAELEASQKESRslstelfkvknvyeesldQLETLRRENKNLQQEISDLTEqiaeggkQI 1526
Cdd:pfam05557 261 ---------LQSWVKLAQDTGLNLRSPEDLSR------------------RIEQLQQREIVLKEENSSLTS-------SA 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1527 HELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQlelnqvksevdRKIAEKDEEIDQLKRNhtrvVETMQSTLDA 1606
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAI----LESYDKELTM 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1607 EIRSRNDALRVK------KKMEGDLNEMEIQLNHANRlaaeslrnyrnTQGILKETQLHLD---DALRGQEDLKEQLAIV 1677
Cdd:pfam05557 372 SNYSPQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQQESLADPSYSK 440
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1678 ERRANLLQaEIEELWATLEQTERSRKIAEQELLDAS-------ERVQLLHTQNTSLINTKKKLENDVSQLQSEVE 1745
Cdd:pfam05557 441 EEVDSLRR-KLETLELERQRLREQKNELEMELERRClqgdydpKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIE 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1496-1935 |
1.97e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1496 DQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLE---HEEGKILRIQLELNQVK 1572
Cdd:TIGR04523 96 DKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnNKYNDLKKQKEELENEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1573 SEVDRKIAEKDEEIDQLKRNHTRVvETMQSTLDAEIRSrndalrvKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGI 1652
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKL-ELLLSNLKKKIQK-------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1653 LKETQLHLDDALRGQEDLKEQLaiverraNLLQAEIEELWATLEQTERSRKIAEQELLD-ASERVQLLHTQ-NTSLINTK 1730
Cdd:TIGR04523 248 ISNTQTQLNQLKDEQNKIKKQL-------SEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKElKSELKNQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1731 KKLENDVSQLqSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQLalkg 1810
Cdd:TIGR04523 321 KKLEEIQNQI-SQNNKIISQLNEQISQLKKELTNSESENSEKQRE------LEEKQNEIEKLKKENQSYKQEIKNL---- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1811 gKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEE 1890
Cdd:TIGR04523 390 -ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 153945790 1891 QSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKIS 1935
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1129-1589 |
2.35e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1129 RASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVE-LNKKREAE--FQKLRR---DLEEATLQHEAMVAALrkkhads 1202
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhLNLVQTALrqQEKIERyqaDLEELEERLEEQNEVV------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1203 mAELGEQIDNLQRVKQKLEKEKSELKMETDDLssnaeaiskakgnlekmcrsledqvselktkeeeQQRLIndltaqraR 1282
Cdd:PRK04863 372 -EEADEQQEENEARAEAAEEEVDELKSQLADY----------------------------------QQALD--------V 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1283 LQTEAGEYS---RQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSrhdcDLLREQYEEeqegKAE 1359
Cdd:PRK04863 409 QQTRAIQYQqavQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA----QAAHSQFEQ----AYQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1360 LQRALSKANSEVAQWRTkyetdAIQRTEELEEAKKkLAQRLQEAEEHveavnakcasLEKTKQRLQNevedlmldversn 1439
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDV-----ARELLRRLREQRH-LAEQLQQLRMR----------LSELEQRLRQ------------- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1440 aacaaldkkQRNFDKVLSEWKQKY---EETQAELEASQKEsrsLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLT 1516
Cdd:PRK04863 532 ---------QQRAERLLAEFCKRLgknLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1517 EQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEgkilriqlELNQVKSEVDRKIAEKDEEIDQL 1589
Cdd:PRK04863 600 ARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERER--------ELTVERDELAARKQALDEEIERL 664
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1667-1900 |
2.42e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1667 QEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEV 1744
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1745 EEvIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNLEQTVKDLQHRLDEAEQLALKGGKKQ 1814
Cdd:COG3206 243 AA-LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1815 IQKLEARVRELEGEVENEQKRnaeaVKGLRKHERRVKELTYQTEEDRKNvlrLQDLVDKLQakvksykrqaeEAEEQSNA 1894
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE-----------EARLAEAL 383
|
....*.
gi 153945790 1895 NLSKFR 1900
Cdd:COG3206 384 TVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1145 |
2.46e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 939 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQ---A 1015
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsgG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1016 EEDKVNILTKAK---------TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKK 1086
Cdd:COG3883 101 SVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1087 EFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRE 1145
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1165-1908 |
2.85e-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: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1165 ELNKKREAEFQKLRrDLEEATLQ-HEAMVAALRKKHADSMAEL-----GEQIDNLQRVKQKLEKEKSELKMETDDLSSNA 1238
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1239 EAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINdltaqrarlqtEAGEYSRQLDEKDALVSQLsrskqastqqIEEL 1318
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD-----------KSKEYIKTISIKEDEIFKI----------INEM 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1319 KHQLEEETKAKNALAHAlqssRHDCdllREQYEEEQEGKAELqraLSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLA 1397
Cdd:TIGR01612 838 KFMKDDFLNKVDKFINF----ENNC---KEKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1398 QR------LQEAEEHVEAVNAKCASLEK--TKQRLQNEVEDLMLDVERSNaacAALDKKQRN-FDKVLSEWKQKYEETQA 1468
Cdd:TIGR01612 908 EEyqnintLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTIKES---NLIEKSYKDkFDNTLIDKINELDKAFK 984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1469 ELEASQKESRslSTELFKVKNVYEESL---------DQLETLRRENKNLQQEISDLTEQIAEGGKQIH--------ELEK 1531
Cdd:TIGR01612 985 DASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIEK 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1532 -IKKQVEQEKCEIqaaLEEAEASLEHEEGkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrvVETMQSTLDAEIrs 1610
Cdd:TIGR01612 1063 eIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI-- 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1611 rNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNyRNTQGILKETQlhlddalrgqedlkEQLAIVERRANLLQaEIEE 1690
Cdd:TIGR01612 1132 -KALEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIE--------------NIVTKIDKKKNIYD-EIKK 1194
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1691 LWATLEQTERsrkiaEQELLDASERVQLLHTQNTSLI------NTKKKLENDVSQLQSEVEEV--IQESRNAEEKAKKAI 1762
Cdd:TIGR01612 1195 LLNEIAEIEK-----DKTSLEEVKGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGIE 1269
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1763 TDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKG 1842
Cdd:TIGR01612 1270 MDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLY 1344
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1843 LRKherrvkeltyqtEEDRKNVLRLQDlVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEE 1908
Cdd:TIGR01612 1345 LNE------------IANIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
945-1612 |
4.27e-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: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 945 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAgldetiAKLSKEKKALQETHQQtlDDLQAEEDKV-NIL 1023
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIK------AQINDLEDVADKAISN--DDPEEIEKKIeNIV 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1024 TK--AKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKlegDLKLAQE-STMDMEndkqQLDEKLEKKEFEISNLISKIEDE 1100
Cdd:TIGR01612 1180 TKidKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGI---NLSYGKNlGKLFLE----KIDEEKKKSEHMIKAMEAYIEDL 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1101 QAVEIQLQKKIKELQARIEELGEEIEAeRASRAKAEKQRSDLSRELEEISERLEEaggatSAQVELNKKREAEFQKLRRD 1180
Cdd:TIGR01612 1253 DEIKEKSPEIENEMGIEMDIKAEMETF-NISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1181 LEEATLQHEamvaalrkKHADSMAELGEQIDNLQRVKQ--KLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQ 1258
Cdd:TIGR01612 1327 LQKNLLDAQ--------KHNSDINLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDD 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1259 VS--ELKTKEEEQ------QRLINDLTAQRARLQTEAGE---YSRQLDEKDALVSQLSRSKQASTQqieelKHQLEEETK 1327
Cdd:TIGR01612 1399 INleECKSKIESTlddkdiDECIKKIKELKNHILSEESNidtYFKNADENNENVLLLFKNIEMADN-----KSQHILKIK 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1328 AKNAlahalqSSRHDCDLlreqyeeeqegkAELQRALSKANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQEAEEHV 1407
Cdd:TIGR01612 1474 KDNA------TNDHDFNI------------NELKEHIDKSK--------GCKDEADKNAKAIEKNKELFEQYKKDVTELL 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1408 E-----AVNAKCASLEKTKQRLQNEVEDL----MLDVERSNAACAALDKKQRNFDKVLSewkqKYEETQAELEASQKESR 1478
Cdd:TIGR01612 1528 NkysalAIKNKFAKTKKDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1479 SLSTELFKVKNVYEESLDQLetlrRENKNLQQEISDLT-----EQIAEGGKQIHELEKIKKQVEQEKCEIqaalEEAEAS 1553
Cdd:TIGR01612 1604 NFENKFLKISDIKKKINDCL----KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNI----EDKKKE 1675
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1554 LEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVET-MQSTLDAEIRSRN 1612
Cdd:TIGR01612 1676 LDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKElIEPTIENLISSFN 1735
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1484-1930 |
5.96e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.47 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1484 LFKVKNVYEEsLDQLETLRRE--NKNLQQEISDLtEQIAEGGKQIHELEKIKKQ----VEQEKCEIQAALEEAEASLEhe 1557
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1558 EGKILRIQLELNQVKS---EVDRKIAEKDEEIDQL----KRNHTRV--VETMQSTLDAEIRSRNDAL-RVKKKMEGDLNE 1627
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELleseEKNREEVeeLKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1628 MEIQLNHANRLAAESlrNYRNTQGILKETQLHLDDAlrgQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQ 1707
Cdd:pfam06160 158 IEEEFSQFEELTESG--DYLEAREVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1708 elLDASERVQLLHTQNTSLINTKKKLE-NDVSQLQSEVEEVIQ---ESRNAEEKAKKaitdaammaeELKKEQDT-SAHL 1782
Cdd:pfam06160 233 --LNVDKEIQQLEEQLEENLALLENLElDEAEEALEEIEERIDqlyDLLEKEVDAKK----------YVEKNLPEiEDYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1783 ERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRN-------AEAVKGLRKHERRV 1850
Cdd:pfam06160 301 EHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeelEEILEQLEEIEEEQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1851 KELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAE----------------EAEEQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLNMDEVNRLLD 460
|
490
....*....|....*.
gi 153945790 1915 IAESQVNKLRVKSREV 1930
Cdd:pfam06160 461 EAQDDVDTLYEKTEEL 476
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1678-1924 |
7.08e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1678 ERRANL--LQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEND---VSQLQSEVEEVIQESR 1752
Cdd:PRK02224 248 ERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADaeaVEARREELEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1753 NAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVEN- 1831
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADD---LEERAEELREEAAELESELEEARE-AVEDRREEIEELEEEIEELRERFGDa 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1832 -EQKRNAEAVKGLRKHER-----RVKELTYQTEEDRKNVLRLQDLVDKLQA-------KVKSYKRQAEEAEEQS---NAN 1895
Cdd:PRK02224 404 pVDLGNAEDFLEELREERdelreREAELEATLRTARERVEEAEALLEAGKCpecgqpvEGSPHVETIEEDRERVeelEAE 483
|
250 260 270
....*....|....*....|....*....|..
gi 153945790 1896 LSKFRKLQHELEEAEERADI---AESQVNKLR 1924
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDlveAEDRIERLE 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1272-1719 |
7.40e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1272 LINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLreqye 1351
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1352 EEQEGKAELQRALSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQEAEEHVEAVnakcasLEKTKQRLQNEVE 1429
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEEleERLEELRELEEELEELEAELAELQEELEEL------LEQLSLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1430 DLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQ 1509
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1510 QEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEaeasLEHEEGKILRIQLELNQVKSevDRKIAEKDEEIDQL 1589
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE----LEEEELEELLAALGLPPDLS--PEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1590 KRNHTRVVETMQSTLDAEIRSRNDAL--RVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQ 1667
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALlaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1668 -----EDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAE--QELLDASERVQLL 1719
Cdd:COG4717 430 leeelEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
943-1313 |
1.04e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.36 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 943 KRKLEDECSELKKDIDDLELTLAKvekekhaTENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNI 1022
Cdd:pfam07888 68 REQWERQRRELESRVAELKEELRQ-------SREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1023 LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEIsnliskiedeqa 1102
Cdd:pfam07888 141 LTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV------------ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1103 veIQLQKKIKELQARIEELGEEIEAERASRakaEKQRSdlSRELEEISERLEEA-GGATSAQVELNKKREAEFQKLRRDL 1181
Cdd:pfam07888 209 --LQLQDTITTLTQKLTTAHRKEAENEALL---EELRS--LQERLNASERKVEGlGEELSSMAAQRDRTQAELHQARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1182 EEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSE 1261
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSE 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1262 LKTKEEEQQRLINDLTAQRARLQTEAGE---YSRQLDEKDALVSQLSRSKQASTQ 1313
Cdd:pfam07888 362 SRRELQELKASLRVAQKEKEQLQAEKQElleYIRQLEQRLETVADAKWSEAALTS 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1453-1620 |
1.05e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1453 DKVLSEWKQKYEETQAELEASQKESRSLSTELfkvknvyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQI------ 1526
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARL-------EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1527 -------HELEKIKKQV---EQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrv 1596
Cdd:COG1579 89 keyealqKEIESLKRRIsdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE---- 164
|
170 180
....*....|....*....|....
gi 153945790 1597 VETMQSTLDAEIRSRNDALRVKKK 1620
Cdd:COG1579 165 REELAAKIPPELLALYERIRKRKN 188
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
844-1413 |
1.14e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 844 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEadsLADAEERCEQLIKNKIQLEAKIK 923
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE---LENLEERLKALTGKHQDVTAKYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 924 EVTERAEEEEeinaeltakKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK--------NLTEEMAGLDETIAKL 995
Cdd:pfam12128 379 RRRSKIKEQN---------NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELReqleagklEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 996 skekKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMEND 1075
Cdd:pfam12128 450 ----KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1076 KQQLDEK-------LEKKEFEISNLISKIEDEQ-----------------------AVEIQLQK--------KIKELQAR 1117
Cdd:pfam12128 526 ELQLFPQagtllhfLRKEAPDWEQSIGKVISPEllhrtdldpevwdgsvggelnlyGVKLDLKRidvpewaaSEEELRER 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1118 IEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGA---------------TSAQVELNKKREA-------EFQ 1175
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlfdekQSEKDKKNKALAErkdsaneRLN 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1176 KLRRDLEEATLQHEAMVAALR--------KKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGN 1247
Cdd:pfam12128 686 SLEAQLKQLDKKHQAWLEEQKeqkreartEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGV 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1248 LEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQteageySRQLDEKDALVSQLSRSKQAstqqIEELKHQL---EE 1324
Cdd:pfam12128 766 DPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ------ETWLQRRPRLATQLSNIERA----ISELQQQLarlIA 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1325 ETKAKNAlahALQSSRHDCDLLREQYEEEQEGKAELQRALSK----ANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRL 1400
Cdd:pfam12128 836 DTKLRRA---KLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedANSEQAQGSIGERLAQL---EDLKLKRDYLSESV 909
|
650
....*....|...
gi 153945790 1401 QEAEEHVEAVNAK 1413
Cdd:pfam12128 910 KKYVEHFKNVIAD 922
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1562-1912 |
1.33e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1562 LRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETmQSTLDAEIRSRND-------ALRVKKKME---GDLNEMEIQ 1631
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEA-ESDLEQDYQAASDhlnlvqtALRQQEKIEryqADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1632 LNHANRLAAESlrnyrntQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQaeieelwatleqterSRKIAEQELLD 1711
Cdd:PRK04863 364 LEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ---------------TRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1712 ASERVQLLhTQNTSLinTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKNLEQ 1791
Cdd:PRK04863 422 ALERAKQL-CGLPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR--SEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1792 TVKDLQHRLDEAEQLAlkggkKQIQKLEARVRELEGEVENEQkrnaEAVKGLRKHERRVkELTYQTEEDrknvlrLQDLV 1871
Cdd:PRK04863 497 VARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRL-GKNLDDEDE------LEQLQ 560
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 153945790 1872 DKLQAKVKSYKRQAEEAEEQSNAnlskfrkLQHELEEAEER 1912
Cdd:PRK04863 561 EELEARLESLSESVSEARERRMA-------LRQQLEQLQAR 594
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1660-1913 |
1.65e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1660 LDDALRGQEDLKEQLAIVERrANLLQAEIEELwatleQTERSRKIAEQELL--DASERVQLLHTQNTSLINTKKKLENDV 1737
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVVPR-AELLQNRLEEC-----LQERAELLQAQEAAnrQREKEKERYKRDREQWERQRRELESRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1738 SQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQK 1817
Cdd:pfam07888 83 AELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1818 LEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEeqsnANLS 1897
Cdd:pfam07888 162 AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE----ALLE 237
|
250
....*....|....*.
gi 153945790 1898 KFRKLQHELEEAEERA 1913
Cdd:pfam07888 238 ELRSLQERLNASERKV 253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
983-1935 |
1.73e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 983 EEMAGLDETIAKLSKEK---KALQETHQQTLDDLQAEEDKvniLTKAKTKLEQQVDDLEGSL----------EQEKKLRM 1049
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELAE---LNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1050 DLERAKRKLEgdlklaqESTMDMENDKQQLDE---KLEKKEFEISNLISKIED-EQAVEIQLQKKIKELQArieelgeei 1125
Cdd:PRK04863 356 DLEELEERLE-------EQNEVVEEADEQQEEneaRAEAAEEEVDELKSQLADyQQALDVQQTRAIQYQQA--------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1126 eAERASRAKAEKQRSDLsrELEEISERLEEAggATSAQVELNKKREAEfQKLRrDLEEATLQHEAMVAALRKkhadsmae 1205
Cdd:PRK04863 420 -VQALERAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK-------- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1206 LGEQID--NLQRVKQKLEKEKSELKMEtddlssnAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQrARL 1283
Cdd:PRK04863 485 IAGEVSrsEAWDVARELLRRLREQRHL-------AEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE-DEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1284 QTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETK-------AKNALAHaLQSSRHDCDLLREQYEEEQEG 1356
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAArapawlaAQDALAR-LREQSGEEFEDSQDVTEYMQQ 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1357 KAELQRALSKANSEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQEAEEHVEAV------------------- 1410
Cdd:PRK04863 636 LLERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsledapyfsa 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1411 ---NAKCA----SLEKTKQRLQNEvEDLMLDVERSNAACAALDkkqrnfDKVLSEWKQKYEETQAELEASQKESRSLSTE 1483
Cdd:PRK04863 705 lygPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFD------DSVFSVEELEKAVVVKIADRQWRYSRFPEVP 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1484 LFKvKNVYEESLDQLetlrrenknlQQEISDLTEQIAEGGKQIHELEKIKKQV----------------EQEKCEIQAAL 1547
Cdd:PRK04863 778 LFG-RAAREKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRR 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1548 EEAEASLEHEEGKILRIQLELNQVKSEVD--RKIAekdEEIDQLKRNH--TRVVEtmqstLDAEIRSRNDALRVKKKMEG 1623
Cdd:PRK04863 847 VELERALADHESQEQQQRSQLEQAKEGLSalNRLL---PRLNLLADETlaDRVEE-----IREQLDEAEEAKRFVQQHGN 918
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1624 DLNEMEIQLNhanrlaaeSLR----NYRNTQGILKETQLHLDDALRGQEDLKEqlaIVERRA--------NLLQAE---I 1688
Cdd:PRK04863 919 ALAQLEPIVS--------VLQsdpeQFEQLKQDYQQAQQTQRDAKQQAFALTE---VVQRRAhfsyedaaEMLAKNsdlN 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1689 EELWATLEQTERSRKIAEQELLDASERvqllHTQN----TSLINTKKKLENDVSQLQSEVEEV-IQESRNAEEKakkait 1763
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQ----LAQYnqvlASLKSSYDAKRQMLQELKQELQDLgVPADSGAEER------ 1057
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1764 dAAMMAEELKKEQDTSahleRMKKN-LEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELEGEVENEQKRNAEAVKG 1842
Cdd:PRK04863 1058 -ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMREQVVNAKAGWCAVLRL 1124
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1843 LRKH--ERRV--KELTYQT---------------------EEDRKNVLRLQDLVDKLQAKVKSY-------KRQAE---- 1886
Cdd:PRK04863 1125 VKDNgvERRLhrRELAYLSadelrsmsdkalgalrlavadNEHLRDVLRLSEDPKRPERKVQFYiavyqhlRERIRqdii 1204
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1887 ------EAEEQSNANLSkfrKLQHELEEAEeradiaesqvNKLRVKSREVHTKIS 1935
Cdd:PRK04863 1205 rtddpvEAIEQMEIELS---RLTEELTSRE----------QKLAISSESVANIIR 1246
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1248-1521 |
1.84e-06 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 52.93 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1248 LEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETK 1327
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1328 AKNALAHALQSSRhdcdllreQYEEEQEGKAELQRALSKANSevaqwrtKYETDAI-QRTEELEEAKKKLAQRLQEAEEH 1406
Cdd:pfam09726 480 ARASAEKQLAEEK--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1407 VEAVNAKCASLEKTKQRlQNEVEDLMldversnAACAALDKKQRNFDKVLSewkqkyEETQAELEasqkesrsLSTELFK 1486
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKLD--------LFSALGD 602
|
250 260 270
....*....|....*....|....*....|....*
gi 153945790 1487 VKNvyeesldQLETLRRENKNLQQEISDLTEQIAE 1521
Cdd:pfam09726 603 AKR-------QLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1132-1431 |
1.93e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.42 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1132 RAKAEKQRSDLSRELEEISERLEEAggatSAQVElnkkreaEFQKLRRDLEEATLQH---------EAMVAALRKKHADS 1202
Cdd:COG3096 780 RAAREKRLEELRAERDELAEQYAKA----SFDVQ-------KLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSEL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1203 MAELGEQIDNLQRVKQKLEKEKSELKM-----------ETDDLSSNAEAISKAKGNLE----------KMCRSLEDQVSE 1261
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqanllADETLADRLEELREELDAAQeaqafiqqhgKALAQLEPLVAV 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1262 LKTKEEEQQRLINDLTAQRARLQteageysrQLDEK-DALVSQLSRSKQASTQQIEELkhqLEEETKAKNALAHALQSSR 1340
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQR--------RLKQQiFALSEVVQRRPHFSYEDAVGL---LGENSDLNEKLRARLEQAE 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1341 HDCDLLREQYEEEQEGKAELQRALSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLAQRLQEAEEHVEAVNAK 1413
Cdd:COG3096 998 EARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSR 1074
|
330
....*....|....*...
gi 153945790 1414 CASLEKTKQRLQNEVEDL 1431
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSL 1092
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1244-1887 |
2.09e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.88 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1244 AKGNLEKmcrsLEDQVSELKTKEEEQQRLIND----LTAQRARLQTEAGEYSRQ---LDEKDALVSQLSRSKQASTQQIE 1316
Cdd:PRK10246 196 ARTELEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSlnwLTRLDELQQEASRRQQALQQALA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1317 ELkhqleeeTKAKNALAhALQSSrHDCDLLREQYEEEQEGKAELQRALSKANS------EVAQWRTKYETDAIQRTEELE 1390
Cdd:PRK10246 272 AE-------EKAQPQLA-ALSLA-QPARQLRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAELQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1391 EAKKKLAQRLQEAE------EHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNA------------ACAALDK--KQR 1450
Cdd:PRK10246 343 AQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1451 NFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKnvyeeslDQLETLRRENKNLQQEISDLtEQIAEGGKQIHELE 1530
Cdd:PRK10246 423 PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV-KTICEQEARIKDLE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1531 KIKKQVEQEK-CEIQAALE----EAEASLEHEEGKILRIQLE--LNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQ-- 1601
Cdd:PRK10246 495 AQRAQLQAGQpCPLCGSTShpavEAYQALEPGVNQSRLDALEkeVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQee 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1602 STLDAEIRSRNDALRVKKKMEGDLN-------EMEIQLNHAN-RLA-----AESLRNYRNTQGILKETQLHLDDALRG-- 1666
Cdd:PRK10246 575 QALTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLLSqRHElqgqiAAHNQQIIQYQQQIEQRQQQLLTALAGya 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1667 ---QEDLKEQLAIVER------------RANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKK 1731
Cdd:PRK10246 655 ltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQ 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1732 KLENDVSQLQSEVEEVIQESRNAEEK---AKKAITDAAMMAEElkkeqdTSAHLERMKKNLEQtvkdlqhRLDEAEQLAL 1808
Cdd:PRK10246 735 TLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDEE------TLTQLEQLKQNLEN-------QRQQAQTLVT 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1809 KGGKKQIQKLEARVRELEG--EVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVdklqAKVKSYKRQAE 1886
Cdd:PRK10246 802 QTAQALAQHQQHRPDGLDLtvTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALM----QQIAQATQQVE 877
|
.
gi 153945790 1887 E 1887
Cdd:PRK10246 878 D 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1461-1681 |
2.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1461 QKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLetlrrenKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEK 1540
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1541 CEIQAALEEAEASLE------HEEGKILRIQLELNQVKSEvdrKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDA 1614
Cdd:COG4942 93 AELRAELEAQKEELAellralYRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1615 LRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRA 1681
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1255-1412 |
2.37e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1255 LEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAK--NAL 1332
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1333 AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNA 1412
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1201-1553 |
2.69e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1201 DSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQR 1280
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1281 ARLQTEAGEYS---RQLDEKDALVSQLSRSKQAS----TQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEE 1353
Cdd:pfam07888 118 DALLAQRAAHEariRELEEDIKTLTQRVLERETElermKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1354 QEGKAELQRALSKANSEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQEAEEHVEAVNAKCASLEKTKQRLQNEVED 1430
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1431 LMLDVERSNAACAALDKKQRNFDkvlSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEE----------------- 1493
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermereklevelgrekd 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1494 -SLDQLETLRRENKNL-------QQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEAS 1553
Cdd:pfam07888 354 cNRVQLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPD 421
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1480-1761 |
2.76e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1480 LSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEheeg 1559
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1560 kilriqlelnqvksEVDRKIAEKDEEIDQLKRNHTRVVETMQstldaeirsrndalrvkkkMEGDLNEMEIQLNHANrlA 1639
Cdd:COG4942 87 --------------ELEKEIAELRAELEAQKEELAELLRALY-------------------RLGRQPPLALLLSPED--F 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1640 AESLRNYRNTQGILKETQLHLddalrgqEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLL 1719
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQA-------EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 153945790 1720 HTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKA 1761
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1453-1642 |
2.93e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1453 DKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ------- 1525
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1526 -----------------------IHELEKIKKQVEQEKCEI------QAALEEAEASLEHEEGKILRIQLELNQVKSEVD 1576
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1577 RKIAEKDEEIDQLKRNHTRVVETMQStLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAES 1642
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1387-1852 |
3.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1387 EELEEAKKKLAQRLQEAEEHVEAVNAKcASLEKTKQRLQNEVEDLMLDVERSNAACAALD--KKQRNFDKVLSEWKQKYE 1464
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1465 EtqaeLEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKN-LQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEI 1543
Cdd:COG4717 150 E----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1544 QAALEEAEASLEHEEgkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEG 1623
Cdd:COG4717 226 EEELEQLENELEAAA---LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1624 DLNEMEiQLNHANRLAAESLRNYRNTQGILKETQL-HLDDALRGQEDLKEQLAIVERRANllQAEIEELwatleQTERSR 1702
Cdd:COG4717 303 EAEELQ-ALPALEELEEEELEELLAALGLPPDLSPeELLELLDRIEELQELLREAEELEE--ELQLEEL-----EQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1703 KIAEQELLDASERVQLLHtqntsLINTKKKLENDVSQLQSEVEEviqesRNAEEKAKKAITDAAMMAEELkkeQDTSAHL 1782
Cdd:COG4717 375 LLAEAGVEDEEELRAALE-----QAEEYQELKEELEELEEQLEE-----LLGELEELLEALDEEELEEEL---EELEEEL 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1783 ERMKKNLEQtvkdLQHRLDEAE-QLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKG---LRKHERRVKE 1852
Cdd:COG4717 442 EELEEELEE----LREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAlelLEEAREEYRE 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1004-1181 |
3.96e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1004 ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQEstmDMENDK 1076
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1077 QQLDEKLEKKEFEisNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEa 1156
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA- 156
|
170 180
....*....|....*....|....*
gi 153945790 1157 ggatsAQVELNKKREAEFQKLRRDL 1181
Cdd:COG1579 157 -----ELEELEAEREELAAKIPPEL 176
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1129-1324 |
5.22e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1129 RASRAKAEKQRSDLSRELEEISERLEEAGGA------------TSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALR 1196
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAAleefrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1197 KKHADSMAELGEQIDN--LQRVKQKLEKEKSELKMETDDLSSNAEAIskakgnlekmcRSLEDQVSELKTK-EEEQQRLI 1273
Cdd:COG3206 247 AQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDV-----------IALRAQIAALRAQlQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1274 NDLTAQRARLQTEAGEYSRQLDEKDALVSQLS----------RSKQASTQQIEELKHQLEE 1324
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPeleaelrrleREVEVARELYESLLQRLEE 376
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
843-1059 |
5.54e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 843 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELeekmvtllKEKN---DLQLQVQSEADSLADAEERCEQLIKNKIQLE 919
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEF--------RQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 920 AKIKEVTERAEEEEEINAELTAkkrklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdetiaklsk 997
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL--------- 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 998 eKKALQETHQQTLDDLQAEedkVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1059
Cdd:COG3206 304 -RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
1106-1549 |
6.54e-06 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 51.20 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1106 QLQKKIKELQARIEelgeeieaerasrakaeKQRSDLSRELEEISeRLEEAGGATSAQVELNKKREAEFQKLRRDLEEAt 1185
Cdd:pfam14817 81 ELQKEIERLRAEIS-----------------RLDKQLEARELELS-REEAERERALDEISDSRHRQLLLEAYDQQCEEA- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1186 lqheamvaalRKKHADSMAELGEQIDNLQRVKQKLEKEkselkMETDDLSSNAEAISkakgnlekmcrSLEDQVselktk 1265
Cdd:pfam14817 142 ----------RKILAEDHQRLQGQLQQLRDAARKAEKE-----VVFGDSKGSKSSVI-----------ALEPQV------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1266 EEEQQRLINDLTAQ-RARLQTEAGEYSrqLDEKDALVSQLSRSKQASTQQIEELKHQLeeetkAKNALAHALQ--SSRHd 1342
Cdd:pfam14817 190 LRDVREACELRAQFlQELLESSLKAYE--GSGIHMNRDQRRAVIQHWLSAVETLLTSH-----PPSHLLQALEhlAARE- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1343 cdllreqyeeeqegKAELQRALSKAN--SEVAQWRTKYETDAIQRTE-ELEEAKKKLAQRLQEAEEHVEAVNAKCASLEK 1419
Cdd:pfam14817 262 --------------KTAIQEETESLDvrADAEALRFRYESNHLLDVSsDESSDLPSVRQLLERQWAHVQQFLNELAETRS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1420 TKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEwkqkyEETQAELEASQKESRSLSTELFKVKNVYEESLDQLE 1499
Cdd:pfam14817 328 RCQQLQARLQGLKDEAELESLGIGDTSQNDSLLRQVLEL-----ELQAAGLAASRDTLRSECQQLNKLARERQEALRSLQ 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 153945790 1500 TlrrenknLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEE 1549
Cdd:pfam14817 403 K-------KWQRILDFRQLVSELQEQIRALIKGNSAAKAFLIRQPAEARE 445
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
849-1838 |
6.66e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 849 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMvtllkekNDlqlqvQSEADSLADAEERceqliKNKIQLEAKIKevter 928
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEIKNHY-------ND-----QINIDNIKDEDAK-----QNYDKSKEYIK----- 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 929 aeeeeeinaELTAKKRKLEDECSELKKDIDDLeltLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEkkalqethqq 1008
Cdd:TIGR01612 822 ---------TISIKEDEIFKIINEMKFMKDDF---LNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAE---------- 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1009 tlddlqAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLerakRKLEGDLKLAQ---ESTMDMENDKQQLDEKLEK 1085
Cdd:TIGR01612 880 ------ISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL----KKVDEYIKICEntkESIEKFHNKQNILKEILNK 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1086 --KEFEISNLISKIEDEQaVEIQLQKKIKELQarieelgeeIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1163
Cdd:TIGR01612 950 niDTIKESNLIEKSYKDK-FDNTLIDKINELD---------KAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYH 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1164 velnkkREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNL---------QRVKQKLE-------KEKSEL 1227
Cdd:TIGR01612 1020 ------QFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniellnKEILEEAEinitnfnEIKEKL 1093
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1228 KMET-DDLSSN-----AEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQ-----TEAGEYSRQLDE 1296
Cdd:TIGR01612 1094 KHYNfDDFGKEenikyADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEdvadkAISNDDPEEIEK 1173
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1297 K-DALVSQLSRSKQAsTQQIEELKHQLEEETKAKNALAHA----LQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEV 1371
Cdd:TIGR01612 1174 KiENIVTKIDKKKNI-YDEIKKLLNEIAEIEKDKTSLEEVkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDL 1252
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1372 aqwrtkyetDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldvERSnaacaaLDKKQRN 1451
Cdd:TIGR01612 1253 ---------DEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR---EKS------LKIIEDF 1314
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1452 FDKvlSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYeesldqlETLRREN-KNLQQEISDLTEQIAEGGKQIH-EL 1529
Cdd:TIGR01612 1315 SEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIY-------NILKLNKiKKIIDEVKEYTKEIEENNKNIKdEL 1385
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1530 EKIKKQVEQEKCEIqaALEEAEASLEHE------EGKILRIQLELNQVKSEVdrkiAEKDEEIDQLKRNHTRVVETMQST 1603
Cdd:TIGR01612 1386 DKSEKLIKKIKDDI--NLEECKSKIESTlddkdiDECIKKIKELKNHILSEE----SNIDTYFKNADENNENVLLLFKNI 1459
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1604 LDAEIRSRNdALRVKKK-----MEGDLNEMEIQLNHANRLAAESLRNYRNTQG---ILKETQLHLDDALR--GQEDLKEQ 1673
Cdd:TIGR01612 1460 EMADNKSQH-ILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFEQYKKDVTELLNkySALAIKNK 1538
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1674 LAIVERRANLLQAEIEELWA--TLEQTERSRKIAE--QELLDASERVQLLHTQNTSLINTKKKLEN------DVSQLQSE 1743
Cdd:TIGR01612 1539 FAKTKKDSEIIIKEIKDAHKkfILEAEKSEQKIKEikKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKK 1618
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1744 VEEVIQESRNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeqlalkggKKQIQKLEARVR 1823
Cdd:TIGR01612 1619 INDCLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIE 1684
|
1050
....*....|....*
gi 153945790 1824 ELEGEVeNEQKRNAE 1838
Cdd:TIGR01612 1685 KIEIDV-DQHKKNYE 1698
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1282-1805 |
7.20e-06 |
|
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: 50.80 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1282 RLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEeetKAKNALAHALQssrhDCDLLREQYEEEQEGKAELQ 1361
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE---RAQTEEAQAKQ----DSELAKLRVEEMEQGIADEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1362 RALSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLAQRLQE---AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVER 1437
Cdd:pfam05701 119 SVAAKAQLEVAKARhAAAVAELKSVKEELESLRKEYASLVSErdiAIKRAEEAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1438 SNAACaaLDKKQRNFDKVLSeWKQKYEETQAELEASQKESRSLSTELFKVKNVYEEsldqLETLRRENKNLQQEISDLTE 1517
Cdd:pfam05701 199 AHAAH--LEAEEHRIGAALA-REQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSK----LETASALLLDLKAELAAYME 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1518 -QIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEH--EEGKILRIQLElnQVKSEVDRKIAEKDEeidqlkrnhT 1594
Cdd:pfam05701 272 sKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKakDEVNCLRVAAA--SLRSELEKEKAELAS---------L 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1595 RVVETMQST----LDAEIRSRNDALRVKKKMEGDLNEMEI----QLNHANRLAAESLRNYRNTQGILKETQLHLDDAlrg 1666
Cdd:pfam05701 341 RQREGMASIavssLEAELNRTKSEIALVQAKEKEAREKMVelpkQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQA--- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1667 qedlKEQLAIVERRANLLQAEIEELWAtleqterSRKIAeqelLDASErvQLLHTQNTSLINTKKKLENDVSQLQSEVEE 1746
Cdd:pfam05701 418 ----KAAASTVESRLEAVLKEIEAAKA-------SEKLA----LAAIK--ALQESESSAESTNQEDSPRGVTLSLEEYYE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1747 VIQESRNAEEKAKKAITDAAMMAEELKKEQDTS-AHLERMKKNLEQTVKDLQHRLDEAEQ 1805
Cdd:pfam05701 481 LSKRAHEAEELANKRVAEAVSQIEEAKESELRSlEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1167-1936 |
8.72e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1167 NKKREAEFQKLrrdLEEATlqheAMVAALRKKHADSMAELGEQIDNLQRvkqklekekselkmetdDLSSNAEAISKAKG 1246
Cdd:PRK04863 252 TQSDRDLFKHL---ITEST----NYVAADYMRHANERRVHLEEALELRR-----------------ELYTSRRQLAAEQY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1247 NLEKMCRSLEDQVSELKTKEEEQQRLINDLT-AQRARLQTEAGE-YSRQLDEK-DALVSQLSRSKQASTQQI--EELKHQ 1321
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLNlVQTALRQQEKIErYQADLEELeERLEEQNEVVEEADEQQEenEARAEA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1322 LEEETK-AKNALAHALQSsrhdCDLLREQYEEEQEGKAELQRA--------LSKANseVAQWRTKYETDAIQRTEELEEa 1392
Cdd:PRK04863 388 AEEEVDeLKSQLADYQQA----LDVQQTRAIQYQQAVQALERAkqlcglpdLTADN--AEDWLEEFQAKEQEATEELLS- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1393 kkkLAQRLQEAEEHVEAVnAKCASLektkqrlqneVEDLMLDVERSNAACAALDK-----KQRNFDKVLSEWKQKYEETQ 1467
Cdd:PRK04863 461 ---LEQKLSVAQAAHSQF-EQAYQL----------VRKIAGEVSRSEAWDVARELlrrlrEQRHLAEQLQQLRMRLSELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1468 AELEASQKESRSLsTELFKVKNVYEESLDQLETLRREnknLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEI---- 1543
Cdd:PRK04863 527 QRLRQQQRAERLL-AEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLaara 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1544 ------QAALE-------EAEASLEHEEGKILRIQL---ELNQVKSEVDRKIAEKDEEIDQLKRNHT-------RVVETM 1600
Cdd:PRK04863 603 pawlaaQDALArlreqsgEEFEDSQDVTEYMQQLLErerELTVERDELAARKQALDEEIERLSQPGGsedprlnALAERF 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1601 QSTLDAEIRSR----------------------NDALRVKKKMEGD--------LNEMEIQLNHANRLAAESLRNyrntq 1650
Cdd:PRK04863 683 GGVLLSEIYDDvsledapyfsalygparhaivvPDLSDAAEQLAGLedcpedlyLIEGDPDSFDDSVFSVEELEK----- 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1651 GILKETQlhlDDALRGQEDLKEQL---AIVERRANLLQAEIEEL---WATLEqtERSRKIaeQELLDASERVQLLHT--- 1721
Cdd:PRK04863 758 AVVVKIA---DRQWRYSRFPEVPLfgrAAREKRIEQLRAEREELaerYATLS--FDVQKL--QRLHQAFSRFIGSHLava 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1722 ------QNTSLINTKK-KLENDVSQLQSEveevIQESRNAEEKAKKAITDAAMMAEELKKEQDTSahlermkknLEQTVK 1794
Cdd:PRK04863 831 feadpeAELRQLNRRRvELERALADHESQ----EQQQRSQLEQAKEGLSALNRLLPRLNLLADET---------LADRVE 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1795 DLQHRLDEAEQLA--LKGGKKQIQKLE---ARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTE-------EDRK 1862
Cdd:PRK04863 898 EIREQLDEAEEAKrfVQQHGNALAQLEpivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyEDAA 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1863 NVL-RLQDLVDKLQAKVKSYKRQAEEAEE---QSNANL-----------SKFRKLQHELEEAEERAD-----IAESQVNK 1922
Cdd:PRK04863 978 EMLaKNSDLNEKLRQRLEQAEQERTRAREqlrQAQAQLaqynqvlaslkSSYDAKRQMLQELKQELQdlgvpADSGAEER 1057
|
890
....*....|....
gi 153945790 1923 LRVKSREVHTKISA 1936
Cdd:PRK04863 1058 ARARRDELHARLSA 1071
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1730-1893 |
9.06e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1730 KKKLENDVSQLQSEVEEVIQESRN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMK-KNLEQTVKDLQHRLDEAEQLA 1807
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1808 lkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQAKVKSYKRQAE- 1886
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL-LEKVEEEARHEAAVLIKEIEe 180
|
....*..
gi 153945790 1887 EAEEQSN 1893
Cdd:PRK12704 181 EAKEEAD 187
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1351-1471 |
1.08e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1351 EEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqeaeehVEAVNAKCASLEKTKQRLQNEVED 1430
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 153945790 1431 lmldversnaacaaLDKKQRNFDKVLSEWKQKYEETQAELE 1471
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1343-1558 |
1.12e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1343 CDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQ 1422
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1423 RLQNEVEDLM----LDVE------RSNAACAALDKKQRNFDKVLSEWKQKYEEtqaelEASQKESRSLSTeLFKVKNVYE 1492
Cdd:PRK05771 118 ELEQEIERLEpwgnFDLDlslllgFKYVSVFVGTVPEDKLEELKLESDVENVE-----YISTDKGYVYVV-VVVLKELSD 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1493 ESLDQLETLRRENKNL------QQEISDLTEQIAEGGKQIHEL-EKIKKQVEQEKCEIQAALEEAEASLEHEE 1558
Cdd:PRK05771 192 EVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLlEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
946-1234 |
1.29e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 946 LEDECSELKKDIDDLELTLAKVEkEKHATENKvkNLTEEMAGLDETIAklskEKKALQETHQQTLDDLQAEEDKvniLTK 1025
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNK--NIEEQRKKNGENIA----RKQNKYDELVEEAKTIKAEIEE---LTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1026 AKTKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEgdlKLAQESTMDMEND-----KQQLDEKLEKkefeisnlISKIEDE 1100
Cdd:PHA02562 242 ELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEGPDR--------ITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1101 QAveiQLQKKIKELQARIEELgeeieaerasrAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLrrd 1180
Cdd:PHA02562 308 LK---ELQHSLEKLDTAIDEL-----------EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL--- 370
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1181 leeatlqheamvAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDL 1234
Cdd:PHA02562 371 ------------QAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
983-1865 |
1.44e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 983 EEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNIL---TKAKTKLEQQVDDLEgsleqekklrmdlerakrKLE 1059
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVqtaLRQQEKIERYQEDLE------------------ELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1060 GDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIED-EQAVEIQLQKKIKELQARieelgeeieaERASRAKAEKQ 1138
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyQQALDVQQTRAIQYQQAV----------QALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1139 RSDLSreLEEISERLEEAggATSAQVELNKKREAEfQKLRrDLEEATLQHEAMVAALRK-------KHADSMA-ELGEQI 1210
Cdd:COG3096 431 LPDLT--PENAEDYLAAF--RAKEQQATEEVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1211 DNLQRVKQKLEkeksELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLindlTAQRARLQTEAGEY 1290
Cdd:COG3096 505 RSQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL----EAQLEELEEQAAEA 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1291 SRQLdekdalvSQLSRSKQASTQQIEELKHQLEEETKAKNALAHAlqssrhdCDLLREQYEEEQEGKAELQRALSKansE 1370
Cdd:COG3096 577 VEQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALERL-------REQSGEALADSQEVTAAMQQLLER---E 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1371 VAQWRTKYEtdAIQRTEELEEAKKKLAQ-------RLQEAEEHVEAVnakcaslektkqrLQNEVEDlmlDVERSNAA-C 1442
Cdd:COG3096 640 REATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGV-------------LLSEIYD---DVTLEDAPyF 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1443 AALDKKQRNFDKV--LSEWK---QKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLE--TLR------------- 1502
Cdd:COG3096 702 SALYGPARHAIVVpdLSAVKeqlAGLEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSdrQWRysrfpevplfgra 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1503 -RENK--NLQQEISDLTEQIAEGGKQIHELEKIKKQVEQ----------------EKCEIQAALEEAEASLEHEEGKILR 1563
Cdd:COG3096 782 aREKRleELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQ 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1564 IQLELNQVKSEVD--RKIA----------------EKDEEIDQLK---------RNHTRVVETMQSTLDAEIRSrNDALR 1616
Cdd:COG3096 862 LRQQLDQLKEQLQllNKLLpqanlladetladrleELREELDAAQeaqafiqqhGKALAQLEPLVAVLQSDPEQ-FEQLQ 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1617 VkkkmegDLNEMEIQLNHAnRLAAESLR---------NYRNTQGILKETQlhlddalrgqeDLKEQLaiverRANLLQAE 1687
Cdd:COG3096 941 A------DYLQAKEQQRRL-KQQIFALSevvqrrphfSYEDAVGLLGENS-----------DLNEKL-----RARLEQAE 997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1688 ieelwatlEQTERSRKIAEQELLDASERVQLLHTQNTSLiNTKKKLendVSQLQSEVEEV-IQESRNAEEKAKkaitdaa 1766
Cdd:COG3096 998 --------EARREAREQLRQAQAQYSQYNQVLASLKSSR-DAKQQT---LQELEQELEELgVQADAEAEERAR------- 1058
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1767 mmaeELKKEQDTSAHLERMKKNleQTVKDLQHRLDEAEQLAlkggkKQIQKLEARVRELEGEVENeQKRNAEAVKGLRKH 1846
Cdd:COG3096 1059 ----IRRDELHEELSQNRSRRS--QLEKQLTRCEAEMDSLQ-----KRLRKAERDYKQEREQVVQ-AKAGWCAVLRLARD 1126
|
970 980
....*....|....*....|....
gi 153945790 1847 ---ERRV--KELTYQTEEDRKNVL 1865
Cdd:COG3096 1127 ndvERRLhrRELAYLSADELRSMS 1150
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1208-1638 |
1.46e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1208 EQIDNLQRVKQKLEKEKSELkmetddlsSNAEA-ISKAKGNLEKMCRSLEDQVSELKTK---EEEQQRLiNDLTAQRARL 1283
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQL--------AQAPAkLRQAQAELEALKDDNDEETRETLSTlslRQLESRL-AQTLDQLQNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1284 QTEAGEYSRQLdekdalVSQLSRSKQAST------QQIEELKHQLEEETKAKNALAHALQssrhdcdllrEQYEEEQ--- 1354
Cdd:PRK11281 141 QNDLAEYNSQL------VSLQTQPERAQAalyansQRLQQIRNLLKGGKVGGKALRPSQR----------VLLQAEQall 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1355 EGKAELQRALSKANS---EVAQWRTKYETDAIQRTEeleeakkKLAQRLQEAeehveaVNAKCASL-EKTKQRLQNeved 1430
Cdd:PRK11281 205 NAQNDLQRKSLEGNTqlqDLLQKQRDYLTARIQRLE-------HQLQLLQEA------INSKRLTLsEKTVQEAQS---- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1431 lmldVERSNAACA-ALDKKQRNFDKVLSewkqkyeetQAELEASQKeSRSLSTELFKVKNvyeesldQLETLRRENKNL- 1508
Cdd:PRK11281 268 ----QDEAARIQAnPLVAQELEINLQLS---------QRLLKATEK-LNTLTQQNLRVKN-------WLDRLTQSERNIk 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1509 -----------------QQ--------EISDLTEQIAEggkqihelekikkqveqekceiqaaleeaeasleheegkiLR 1563
Cdd:PRK11281 327 eqisvlkgslllsrilyQQqqalpsadLIEGLADRIAD----------------------------------------LR 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1564 I-QLELNQVKSevdrKIAEKDEEIDQLKRNHTRVVEtmqstlDAEIRSRNDALRVKKKMEGDLN-EMEIQLNHANRL 1638
Cdd:PRK11281 367 LeQFEINQQRD----ALFQPDAYIDKLEAGHKSEVT------DEVRDALLQLLDERRELLDQLNkQLNNQLNLAINL 433
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1014-1285 |
1.59e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1014 QAEEDKVNILTKAKTKLEQQVDDLEGSLEQ-EKKLRmdlerakrklegdlklaqestmdmendkqqldeklekkEFEISN 1092
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALE--------------------------------------EFRQKN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1093 LISKIEDEQAVEIQlqkKIKELQARIeelgeeieaerasrAKAEKQRSDLSRELEEISERLEEAGGATSAQVElnkkrEA 1172
Cdd:COG3206 206 GLVDLSEEAKLLLQ---QLSELESQL--------------AEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1173 EFQKLRRDLEEATLQHEAMVAALRKKHADsMAELGEQIDNLQRVKQKlekeksELKMETDDLSSNAEAISKAKGNLEKMC 1252
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPD-VIALRAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQL 336
|
250 260 270
....*....|....*....|....*....|...
gi 153945790 1253 RSLEDQVSELKTKEEEQQRLINDLTAQRARLQT 1285
Cdd:COG3206 337 AQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1389-1599 |
1.96e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1389 LEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcaaldkkqrnfdkvLSEWKQKYEETQA 1468
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA--------------LNKLNTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1469 ELEASQKESRSLS--TELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEqekcEIQAA 1546
Cdd:PHA02562 270 KIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNK 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1547 LEEAEASLEHEEGKILRIQLELNQVKSEVdrkiAEKDEEIDQLKRNHTRVVET 1599
Cdd:PHA02562 346 ISTNKQSLITLVDKAKKVKAAIEELQAEF----VDNAEELAKLQDELDKIVKT 394
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1602-1929 |
2.08e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1602 STLDAEIRSRNDALRVKKKMEGDLNEMEiqlnhaNRLAAESLRNYR--NTQGILKETQ---LHLDDA-LRGQEDLKEQLA 1675
Cdd:PLN02939 90 STSSDDDHNRASMQRDEAIAAIDNEQQT------NSKDGEQLSDFQleDLVGMIQNAEkniLLLNQArLQALEDLEKILT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1676 ivERRAnlLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQEsrNAE 1755
Cdd:PLN02939 164 --EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE--NML 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1756 EKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENE 1832
Cdd:PLN02939 238 LKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1833 QKRNAEAVKGLRKH---ERRVKELTYQTEEdrKNVLRLQ-DLVDKLQAKVKSykrqAEEAEEQSNANLSKFRKLQHELee 1908
Cdd:PLN02939 313 TNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKL----LEERLQASDHEIHSYIQLYQES-- 384
|
330 340
....*....|....*....|.
gi 153945790 1909 AEERADIAESQVNKLRVKSRE 1929
Cdd:PLN02939 385 IKEFQDTLSKLKEESKKRSLE 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1533-1771 |
2.21e-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: 48.99 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1533 KKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVksevDRKIAEKDEEIDQLkrnhtrvvETMQSTLDAEIRSRN 1612
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRAL--------EQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1613 DALrvkKKMEGDLNEMEIQLnhANRLAAeSLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELW 1692
Cdd:COG4942 90 KEI---AELRAELEAQKEEL--AELLRA-LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1693 ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEE 1771
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1498-1909 |
2.25e-05 |
|
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: 49.84 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1498 LETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR 1577
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1578 KIAEKDEEIDQLKRNHTRV----VETMQSTLDAEIRSRNDALRVKKKMEGDL-NEMEIQLNHANRLAAESLRNYRNTQGI 1652
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFldadIETAAADQEQLPSWQSELENLEERLKALTgKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1653 lketqlhlDDALRGQEDLKEQLAIVERraNLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1732
Cdd:pfam12128 396 --------KDKLAKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1733 LENDVSQLQSEVEEviQESRNAE-EKAKKAITDAAMMAEE-LKKEQDTSAHLERMKKNLEQtvkdLQHRLDEAEQLALK- 1809
Cdd:pfam12128 466 LENFDERIERAREE--QEAANAEvERLQSELRQARKRRDQaSEALRQASRRLEERQSALDE----LELQLFPQAGTLLHf 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1810 ------GGKKQIQKLEARVR----ELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDrknvlRLQDLVDKLQAKVK 1879
Cdd:pfam12128 540 lrkeapDWEQSIGKVISPELlhrtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE-----ELRERLDKAEEALQ 614
|
410 420 430
....*....|....*....|....*....|
gi 153945790 1880 SYKRQAEEAEEQSNANLSKFRKLQHELEEA 1909
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFA 644
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1509-1789 |
2.29e-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: 48.99 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1509 QQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQ 1588
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1589 LKRNHTRVVETMQSTLDAEIRSrndalrvkkkmeGDLNEMEIQLNHANrlAAESLRNYRNTQGILKETQLHLddalrgqE 1668
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRL------------GRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQA-------E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1669 DLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQElldaservqllhtqntslINTKKKLENDVSQLQSEVEEVI 1748
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEAL------------------KAERQKLLARLEKELAELAAEL 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 153945790 1749 QESRNAEEKAKKAItDAAMMAEELKKEQDTSAHLERMKKNL 1789
Cdd:COG4942 216 AELQQEAEELEALI-ARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
998-1406 |
2.47e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.30 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESTMDMENDKQ 1077
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLE----QLQEENFRLETARD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1078 QLDEKLEKKEFEISNLISKIEDEQ--AVEIQ-LQKKIKELQARIEELGEEIEAERASRAKAEkQRSDLSRELEEISER-- 1152
Cdd:pfam05622 84 DYRIKCEELEKEVLELQHRNEELTslAEEAQaLKDEMDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKLLEERna 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1153 --------LEEA---GGATSAQVELNKKreaEFQKLRRDLEEATLQHEAMVAALRKKHadsmaelgEQIDNLQRVKQKLE 1221
Cdd:pfam05622 163 eymqrtlqLEEElkkANALRGQLETYKR---QVQELHGKLSEESKKADKLEFEYKKLE--------EKLEALQKEKERLI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1222 KEKSELKMETDDL---SSNAEAISKAKGNLEKMCRSLEDQVSELKTKE--EEQQRLIND----LTAQRARLQTEAGEYSR 1292
Cdd:pfam05622 232 IERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRLQHEnkmlRLGQEGSYRERLTELQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1293 QLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAhalqSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVA 1372
Cdd:pfam05622 312 LLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIE 387
|
410 420 430
....*....|....*....|....*....|....
gi 153945790 1373 QWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEH 1406
Cdd:pfam05622 388 ELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1256-1483 |
2.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1256 EDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHA 1335
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1336 LQSSRHDCDLLrEQYEEEQE-----GKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAV 1410
Cdd:COG3883 95 LYRSGGSVSYL-DVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1411 NAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTE 1483
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1099-1794 |
2.80e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1099 DEQAVEIQL-QKKIKELQARIeelgeeieaerasrakaEKQRSDLSRELEEISERLEEAGGATsaqveLNKKREAEFQKL 1177
Cdd:pfam10174 126 ERQAKELFLlRKTLEEMELRI-----------------ETQKQTLGARDESIKKLLEMLQSKG-----LPKKSGEEDWER 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1178 RRDLEEATLQHEAMVAALRKKHADSMAelgeqidnlQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLED 1257
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKENIH---------LREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLED 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1258 QVSELKTK----EEEQQRLINDLTAQRAR---LQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLE---EETK 1327
Cdd:pfam10174 255 EVQMLKTNgllhTEDREEEIKQMEVYKSHskfMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkESLT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1328 AKNALAHALQSsrhDCDLLREQYEEEqegkaelQRALSKansevaqwrtkyETDAIQRteeLEEAKKKLAQRLQEAEEHV 1407
Cdd:pfam10174 335 AKEQRAAILQT---EVDALRLRLEEK-------ESFLNK------------KTKQLQD---LTEEKSTLAGEIRDLKDML 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1408 EAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELfkv 1487
Cdd:pfam10174 390 DVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRER--- 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1488 knvyeesLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEH--EEGKILRIQ 1565
Cdd:pfam10174 467 -------LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQ 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1566 LELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVE---TMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAES 1642
Cdd:pfam10174 540 LKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKK 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1643 LRNYRNTQGILKETQLHLDDALRGQEDlkeqlaivERRANLLQAEIEELWATLEQTERSRKIAEQELldaSERVQLLHTQ 1722
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQLLEEARRRED--------NLADNSQQLQLEELMGALEKTRQELDATKARL---SSTQQSLAEK 688
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1723 NTSLINTK----KKLEndvsqlqsEVEEVIQESRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVK 1794
Cdd:pfam10174 689 DGHLTNLRaerrKQLE--------EILEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
855-1422 |
2.90e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 855 MKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERceqlIKNKIQLEAKIKEVTERAEEEEE 934
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSA----LNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 935 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLskekkalqETHQQTLDDLQ 1014
Cdd:PRK01156 264 DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKY--------HAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1015 AEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlklaqESTMDMENDKQQLDEKLEKKEFEISNLI 1094
Cdd:PRK01156 336 KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE-------EYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1095 SKIEDEQAVEIQLQKKIKELQARIeelgeeieaeRASRAKAEkqrsdlsrELEEISERLEEAG-----GATSAQVELNKK 1169
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRI----------RALRENLD--------ELSRNMEMLNGQSvcpvcGTTLGEEKSNHI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1170 REAEFQKLRRdLEEATLQHEAMVAAL--RKKHADSMAEL--GEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAK 1245
Cdd:PRK01156 471 INHYNEKKSR-LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1246 gnlekmcrSLEDQVSELKTKEEEQQRL-INDLTAQRA-----RLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELK 1319
Cdd:PRK01156 550 --------EIKNRYKSLKLEDLDSKRTsWLNALAVISlidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1320 HQLEEETKAKNALAHALQSSRHDCDLLREQ---YEEEQEGKAELQRALSKANSEVAQWRT--KYETDAIQRTE----ELE 1390
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKidnYKKQIAEIDSIIPDLKEITSRINDIEDnlKKSRKALDDAKanraRLE 701
|
570 580 590
....*....|....*....|....*....|..
gi 153945790 1391 EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQ 1422
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1536-1933 |
2.96e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1536 VEQEKCEIQAALEEAEASLEHEEGKILRIQL-ELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQS---------TLD 1605
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerreeleTLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1606 AEIRSRNDALRVKKKMEGDLNEmEIQlnhANRLAAESLRNYRNtqGILKETQLhlDDAlrGQEDLKEQLAIVERRANLLQ 1685
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAE-EVR---DLRERLEELEEERD--DLLAEAGL--DDA--DAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1686 AEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDA 1765
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1766 AMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLaLKGGKkqiqklearVRELEGEVENeqkrnAEAVKGLRK 1845
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGK---------CPECGQPVEG-----SPHVETIEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1846 HERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNanlskfrkLQHELEEAEERADIAESQVNKLRV 1925
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED--------LEELIAERRETIEEKRERAEELRE 544
|
....*...
gi 153945790 1926 KSREVHTK 1933
Cdd:PRK02224 545 RAAELEAE 552
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
998-1601 |
3.55e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.05 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQTLDDLQAEEDKVNILTKAKTKL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDME 1073
Cdd:pfam10174 68 ENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSpvdgEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1074 NDKQQL---DEKLEK-------------KEFEISNLISKIEDEQA----VEIQLQKKIKELQArieelgEEIEAERASRA 1133
Cdd:pfam10174 148 TQKQTLgarDESIKKllemlqskglpkkSGEEDWERTRRIAEAEMqlghLEVLLDQKEKENIH------LREELHRRNQL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1134 KAEkqrsdlSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALR--KKHADSMAELGEQid 1211
Cdd:pfam10174 222 QPD------PAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvyKSHSKFMKNKIDQ-- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1212 nlqrVKQKLEKEKSEL-----KMET--DDLSSNAEAISKAKGNL---EKMCRSLEDQVSELKTKEEEQQRLINDLTAQRA 1281
Cdd:pfam10174 294 ----LKQELSKKESELlalqtKLETltNQNSDCKQHIEVLKESLtakEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1282 RLQTEAGEYSRQL-DEKDALVSQlSRSKQASTQQIEELKHQLEEETKAKNALAHALQSsrhdcdlLREQYEEEQEGKAEL 1360
Cdd:pfam10174 370 DLTEEKSTLAGEIrDLKDMLDVK-ERKINVLQKKIENLQEQLRDKDKQLAGLKERVKS-------LQTDSSNTDTALTTL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1361 QRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKlaqrLQEAEEHVEAVnakcaslektkQRLQNEVEDLMLDVERSNA 1440
Cdd:pfam10174 442 EEALSEKERIIERLKEQREREDRERLEELESLKKE----NKDLKEKVSAL-----------QPELTEKESSLIDLKEHAS 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1441 ACAALDKKQRNFDKVLsewkqkyeetQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRREnKNLQQEISDLTEQIA 1520
Cdd:pfam10174 507 SLASSGLKKDSKLKSL----------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARYKEESG 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1521 EGGKQIHELEKIKKQVEQEKCEIQAALEEAE--ASLEHEEGKILRIQLELNQvkSEVDRKIAEKDEEIDQLKRNHTRVVE 1598
Cdd:pfam10174 576 KAQAEVERLLGILREVENEKNDKDKKIAELEslTLRQMKEQNKKVANIKHGQ--QEMKKKGAQLLEEARRREDNLADNSQ 653
|
...
gi 153945790 1599 TMQ 1601
Cdd:pfam10174 654 QLQ 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-1046 |
3.93e-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: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 856 KEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEI 935
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 936 NAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 990
Cdd:COG4942 106 LAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 991 TIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKK 1046
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1314-1554 |
4.11e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 47.41 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1314 QIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEgkaELQRALSKAnsevaQWRTKYETDAIQRTEELEEAK 1393
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAKA-----QQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1394 KKLAQRLQEAEEHVEAVNAKCASL-EKTKQRLQNEVEDLMLDVERSNaacaaLDKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1473 SQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTeqiAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEA 1552
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 153945790 1553 SL 1554
Cdd:pfam06008 244 SL 245
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1145-1482 |
4.12e-05 |
|
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: 48.75 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1145 ELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAA--------LRKKHADSMAELGEQIDNLQ-R 1215
Cdd:pfam15964 221 ELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAstssrvggLCLKCAQHEAVLAQTHTNVHmQ 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1216 VKQKLEKEKSELKMETDDL-SSNAEAISKAKGNLEKMCRSLE--DQVSELKTKEEEQ-QRLINDLTAQRARLQTE-AGEY 1290
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVrSSLAEAQQRESSAYEQVKQAVQmtEEANFEKTKALIQcEQLKSELERQKERLEKElASQQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1291 SRQLDEKDALVSQLSRSKQ-------ASTQQIEELKHQLEEETKAKNALAHALQSSRHDcdlLREQYEEEQEGKAELQRA 1363
Cdd:pfam15964 381 EKRAQEKEALRKEMKKEREelgatmlALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQ---LASQEMDVTKVCGEMRYQ 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1364 LSKAN-------SEVAQWRTKYETDAIQRTEELEEAKKKLA---QRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLML 1433
Cdd:pfam15964 458 LNQTKmkkdeaeKEHREYRTKTGRQLEIKDQEIEKLGLELSeskQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL 537
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1434 DVERS------NAACAALDKKQRNfdkvlSEWKQKYEETQAELEASQKESRSLST 1482
Cdd:pfam15964 538 EKESIqqsfsnEAKAQALQAQQRE-----QELTQKMQQMEAQHDKTVNEQYSLLT 587
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1194-1936 |
4.31e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1194 ALRKKHAD--SMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNL----------EKMCRSLEDQVSE 1261
Cdd:TIGR00606 170 ALKQKFDEifSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItskeaqlessREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1262 LKtkeeEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKaknalahalqssrh 1341
Cdd:TIGR00606 250 LK----NRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ-------------- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1342 dcdllREQYEEEQEgKAELQRALSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEkTK 1421
Cdd:TIGR00606 312 -----RTVREKERE-LVDCQRELEKLNKERRLLN--------QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA-TR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1422 QRLQNEVEDLMLDVERSNA---ACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQL 1498
Cdd:TIGR00606 377 LELDGFERGPFSERQIKNFhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1499 ETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEkceiqaALEEAEASLEHEEGKILRIQLELNQVKSEVD-- 1576
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTE------TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhh 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1577 -----------RKIAEKDEEIDQLKRNH-------------TRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQL 1632
Cdd:TIGR00606 531 tttrtqmemltKDKMDKDEQIRKIKSRHsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHI 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1633 NHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKE---QLAIVERRANLLQAEIEELWATLEQTERSRKIAEQEL 1709
Cdd:TIGR00606 611 NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKsskQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1710 LDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQEsrnAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL 1789
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL---APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1790 EQTVKDLQHRLDEAEQlalkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHErrvKELTYQteEDRKNVLRLQD 1869
Cdd:TIGR00606 768 EEQETLLGTIMPEEES------AKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD---LDRTVQ--QVNQEKQEKQH 836
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1870 LVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISA 1936
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE 903
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1349-1553 |
4.58e-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: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1349 QYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEV 1428
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1429 EDLMLDVERSNAACAALDK--KQRNFDKVLSEWK-------------QKYEETQAELEASQKESRSLSTELFKVKNVYEE 1493
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1494 SLDQLETLRRENknlQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEAS 1553
Cdd:COG3883 169 AKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1129-1431 |
4.95e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1129 RASRAKAEKQRSDLSRELEEISER---LEEAGGATSAQveLNKKREAEFQ--KLRR---DLEEATLQHEAMVAALrkkha 1200
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSAResdLEQDYQAASDH--LNLVQTALRQqeKIERyqeDLEELTERLEEQEEVV----- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1201 dsmAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAE-----AIS-----KAKGNLEKMCR-------SLEDQVSELK 1263
Cdd:COG3096 371 ---EEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtrAIQyqqavQALEKARALCGlpdltpeNAEDYLAAFR 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1264 TKEEEQQRLINDLtAQRARLQTEA-GEYSRQLDEKDALVSQLSRSK--QASTQQIE---ELKHQLEEETKAKNALAHAlq 1337
Cdd:COG3096 448 AKEQQATEEVLEL-EQKLSVADAArRQFEKAYELVCKIAGEVERSQawQTARELLRryrSQQALAQRLQQLRAQLAEL-- 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1338 ssrhdcdllrEQYEEEQEGKAELQRALSKansevaqwRTKYETDAiqrTEELEEAKKKLAQRLQEAEEHVEAVNAKCASL 1417
Cdd:COG3096 525 ----------EQRLRQQQNAERLLEEFCQ--------RIGQQLDA---AEELEELLAELEAQLEELEEQAAEAVEQRSEL 583
|
330
....*....|....
gi 153945790 1418 EKTKQRLQNEVEDL 1431
Cdd:COG3096 584 RQQLEQLRARIKEL 597
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
963-1165 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 963 TLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLE 1042
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1043 ------QEKKLRMD--------------LERAKRklegdLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQA 1102
Cdd:COG3883 90 eraralYRSGGSVSyldvllgsesfsdfLDRLSA-----LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1103 veiQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVE 1165
Cdd:COG3883 165 ---ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
850-1636 |
5.03e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 850 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQliKNKIQ--------LEAK 921
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIEryqadleeLEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 922 IKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKE 970
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 971 KHATENKVKNLTEEMAGLDETI----AKLSKEKKALQ------------ETHQQTLDDL-QAEEDKvnILTKAKTKLEQQ 1033
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLsvaqAAHSQFEQAYQlvrkiagevsrsEAWDVARELLrRLREQR--HLAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1034 VDDLEGSLEQEKklrmDLERAKRKLEGDLKLaqestmdMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKE 1113
Cdd:PRK04863 522 LSELEQRLRQQQ----RAERLLAEFCKRLGK-------NLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1114 LQARIEELGEEIEAERASRAKAEKqrsdlsreLEEIS-ERLEEAGGATSA-QVELNKKREAEFQklrRDLEEATLQheam 1191
Cdd:PRK04863 591 LQARIQRLAARAPAWLAAQDALAR--------LREQSgEEFEDSQDVTEYmQQLLERERELTVE---RDELAARKQ---- 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1192 vaalrkkhadsmaELGEQIDNLQ--------RVKQKLEKEKSELKMET-DDLS-SNAEAISKAKGNLekMCRSLEDQVSE 1261
Cdd:PRK04863 656 -------------ALDEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDVSlEDAPYFSALYGPA--RHAIVVPDLSD 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1262 LKTKEEEQQRLINDLTAQRARLQT-EAGEYSRQLDEKDALV------SQLSR-------SKQASTQQIEELKHQLEEETk 1327
Cdd:PRK04863 721 AAEQLAGLEDCPEDLYLIEGDPDSfDDSVFSVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELA- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1328 aknalahalqssrhdcdllrEQYEEEQEGKAELQRALSKANSEVA-------QWRTKYETDAIQRT--------EELEEA 1392
Cdd:PRK04863 800 --------------------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRrveleralADHESQ 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1393 KKKLAQRLQEAEEHVEAVNaKCASLEKTKQR--LQNEVEDLMLDVERSNAACAALDKKQRNFDK------VLSEWKQKYE 1464
Cdd:PRK04863 860 EQQQRSQLEQAKEGLSALN-RLLPRLNLLADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQlepivsVLQSDPEQFE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1465 ETQAELEASQKESRSLSTELFKVKNV--------YEESLDQL-------ETLRRENKNLQQEISDLTEQIAEGGKQIHEl 1529
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVvqrrahfsYEDAAEMLaknsdlnEKLRQRLEQAEQERTRAREQLRQAQAQLAQ- 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1530 ekiKKQVEQE-KCEIQAALEE-AEASLEHEEgkilriqLELNQVKSEVDRKIAEKDEEIDQLKRNHTRV--VETMQSTLD 1605
Cdd:PRK04863 1018 ---YNQVLASlKSSYDAKRQMlQELKQELQD-------LGVPADSGAEERARARRDELHARLSANRSRRnqLEKQLTFCE 1087
|
890 900 910
....*....|....*....|....*....|.
gi 153945790 1606 AEIRSRNDALRvkkKMEGDLNEMEIQLNHAN 1636
Cdd:PRK04863 1088 AEMDNLTKKLR---KLERDYHEMREQVVNAK 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1735-1936 |
5.10e-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: 47.84 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1735 NDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQ 1814
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------KE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1815 IQKLEARVRELEGEVEN------------------EQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQA 1876
Cdd:COG4942 92 IAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1877 KVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISA 1936
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
857-1087 |
5.62e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 48.23 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 857 EEFQKTKDELAKSEAKRKELEEKMVTLLKEK--NDLQLQVQSEADSLADaeerceqliknkiQLEAKIKEVTERAEEEEE 934
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEKKLESKsgNKNKMEAKAQANSQKD-------------EIFALINKEANRDARAIA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 935 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL-------DETIAKLSKEKKALQETHQ 1007
Cdd:pfam18971 677 YTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSvkdlginPEWISKVENLNAALNEFKN 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1008 QTLDDLQAeedkvniLTKAKTKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESTMDMEN-DKQQLDEKLEK 1085
Cdd:pfam18971 757 GKNKDFSK-------VTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQK 829
|
..
gi 153945790 1086 KE 1087
Cdd:pfam18971 830 NE 831
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1653-1861 |
5.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1653 LKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1732
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1733 LENDVSQLqseveEVIQESRNAEE-----KAKKAITDA-AMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQl 1806
Cdd:COG3883 98 SGGSVSYL-----DVLLGSESFSDfldrlSALSKIADAdADLLEELKADKAE---LEAKKAELEAKLAELEALKAELEA- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1807 ALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDR 1861
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1375-1510 |
7.20e-05 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 47.70 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1375 RTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQrnfdK 1454
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1455 VLSEWKQKYEETQAELEASQKESRSLSTELFKVknvyeesLDQLETLRRENKNLQQ 1510
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQV-------LDKVQEIHEDCSVLLQ 133
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1464-1748 |
7.27e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1464 EETQAELEASQKeSRSLSTELFKVKNVYEESLDQLETLRR---ENKNLQQEISDLTEQIAEGGKqihELEKIKKQVEQEK 1540
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLDKIDRqkeETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1541 CEIQAA--LEEAEASLEHEEGKILRIQLELNQVKSevdrkiaekdeeidQLKRNHTRvVETMQSTLDA------EIRSRN 1612
Cdd:PRK11281 115 RETLSTlsLRQLESRLAQTLDQLQNAQNDLAEYNS--------------QLVSLQTQ-PERAQAALYAnsqrlqQIRNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1613 DALRVKKKmegDLNEMEIQLNHAnRLAAESLRNYRNTQGILKETQLHldDALRGQEDLK-EQLAIVERRANLLQAEI--- 1688
Cdd:PRK11281 180 KGGKVGGK---ALRPSQRVLLQA-EQALLNAQNDLQRKSLEGNTQLQ--DLLQKQRDYLtARIQRLEHQLQLLQEAInsk 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1689 --EELWATLEQTERSRKIAE------------------QELLDASERVQLLHTQNtslINTKKKLENdVSQLQSEVEEVI 1748
Cdd:PRK11281 254 rlTLSEKTVQEAQSQDEAARiqanplvaqeleinlqlsQRLLKATEKLNTLTQQN---LRVKNWLDR-LTQSERNIKEQI 329
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1149-1427 |
7.36e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1149 ISERLEEAGGATSAQVELNKKREAEFQKL--RRDLEEATLQHEAMV---AALRKKHADSMAELGEQIDNLQRVKQKLEKE 1223
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEMdrqAAIYAEQERMAMERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1224 K---SELKMETDDLSSNAEAISKAKGNLEKMCRSLEdQVSELKTKEEEQQRLINDLTAQRARLQTEAgEYSRQL------ 1294
Cdd:pfam17380 364 RirqEEIAMEISRMRELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQ-EEARQRevrrle 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1295 DEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE-----------LQRA 1363
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamieeerkrklLEKE 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1364 LSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNE 1427
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1756-1928 |
7.59e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1756 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggkKQIQKLEARVRELEGEVENEQKR 1835
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1836 naeaVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQA-EEAEEQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 153945790 1915 IAESQVNKLRVKSR 1928
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1380-1604 |
8.47e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1380 TDAIQRTEELEEAKKKLAQRLQEAEehveavnakcASLEKTKQrlQNEVEDlmldversnaacaaLDKKQRNFDKVLSEW 1459
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAE----------AALEEFRQ--KNGLVD--------------LSEEAKLLLQQLSEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1460 KQKYEETQAELEASQKESRSLSTELFKVKNVYEESLD--QLETLRRENKNLQQEISDLTEQIAEGGKQI----HELEKIK 1533
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVialrAQIAALR 304
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1534 KQVEQekcEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVdRKIAEKDEEIDQLKRNHTRVVETMQSTL 1604
Cdd:COG3206 305 AQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLL 371
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1676-1917 |
1.43e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1676 IVERRANLLQAEIEELwatLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEViqesrnaE 1755
Cdd:COG1842 2 IFKRLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1756 EKAKKAitdaammaeeLKKEQDTSAH--LERmKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLEARVRELEGEVEN-- 1831
Cdd:COG1842 72 EKARLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELKAKKDTlk 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1832 EQKRNAEAVKGLRKHERRVkeltyQTEEDRKNVLRLQDLVDKLQAKVKSYkrqAEEAEEQSnanlskfrkLQHELEEAEE 1911
Cdd:COG1842 140 ARAKAAKAQEKVNEALSGI-----DSDDATSALERMEEKIEEMEARAEAA---AELAAGDS---------LDDELAELEA 202
|
....*.
gi 153945790 1912 RADIAE 1917
Cdd:COG1842 203 DSEVED 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1454-1699 |
1.46e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1454 KVLSEWKQKYEETQAEL--EASQKESRSLSTELFKVKNVYEESLDQLETLRRENK--NLQQEISDLTEQIAEGGKQIHEL 1529
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1530 EKIKKQVEQEKCEIQAALEEAEASLEheegkILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVEtmqstLDAEIR 1609
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-----LRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1610 SrndalrVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRgqedlkeQLAIVERRANLLQAEIE 1689
Cdd:COG3206 302 A------LRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA-------ELRRLEREVEVARELYE 368
|
250
....*....|
gi 153945790 1690 ELWATLEQTE 1699
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
863-1089 |
1.46e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 863 KDELAKSEAKRKELEEkMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKI-------QLEAKIKEVTERAEEEEEI 935
Cdd:PLN02939 142 KNILLLNQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 936 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDETIAKLSKEKKALQ------------ 1003
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQedvsklsplqyd 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1004 ------ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQE-----------------KKLRMDLERAKRKLEG 1060
Cdd:PLN02939 297 cwwekvENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAnvskfssykvellqqklKLLEERLQASDHEIHS 376
|
250 260
....*....|....*....|....*....
gi 153945790 1061 DLKLAQESTMDMENDKQQLDEKLEKKEFE 1089
Cdd:PLN02939 377 YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1358-1537 |
1.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1358 AELQRALSKANSEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldve 1436
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1437 rSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFK-VKNVYEESLDQLETLRRENKNLQQEISDL 1515
Cdd:COG3206 261 -QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180
....*....|....*....|..
gi 153945790 1516 TEQIAEGGKQIHELEKIKKQVE 1537
Cdd:COG3206 340 EARLAELPELEAELRRLEREVE 361
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1206-1378 |
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 153945790 1206 LGEQIDNLQRVKQKLEKEKSELkmetddlssnAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRL---INDLTAQRAR 1282
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAEL----------ADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLqalLAELAGAGAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1283 LQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLeeetkakNALAHALQSSrhdcdllrEQYEEEQEGKAE--- 1359
Cdd:PRK09039 114 AEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL-------AALEAALDAS--------EKRDRESQAKIAdlg 178
|
170 180
....*....|....*....|.
gi 153945790 1360 --LQRALSKANSEVAQWRTKY 1378
Cdd:PRK09039 179 rrLNVALAQRVQELNRYRSEF 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1255-1474 |
2.03e-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: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1255 LEDQVSELKTKEEEQQRLINDLTAQR--ARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNAL 1332
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1333 AHALQSSRhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNA 1412
Cdd:COG3206 260 LQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1413 KcasLEKTKQRLQ--NEVEDLMLDVERSnaacaaLDKKQRNFDKVLsewkQKYEETQAELEASQ 1474
Cdd:COG3206 335 Q---LAQLEARLAelPELEAELRRLERE------VEVARELYESLL----QRLEEARLAEALTV 385
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
842-1116 |
2.50e-04 |
|
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: 46.26 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 842 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKnkiqleaK 921
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN-------E 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 922 IKEVTERAEEEEEINAELtakKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlteeMAGLDETIAKLSKEKKA 1001
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1002 LQETHQQTLDDLQAeedKVNILTKAKTKLEQQVDDLEgslEQEKKLRMDLERA---KRKLEGDLKLAQESTMDMENDKQQ 1078
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKVAN 808
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 153945790 1079 LDEKLEKKEFEISNL--ISKIEDEQAVEIQLQKK--IKELQA 1116
Cdd:pfam15921 809 MEVALDKASLQFAECqdIIQRQEQESVRLKLQHTldVKELQG 850
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1208-1306 |
2.62e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1208 EQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAiskakgNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEA 1287
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERLA------ELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRY 484
|
90 100
....*....|....*....|..
gi 153945790 1288 G---EYSRQLDEKDALVSQLSR 1306
Cdd:COG0542 485 GkipELEKELAELEEELAELAP 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1742-1937 |
2.81e-04 |
|
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: 46.21 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1742 SEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQtVKDLQHRLDEAEQLALKGGK----KQIQK 1817
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER---LRREREKAER-YQALLKEKREYEGYELLKEKealeRQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1818 LEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKN-VLRLQDLVDKLQAKVKSYKRQAEEAEEqsnanl 1896
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKER------ 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153945790 1897 skfrklqhELEEAEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:TIGR02169 316 --------ELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1752-1917 |
2.85e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1752 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRL-DEAEQlALKGGKKQIQKLEARVRELEGEVE 1830
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1831 NEQKRnaeavkgLRKHERRVkeltyqtEEDRKNVLRLQDLVDKLQAKVKSyKRQAEEAEEQSNANLSKFRKLQHELEEAE 1910
Cdd:PRK12704 100 RKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELEE-LIEEQLQELERISGLTAEEAKEILLEKVE 164
|
....*....
gi 153945790 1911 E--RADIAE 1917
Cdd:PRK12704 165 EeaRHEAAV 173
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1457-1913 |
3.08e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1457 SEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEisdlTEQIAEGGKQIHELEKIKKQV 1536
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1537 EQEKCEIQAALEEAEAslehEEGKILRIQLELNQVKSEVdrKIAEKDEEIDQLKRNHTRVVETMQSTLdaeiRSRNDALR 1616
Cdd:TIGR00618 259 QQLLKQLRARIEELRA----QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKM----RSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1617 VKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGIL-----KETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEEL 1691
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsireiSCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1692 WATLEQTERSRKIAEQELLDASERVQL---------LHTQNTSLINTKKKLE-NDVSQLQSEVEEVIQESRNAEEKAKKA 1761
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELqqryaelcaAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1762 ITDAAMMAEELKKEQdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAE--- 1838
Cdd:TIGR00618 489 KAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASlke 563
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1839 ----AVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERA 1913
Cdd:TIGR00618 564 qmqeIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1034-1451 |
3.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1034 VDDLEGSLeqeKKLRMDLE--RAKRKLEGDLK-LAQEST-------MDMENDKQQLDEKLEKKEFEISNLISKIEDEQAV 1103
Cdd:PRK04863 232 FQDMEAAL---RENRMTLEaiRVTQSDRDLFKhLITESTnyvaadyMRHANERRVHLEEALELRRELYTSRRQLAAEQYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1104 EIQLQKKIKELQARIEELGEEIEAERASRAK---AEKQRSDLSR---ELEEISERLEEAGGATSAQVELNKKREAEFQkl 1177
Cdd:PRK04863 309 LVEMARELAELNEAESDLEQDYQAASDHLNLvqtALRQQEKIERyqaDLEELEERLEEQNEVVEEADEQQEENEARAE-- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1178 rrdleeatlQHEAMVAALRKKHADSMAELGEQ---IDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMC-- 1252
Cdd:PRK04863 387 ---------AAEEEVDELKSQLADYQQALDVQqtrAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATee 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1253 -RSLEDQVS---ELKTKEEEQQRLINDLTAQ--RARLQTEAGEYSRQLDEKDALVSQLsrskQASTQQIEELKHQLEEET 1326
Cdd:PRK04863 458 lLSLEQKLSvaqAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1327 KAKNALAHALQSSRHDCDlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQR------L 1400
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQRLAARapawlaA 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1401 QEA----EEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRN 1451
Cdd:PRK04863 609 QDAlarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1458-1937 |
3.17e-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: 45.81 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1458 EWKQKYEETQAELEASQKESRSlstelfkvknvYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVE 1537
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKS-----------YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1538 QEKCEIQAALEEAEASLEHEEG--------KILRIQLE----------LNQVKSEVDRKIAEKDEEIDQ-----LKRNHT 1594
Cdd:TIGR00606 290 LKMEKVFQGTDEQLNDLYHNHQrtvrekerELVDCQREleklnkerrlLNQEKTELLVEQGRLQLQADRhqehiRARDSL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1595 RVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQL 1674
Cdd:TIGR00606 370 IQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1675 AIVERRANLLQAEIEELWAT----LEQTERSRKiAEQELLDASE---------RVQLLHTQNTSLINTKKKLENDVSQLQ 1741
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSsdriLELDQELRK-AERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEMEQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1742 SEVEEVIQESRNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLA- 1807
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKn 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1808 -----LKGGKKQIQKLEARVRE------LEGEVENEQKRNAEAVKGLRK-------HERRVKELTYQT-------EEDRK 1862
Cdd:TIGR00606 609 hinneLESKEEQLSSYEDKLFDvcgsqdEESDLERLKEEIEKSSKQRAMlagatavYSQFITQLTDENqsccpvcQRVFQ 688
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1863 NVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:TIGR00606 689 TEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1137-1717 |
3.34e-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: 45.51 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1137 KQRSDLSRELEEIsERLEEaggatsaqvELNKKREAEFQKLRRdLEEATLQHEAMVAALRKKHADS----MAELGEQI-- 1210
Cdd:pfam07111 63 QQAELISRQLQEL-RRLEE---------EVRLLRETSLQQKMR-LEAQAMELDALAVAEKAGQAEAeglrAALAGAEMvr 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1211 DNLQRVKQKLEKEKSELKMEtdDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEY 1290
Cdd:pfam07111 132 KNLEEGSQRELEEIQRLHQE--QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1291 SRQLDEKDALVSQL-------------SRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGK 1357
Cdd:pfam07111 210 QEELEAQVTLVESLrkyvgeqvppevhSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1358 AELQRALS-----KANSEVAQWRTKYETDAIQ-RTEELE--EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVE 1429
Cdd:pfam07111 290 IQPSDSLEpefpkKCRSLLNRWREKVFALMVQlKAQDLEhrDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1430 dlmldVERSNAACAALDKKQrnfdkvlsewkqkyeeTQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQ 1509
Cdd:pfam07111 370 -----VERMSAKGLQMELSR----------------AQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1510 QEISDLTEQIAEGGKQIHELEKIKK------QVEQEKCEIQAALEEAEASLeheegkilriQLELNQVKSEVDRKIAEKD 1583
Cdd:pfam07111 429 ARIPSLSNRLSYAVRKVHTIKGLMArkvalaQLRQESCPPPPPAPPVDADL----------SLELEQLREERNRLDAELQ 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1584 EEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDA 1663
Cdd:pfam07111 499 LSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQA 578
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1664 LRG-----QEDLKEQLAIVERRANLLQAEIEELWATLEQTERsRKIAEQELLDASERVQ 1717
Cdd:pfam07111 579 LQEkvaevETRLREQLSDTKRRLNEARREQAKAVVSLRQIQH-RATQEKERNQELRRLQ 636
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1498-1937 |
3.46e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.28 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1498 LETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAAL--------EEAEASLEHEEGKILRIQLELN 1569
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1570 QVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNT 1649
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1650 QGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1729
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1730 KKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALK 1809
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1810 GGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAE 1889
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 153945790 1890 EQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1464-1832 |
3.54e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.06 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1464 EETQAELEASQKESRSLSTELfkvknvyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEI 1543
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALL-------AQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1544 QAAL-------EEAEASLEHEEGKILRIQLELNQVKSEV---DRKIAEKDEEIDQLKRNHTRvvetmqstLDAEIRSRNd 1613
Cdd:pfam19220 110 RIELrdktaqaEALERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGELATARERLAL--------LEQENRRLQ- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1614 alRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAiVERRAnlLQAEIEELWA 1693
Cdd:pfam19220 181 --ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHR-AERAS--LRMKLEALTA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1694 TLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEviQESRNAE-EKAKKAITD-AAMMAEE 1771
Cdd:pfam19220 256 RAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER--RTQQFQEmQRARAELEErAEMLTKA 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1772 LKkeqDTSAHLERMkknlEQTVKDLQHRLDEAEQLALKggkkQIQKLEARVRELEGEVENE 1832
Cdd:pfam19220 334 LA---AKDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1344-1536 |
3.64e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 45.42 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1344 DLLREQYEEEQE-GKAELQR---ALSKAnsevaqwRTKYETDaIQRTEE----LEEAKKKLAQRLQEAEEHVEAVNAKCa 1415
Cdd:pfam10168 542 QVFREEYLKKHDlAREEIQKrvkLLKLQ-------KEQQLQE-LQSLEEerksLSERAEKLAEKYEEIKDKQEKLMRRC- 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1416 slEKTKQRLqNEVEDLMLDVERSNAA-CAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRslstelfkvKNVYEES 1494
Cdd:pfam10168 613 --KKVLQRL-NSQLPVLSDAEREMKKeLETINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRK---------KSSLSLS 680
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153945790 1495 LDQLETLRrenKNLQQEisdlTEQIAEggkQIHELEKIKKQV 1536
Cdd:pfam10168 681 EKQRKTIK---EILKQL----GSEIDE---LIKQVKDINKHV 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1637-1935 |
3.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1637 RLAAESLRnyRNTQGILkeTQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERV 1716
Cdd:PRK02224 175 RLGVERVL--SDQRGSL--DQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1717 QLLHTqntslintkkkLENDVSQLQSEVEEVIQEsrnaEEKAKKAITDAAMMAEELKKEqdtsahlermkknLEQTVKDL 1796
Cdd:PRK02224 251 EELET-----------LEAEIEDLRETIAETERE----REELAEEVRDLRERLEELEEE-------------RDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1797 QhrLDEAEQLALKggkKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQA 1876
Cdd:PRK02224 303 G--LDDADAEAVE---ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1877 KVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKIS 1935
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1730-1929 |
3.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1730 KKKLENDVSQLQSEVEEvIQESRNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKKNL-----EQTVKDLQHRLD 1801
Cdd:COG4913 220 EPDTFEAADALVEHFDD-LERAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1802 EAEQlALKGGKKQIQKLEARVRELEGEVEN-EQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKS 1880
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153945790 1881 YKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNK-LRVKSRE 1929
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1685-1912 |
4.00e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1685 QAEIEELWATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLENDVSQLQsEVEEVIQESRNAEEKAKKAITD 1764
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1765 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-DEAEQLalkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGL 1843
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1844 RKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVksykrQAEEAEEQSNANLSKFRKLQHELEEAEER 1912
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1347-1708 |
4.24e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.13 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1347 REQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-AEEHVEAVNAKCASLEKTKQRLQ 1425
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1426 NEVEDLMLDVERSNAAcaALDKKQRNFDKVLSEWKQKYEETQAELEASQKE----SRSLSTELFKVKNVYEESLDQLETL 1501
Cdd:pfam09731 157 QAVKAHTDSLKEASDT--AEISREKATDSALQKAEALAEKLKEVINLAKQSeeeaAPPLLDAAPETPPKLPEHLDNVEEK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1502 RRENKNLQQEISDLTEQIAEGGKQ-IHELEKIKKQVEQEKCEIQAAL-EEAEASLEHEEGKILRIQLELNQVKSEVDRK- 1578
Cdd:pfam09731 235 VEKAQSLAKLVDQYKELVASERIVfQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAELKKREEKHi 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1579 ---IAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDA--LRVKKKMEgdlNEMEIQLNHANRLAAESLRNYRNTQGIL 1653
Cdd:pfam09731 315 eraLEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERerEEIRESYE---EKLRTELERQAEAHEEHLKDVLVEQEIE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1654 KEtqlhlddaLRGQEDLKEQlaiVERRANLLQAEIEELWATLEQTER---SRKIAEQE 1708
Cdd:pfam09731 392 LQ--------REFLQDIKEK---VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1705-1896 |
4.42e-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: 43.76 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1705 AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEViqesRNAEEKAKKAITDAAMMAEELKKE-QDTSAHLE 1783
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEiEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1784 RMKKNLEQ--TVKDLQHRLDEAEQLalkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTyqteedr 1861
Cdd:COG1579 77 KYEEQLGNvrNNKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 153945790 1862 knvLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANL 1896
Cdd:COG1579 145 ---AELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1130-1373 |
4.79e-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: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1130 ASRAKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRRDLEEATLQHEAMVAALRKKHADsMAELGEQ 1209
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1210 IDNLQrvkQKLEKEKSELKM------ETDDLSSNAEAISKAKgnlekmcrSLED---QVSELKTKEEEQQRLINDLTAQR 1280
Cdd:COG3883 74 IAEAE---AEIEERREELGEraralyRSGGSVSYLDVLLGSE--------SFSDfldRLSALSKIADADADLLEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1281 ARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEE---LKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGK 1357
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqeaLLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
250
....*....|....*.
gi 153945790 1358 AELQRALSKANSEVAQ 1373
Cdd:COG3883 223 AAAAAAAAAAAAAAAA 238
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
951-1156 |
4.94e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 951 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDL----------------- 1013
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1014 ---------------QAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMEN---- 1074
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1075 DKQQLDEKlekkefeisnliskiedeQAVEIQLQKKIkelqARieelgeeieAERASRAKAEKQrsdlSRELEEISERLE 1154
Cdd:PRK11637 231 DQQQLSEL------------------RANESRLRDSI----AR---------AEREAKARAERE----AREAARVRDKQK 275
|
..
gi 153945790 1155 EA 1156
Cdd:PRK11637 276 QA 277
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1266-1549 |
5.20e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1266 EEEQQRLIND-----------LTAQRARLQTEAgeysRQLDEKDAlvSQLSRSKQASTQQIEELKHQLEEETKAKNALAH 1334
Cdd:pfam00038 2 EKEQLQELNDrlasyidkvrfLEQQNKLLETKI----SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1335 ALQSSRHDCDLLREQYEEEQEGKAELQ---RALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQEAE 1404
Cdd:pfam00038 76 ELDNLRLAAEDFRQKYEDELNLRTSAEndlVGLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1405 EHVEAVNAKCASLEKTKQRLQNEVEDLMldversnaacaaldkkQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTEL 1484
Cdd:pfam00038 156 VNVEMDAARKLDLTSALAEIRAQYEEIA----------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEI 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153945790 1485 FKVKNVYEESLDQLETLRRENKNLQQEISDLTE----QIAEGGKQIHELEkikKQVEQEKCEIQAALEE 1549
Cdd:pfam00038 220 TELRRTIQSLEIELQSLKKQKASLERQLAETEEryelQLADYQELISELE---AELQETRQEMARQLRE 285
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1133-1283 |
5.75e-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: 43.76 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1133 AKAEKQRSDLSRELEEISERLEEAggatsaqvelnKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGE---- 1208
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAAL-----------EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1209 --------QIDNLQRVKQKLEKEKSELKMETDDLSsnaEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQR 1280
Cdd:COG1579 89 keyealqkEIESLKRRISDLEDEILELMERIEELE---EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
...
gi 153945790 1281 ARL 1283
Cdd:COG1579 166 EEL 168
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1391-1805 |
6.05e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1391 EAKKKLA---QRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldversnaacaaldKKQRNFDKVLSEWKQKYEETQ 1467
Cdd:pfam06160 83 KAKKALDeieELLDDIEEDIKQILEELDELLESEEKNREEVEELK--------------DKYRELRKTLLANRFSYGPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1468 AELEASQKESRSLSTELFKVKNV--YEESLDQLETLRRENKNLQQEISDLTEQIAEGGK----QIHELEKIKKQVEQEK- 1540
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTelpdQLEELKEGYREMEEEGy 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1541 ----CEIQAALEEAEASLEHEEGKILRIQLElnqvksEVDRKIAEKDEEIDQLkrnhtrvvetmQSTLDAEIRSRNDALR 1616
Cdd:pfam06160 229 alehLNVDKEIQQLEEQLEENLALLENLELD------EAEEALEEIEERIDQL-----------YDLLEKEVDAKKYVEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1617 VKKKMEGDLNEMEIQLNHANRLAAESLRNYrntqgILKETQLHLddalrgQEDLKEQLAIVERRANLLQAEIEElwatlE 1696
Cdd:pfam06160 292 NLPEIEDYLEHAEEQNKELKEELERVQQSY-----TLNENELER------VRGLEKQLEELEKRYDEIVERLEE-----K 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1697 QTERSrkIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKK------------AITD 1764
Cdd:pfam06160 356 EVAYS--ELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKsnlpglpesyldYFFD 433
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 153945790 1765 AAMMAEELKKEqdtsahLERMKKNLEQtvkdLQHRLDEAEQ 1805
Cdd:pfam06160 434 VSDEIEDLADE------LNEVPLNMDE----VNRLLDEAQD 464
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
951-1283 |
6.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 951 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKL 1030
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1031 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKK 1110
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1111 IKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEA 1190
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1191 MVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQ 1270
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330
....*....|...
gi 153945790 1271 RLINDLTAQRARL 1283
Cdd:COG4372 347 LVGLLDNDVLELL 359
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
832-1795 |
6.82e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 832 WMKLFFKIKPLL-----KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTL------LKEKNDLQLQVQSE--- 897
Cdd:TIGR01612 556 WKKLIHEIKKELeeeneDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNIsdkneyIKKAIDLKKIIENNnay 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 898 ADSLADAEE-RCEQLIKNKIQLEAKIKevteraeeeeeinaeltakkrkledecSELKK----DIDDLELTLAKVEKEkh 972
Cdd:TIGR01612 636 IDELAKISPyQVPEHLKNKDKIYSTIK---------------------------SELSKiyedDIDALYNELSSIVKE-- 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 973 ateNKVKNlTEEMAGLDETIAKLSKEKKALQETHQQTLddlqaEEDKVNILTKaKTKLEQQVddlegsLEQEKKLRMDLE 1052
Cdd:TIGR01612 687 ---NAIDN-TEDKAKLDDLKSKIDKEYDKIQNMETATV-----ELHLSNIENK-KNELLDII------VEIKKHIHGEIN 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1053 RAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEiqlqkKIKELQArieelgeeieaerasr 1132
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINID-----NIKDEDA---------------- 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1133 akaeKQRSDLSRELEEISERLEEAGGATSAQVELNK----KREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAElge 1208
Cdd:TIGR01612 810 ----KQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddflNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD--- 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1209 qiDNLQRVKQKLEKEKS---ELKMETDDLSSNAEAISKAKGNLeKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQT 1285
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSlinEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNKQNILKEILNKNIDTIKESNL 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1286 EAGEYSRQLDekDALVSQLSRSKQASTQ-QIEELKHQLEEETKAKNALAHALQSSRHDcdLLREQYEEEQEGKAELQRAL 1364
Cdd:TIGR01612 960 IEKSYKDKFD--NTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKEN--MLYHQFDEKEKATNDIEQKI 1035
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1365 SKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEaeEHVEAVNAKCASLEKTKQRLqnevedlmldversnaacaa 1444
Cdd:TIGR01612 1036 EDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNK--EILEEAEINITNFNEIKEKL-------------------- 1093
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1445 ldkKQRNFDKVLSEWKQKYEEtqaeleasqkESRSLSTELFKVKNVYEESLDQLETLRRENKN----LQQEISDLtEQIA 1520
Cdd:TIGR01612 1094 ---KHYNFDDFGKEENIKYAD----------EINKIKDDIKNLDQKIDHHIKALEEIKKKSENyideIKAQINDL-EDVA 1159
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1521 EGGKQIHELEKIKKQVEQ--EKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSeVDRKIAEKD-----EEIDQLKRNH 1593
Cdd:TIGR01612 1160 DKAISNDDPEEIEKKIENivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKG-INLSYGKNLgklflEKIDEEKKKS 1238
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1594 TRVVETMQSTLDaeirsrnDALRVKKKMEGDLNEMEIQLNHANRLAAESLRN--YRNTQGILKETQLHLDDalrgqedlk 1671
Cdd:TIGR01612 1239 EHMIKAMEAYIE-------DLDEIKEKSPEIENEMGIEMDIKAEMETFNISHddDKDHHIISKKHDENISD--------- 1302
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1672 eqlaIVERRANLLQAEIEElwatlEQTERSRKIAEQELLDASER---VQLLHTQNTSLINTKKKleNDVSQLQSEVEEVI 1748
Cdd:TIGR01612 1303 ----IREKSLKIIEDFSEE-----SDINDIKKELQKNLLDAQKHnsdINLYLNEIANIYNILKL--NKIKKIIDEVKEYT 1371
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*..
gi 153945790 1749 QESrnaeEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKD 1795
Cdd:TIGR01612 1372 KEI----EENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD 1414
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1456-1721 |
7.33e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1456 LSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQ 1535
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1536 VEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-KIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDA 1614
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1615 LRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILkETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWAT 1694
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL-EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260
....*....|....*....|....*..
gi 153945790 1695 LEQTERSRKIAEQELLDASERVQLLHT 1721
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLA 319
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1078-1364 |
7.93e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1078 QLDEKLEKKEFEISNLISKIEDEQAveiQLQKKIKELQArieelgeeieaeraSRAKAEKQRSDLSRELEEISERLEEag 1157
Cdd:pfam00038 33 KISELRQKKGAEPSRLYSLYEKEIE---DLRRQLDTLTV--------------ERARLQLELDNLRLAAEDFRQKYED-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1158 gatsaqvELNKKR--EAEFQKLRRDLEEATL-------QHEAM---VAALRKKHADSMAELGEQIDNLQRV-------KQ 1218
Cdd:pfam00038 94 -------ELNLRTsaENDLVGLRKDLDEATLarvdleaKIESLkeeLAFLKKNHEEEVRELQAQVSDTQVNvemdaarKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1219 KLEKEKSELKMETDDLSSnaeaiskakgnlekmcRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKD 1298
Cdd:pfam00038 167 DLTSALAEIRAQYEEIAA----------------KNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1299 ALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQssrhdcdllreqyEEEQEGKAELQRAL 1364
Cdd:pfam00038 231 IELQSLKKQKASLERQLAETEERYELQLADYQELISELE-------------AELQETRQEMARQL 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1525-1717 |
8.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1525 QIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVD---RKIAEKDEEIDQLKRNHTRVVETMQ 1601
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDklqAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1602 ------STLDAEIRSRNDalrvkkkmeGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLA 1675
Cdd:COG3883 97 rsggsvSYLDVLLGSESF---------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153945790 1676 IVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQ 1717
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
865-1020 |
1.05e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 865 ELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKK- 943
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKe 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 944 -RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKV 1020
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
844-1796 |
1.09e-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: 44.27 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 844 KSAETEKEMATMKEEFQKTKDELaksEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADaeerceqlIKNKIQLEAKIK 923
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKIINEM---KFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAE--------LTNKIKAEISDD 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 924 EVTERAEEEEEINAELTAKKRKLEDECSELKkdiddlelTLAKVE---KEKHATENKVKNLTEEMAGLDETIAK---LSK 997
Cdd:TIGR01612 884 KLNDYEKKFNDSKSLINEINKSIEEEYQNIN--------TLKKVDeyiKICENTKESIEKFHNKQNILKEILNKnidTIK 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQTLDdlqaeedkvNILTKAKTKLEQQVDDLegSLEQEKKLRMDLERAKRKLEGDLKLAQESTMdmendKQ 1077
Cdd:TIGR01612 956 ESNLIEKSYKDKFD---------NTLIDKINELDKAFKDA--SLNDYEAKNNELIKYFNDLKANLGKNKENML-----YH 1019
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1078 QLDEKlekkEFEISNLISKIEDEQA----VEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSdlSRELEEISERL 1153
Cdd:TIGR01612 1020 QFDEK----EKATNDIEQKIEDANKnipnIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEIN--ITNFNEIKEKL 1093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1154 EEAGGATSAQvELNKKREAEFQKLRRDLEEATLQHEAMVAAL---RKKHADSMAELGEQIDNLQRVKQK---------LE 1221
Cdd:TIGR01612 1094 KHYNFDDFGK-EENIKYADEINKIKDDIKNLDQKIDHHIKALeeiKKKSENYIDEIKAQINDLEDVADKaisnddpeeIE 1172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1222 KE----------KSELKMETDDLSSNAEAISKAKGNLEKM-------CRSLE----DQVSELKTKEEE----QQRLINDL 1276
Cdd:TIGR01612 1173 KKienivtkidkKKNIYDEIKKLLNEIAEIEKDKTSLEEVkginlsyGKNLGklflEKIDEEKKKSEHmikaMEAYIEDL 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1277 TAQRARLQTEAGEYSRQLDEKDAL-VSQLSRSKQASTQQIEELKHQLEEETKAKNalahalqssrhdCDLLREQYEEE-- 1353
Cdd:TIGR01612 1253 DEIKEKSPEIENEMGIEMDIKAEMeTFNISHDDDKDHHIISKKHDENISDIREKS------------LKIIEDFSEESdi 1320
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1354 QEGKAELQRALS---KANSEVAQWRTKYET---------------DAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKcA 1415
Cdd:TIGR01612 1321 NDIKKELQKNLLdaqKHNSDINLYLNEIANiynilklnkikkiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDD-I 1399
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1416 SLEKTKQRLQNEVEDLMLDversnaACAALDKKQRNFdkVLSEwkqkyEETQAELEASQKESRSLSTELFKVKNVYEESL 1495
Cdd:TIGR01612 1400 NLEECKSKIESTLDDKDID------ECIKKIKELKNH--ILSE-----ESNIDTYFKNADENNENVLLLFKNIEMADNKS 1466
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1496 DQLETLRREN--KNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGkiLRIQLELNQVKS 1573
Cdd:TIGR01612 1467 QHILKIKKDNatNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSA--LAIKNKFAKTKK 1544
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1574 EVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNemeIQLnhanrlaaeSLRNYRNTQGIL 1653
Cdd:TIGR01612 1545 DSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAID---IQL---------SLENFENKFLKI 1612
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1654 KETQLHLDDALRGQEDLKEQLAIVerranllqaeieelwaTLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKL 1733
Cdd:TIGR01612 1613 SDIKKKINDCLKETESIEKKISSF----------------SIDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKEL 1676
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1734 ENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEElkkeqdtsaHLERMKKNLEQTVKDL 1796
Cdd:TIGR01612 1677 DELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKE---------EIESIKELIEPTIENL 1730
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1429-1571 |
1.09e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.50 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1429 EDLMLDVERSNAACAALdKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEE---SLDQLETLRREN 1505
Cdd:COG1566 79 TDLQAALAQAEAQLAAA-EAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgavSQQELDEARAAL 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1506 KNLQQEISDLTEQIAEGGKQIHELEKI---KKQVEQekceIQAALEEAEASLEHEE------GKILRIQLELNQV 1571
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREEEELaaaQAQVAQ----AEAALAQAELNLARTTirapvdGVVTNLNVEPGEV 228
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1027-1558 |
1.26e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1027 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEfeisnlisKIEDEQAVEIQ 1106
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE--------EALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1107 LQKKIKElqarieelgeeieaerasrakaekqrsDLSRELEEISERLEEAGgatsaQVELNKKREAefqklrrdleeATL 1186
Cdd:pfam05557 80 LKKKYLE---------------------------ALNKKLNEKESQLADAR-----EVISCLKNEL-----------SEL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1187 QHEAMVAALrkkhadsmaELGEQIDNLQRVKQKLEKEKSELKmetddlssnaeaiskakgNLEKMCRSLEDQVSELKTKE 1266
Cdd:pfam05557 117 RRQIQRAEL---------ELQSTNSELEELQERLDLLKAKAS------------------EAEQLRQNLEKQQSSLAEAE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1267 EEQQRLindltaqrarlqteagEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKaknalahALQSSRHDCDLL 1346
Cdd:pfam05557 170 QRIKEL----------------EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNK-------HLNENIENKLLL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1347 REQ----------YEEEQEGKAELQRALSKANSEVAQWRtKYETDAIQRTEELEEAKKKLAQRLQEAEEHVE---AVNAK 1413
Cdd:pfam05557 227 KEEvedlkrklerEEKYREEAATLELEKEKLEQELQSWV-KLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEensSLTSS 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1414 CASLEKTKQRLQNE-------VEDLMLDVERSNAACAALDK------KQRNFDKVLSEwkqKYEETQAELEASQKES--- 1477
Cdd:pfam05557 306 ARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvllltKERDGYRAILE---SYDKELTMSNYSPQLLeri 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1478 RSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDL---------TEQIAEGGKQIHELEKIKKQVEQ---EKCEIQA 1545
Cdd:pfam05557 383 EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLerelqalrqQESLADPSYSKEEVDSLRRKLETlelERQRLRE 462
|
570
....*....|...
gi 153945790 1546 ALEEAEASLEHEE 1558
Cdd:pfam05557 463 QKNELEMELERRC 475
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1224-1478 |
1.32e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1224 KSELKMETDDLSSNAEAISKAKgnlekmcRSLEDQvselKTKEEEQQRLindlTAQRARLQTEAGEYSRQLDEKD--ALV 1301
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQ-------NALADK----ERAEADRQRL----EQEKQQQLAAISGSQSQLESTDqnALE 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1302 SQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQegKAELQRALSKANSEVAqwrtkyetd 1381
Cdd:NF012221 1602 TNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQEQLDDAKKISG--------- 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1382 aiqrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDlmldversnaacAALDKKQRNFDKVLSEWKQ 1461
Cdd:NF012221 1671 -----KQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDD------------AKADAEKRKDDALAKQNEA 1733
|
250
....*....|....*..
gi 153945790 1462 KYEETQAELEASQKESR 1478
Cdd:NF012221 1734 QQAESDANAAANDAQSR 1750
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1313-1508 |
1.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1313 QQIEELKHQLEEETKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDaiqrTEELEEA 1392
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY----EEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1393 KKklaqrlqeaEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:COG1579 86 RN---------NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 153945790 1473 SQKESRSLSTELfkVKNVYEESLDQLETLRRENKNL 1508
Cdd:COG1579 157 ELEELEAEREEL--AAKIPPELLALYERIRKRKNGL 190
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
840-1160 |
1.39e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 840 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMvTLLKEKNDLQLQVQSEADSLADAEERceQLikNKIQLE 919
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAMERER--EL--ERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 920 AKIKEVTERAEEEEEINaelTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDetiaKLSKEK 999
Cdd:pfam17380 357 ERKRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1000 KALQETHQQTLDDLQAEEdkVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRK-----------LEGDLKLAQES 1068
Cdd:pfam17380 430 EEARQREVRRLEEERARE--MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkraeeqrrkiLEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1069 TMDMENDKQQLDEKLEKKEFEISNLISKIEDEQavEIQLQKKIKElQARIEELGEEIEAERaSRAKAEKQRSDLSRELEE 1148
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEE--ERRKQQEMEE-RRRIQEQMRKATEER-SRLEAMEREREMMRQIVE 583
|
330
....*....|..
gi 153945790 1149 ISERLEEAGGAT 1160
Cdd:pfam17380 584 SEKARAEYEATT 595
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1243-1304 |
1.44e-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: 41.46 E-value: 1.44e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 1243 KAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQL 1304
Cdd:pfam08614 71 RSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDL 132
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1437-1581 |
1.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1437 RSNAACAALDKKQRNFDKVLSEWKQKYEET--QAELEAsQKESRSLSTELFKVKNVYEESLDQLE-TLRRENKNLQQEIS 1513
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEA-KEEIHKLRNEFEKELRERRNELQKLEkRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1514 DLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEH------EEGKilriQLELNQVKSEVDRKIAE 1581
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEAK----EILLEKVEEEARHEAAV 173
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1132-1337 |
1.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1132 RAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREaeFQKLRRDLEEatlqheamvaalrkkhadsmaELGEQID 1211
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE--IHKLRNEFEK---------------------ELRERRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1212 NLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQ-QRL--INDLTAQRARlqteag 1288
Cdd:PRK12704 83 ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELerISGLTAEEAK------ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153945790 1289 eySRQLDEkdaLVSQLSRSKQASTQQIEElKHQLEEETKAKNALAHALQ 1337
Cdd:PRK12704 157 --EILLEK---VEEEARHEAAVLIKEIEE-EAKEEADKKAKEILAQAIQ 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
984-1138 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 984 EMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAK--RKLEGD 1061
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153945790 1062 LKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAveiQLQKKIKELQARIEELGEEIEAERASRAKAEKQ 1138
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1315-1581 |
1.64e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.46 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1315 IEELKHQLEEETKAKNaLAHALQSSRHDCDLLREQYEEEQEGKAELqraLSKANSEVAQWRTKYETDAIQRTEELEEAKK 1394
Cdd:NF033838 71 LSEIQKSLDKRKHTQN-VALNKKLSDIKTEYLYELNVLKEKSEAEL---TSKTKKELDAAFEQFKKDTLEPGKKVAEATK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1395 KLAQRLQEAEEHVEA---------------------VNAKCASLEKTKQRLQNEvedlmLDVERSNAACAALDKKQRNFD 1453
Cdd:NF033838 147 KVEEAEKKAKDQKEEdrrnyptntyktleleiaesdVEVKKAELELVKEEAKEP-----RDEEKIKQAKAKVESKKAEAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1454 KVLsewKQKYEETQAELEASQKESRSLSTELFKVKNVYEE----------SLDQLETLRRENKNLQQEISDLTEQ----- 1518
Cdd:NF033838 222 RLE---KIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQdkpkrrakrgVLGEPATPDKKENDAKSSDSSVGEEtlpsp 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1519 -------IAEGGKQIHELEK-IKKQVEQEK---------------CEIQAALEEAEASLEHEEGKILRIQLELNQVKSEV 1575
Cdd:NF033838 299 slkpekkVAEAEKKVEEAKKkAKDQKEEDRrnyptntyktleleiAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKV 378
|
....*.
gi 153945790 1576 DRKIAE 1581
Cdd:NF033838 379 ESKKAE 384
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1166-1410 |
1.69e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1166 LNKKREAEFQKLRR----DLEEatLQHEAMVAALRKKHADSMaELGEQIDNLQRVKQKLEKEKSEL-KMETDDLSSNAEA 1240
Cdd:PRK05771 14 LKSYKDEVLEALHElgvvHIED--LKEELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKkKVSVKSLEELIKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1241 ISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTaqraRLQTEAGEYSRQLDEK--DALVSQLSRSKQASTQQIEEL 1318
Cdd:PRK05771 91 VEEELEKIEKEIKELEEEISELENEIKELEQEIERLE----PWGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1319 KHQLE-EETKAKNALA---HALQSSRHDCDLLREQYEEEQ-EGKAELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAK 1393
Cdd:PRK05771 167 ENVEYiSTDKGYVYVVvvvLKELSDEVEEELKKLGFERLElEEEGTPSELIREIKEELEEIEKERE----SLLEELKELA 242
|
250
....*....|....*..
gi 153945790 1394 KKLAQRLQEAEEHVEAV 1410
Cdd:PRK05771 243 KKYLEELLALYEYLEIE 259
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1672-1935 |
1.75e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1672 EQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQES 1751
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1752 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQiQKLEARVRELEGEVEN 1831
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER-KLLEERISEFTSNLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1832 EQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEE 1911
Cdd:pfam01576 171 EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA 250
|
250 260
....*....|....*....|....
gi 153945790 1912 RADIAESQVNKLRVKSREVHTKIS 1935
Cdd:pfam01576 251 RLEEETAQKNNALKKIRELEAQIS 274
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1781-1905 |
1.96e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1781 HLERMKKNLEQTVKDLQHRLDEAEQLAlkggKKQIQKLEARVRELEGEVEnEQKRNAEAVKGLRKHERrvkeltyQTEED 1860
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH----EKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES-------QSQED 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 153945790 1861 RKNvlRLQDLVDKLQAkVKSYKrqaEEAEEQSNANLSKFRK--LQHE 1905
Cdd:pfam15921 143 LRN--QLQNTVHELEA-AKCLK---EDMLEDSNTQIEQLRKmmLSHE 183
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
874-1228 |
2.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 874 KELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSEL 953
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 954 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQ 1033
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1034 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKE 1113
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1114 LQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVA 1193
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|....*
gi 153945790 1194 ALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELK 1228
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1107-1858 |
2.28e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1107 LQKKIKELQaRIEELGEEIEAERASR--AKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKL------- 1177
Cdd:pfam10174 1 LQAQLRDLQ-RENELLRRELDIKESKlgSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLqltiqal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1178 ------RRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKM 1251
Cdd:pfam10174 80 qdelraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1252 CRSLED--QVSELKTKEEEQQrliNDLTAQRARLQTEAGEYSRQLDEKD----ALVSQLSR--------SKQASTQQIEE 1317
Cdd:pfam10174 160 IKKLLEmlQSKGLPKKSGEED---WERTRRIAEAEMQLGHLEVLLDQKEkeniHLREELHRrnqlqpdpAKTKALQTVIE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1318 LK-----------HQLEEEtkaknalahaLQSSRHDCDLLREQYEEE--------------QEGKAELQRALSKANSEVA 1372
Cdd:pfam10174 237 MKdtkisslerniRDLEDE----------VQMLKTNGLLHTEDREEEikqmevykshskfmKNKIDQLKQELSKKESELL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1373 QWRTKYETdaiqrteeleeakkkLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDversnaacaaLDKKQRNF 1452
Cdd:pfam10174 307 ALQTKLET---------------LTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLR----------LEEKESFL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1453 DKvlsewKQKYeetqaeLEASQKESRSLSTELFKVKnvyeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKI 1532
Cdd:pfam10174 362 NK-----KTKQ------LQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1533 KKQVEQEKCEIQAALEEAEASLEHEEGKILRIqlelnqvKSEVDRKIAEKDEEIDQLKRN-----------HTRVVETMQ 1601
Cdd:pfam10174 424 VKSLQTDSSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKES 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1602 STLDAEIRSRNDALRVKKKmEGDLNEMEIQLNhanrlaaESLRNYRNTQGILKETQlHLDDALRGQEDLKEQLAIVERR- 1680
Cdd:pfam10174 497 SLIDLKEHASSLASSGLKK-DSKLKSLEIAVE-------QKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEv 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1681 ------ANLLQAEIEELWATLEQTE-----RSRKIAEQElldaSERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQ 1749
Cdd:pfam10174 568 arykeeSGKAQAEVERLLGILREVEnekndKDKKIAELE----SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1750 ESRNAEEKAKKAITDAAMMA-EELKKEQD-TSAHLERMKKNLEQTVKDLQH-RLDEAEQLALKGGKKQiQKLEARVRELE 1826
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGAlEKTRQELDaTKARLSSTQQSLAEKDGHLTNlRAERRKQLEEILEMKQ-EALLAAISEKD 722
|
810 820 830
....*....|....*....|....*....|....*....
gi 153945790 1827 GEV------ENEQKRNAEAVKGL-RKHERRVKELTYQTE 1858
Cdd:pfam10174 723 ANIallelsSSKKKKTQEEVMALkREKDRLVHQLKQQTQ 761
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1076-1801 |
2.28e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1076 KQQLDEKLEKKEFEISNLISKIEdEQAVEIQLQKKIKELQARieelgeeIEAERASRAKAEKQRSDLSRELEEISERLEE 1155
Cdd:NF041483 519 RRQAEETLERTRAEAERLRAEAE-EQAEEVRAAAERAARELR-------EETERAIAARQAEAAEELTRLHTEAEERLTA 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1156 AGGA-TSAQVELNK-KREA--EFQKLRRDLEE--ATLQHEAMVAALR---KKHADSMAELGEQIDNLQRVKQKLEKEKSE 1226
Cdd:NF041483 591 AEEAlADARAEAERiRREAaeETERLRTEAAEriRTLQAQAEQEAERlrtEAAADASAARAEGENVAVRLRSEAAAEAER 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1227 LKMETDDLSSN----------------AEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLIND-----LTAQRARLQT 1285
Cdd:NF041483 671 LKSEAQESADRvraeaaaaaervgteaAEALAAAQEEAARRRREAEETLGSARAEADQERERAREqseelLASARKRVEE 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1286 EAGEYSRQLDEKDALVSQLSRSKQASTQQIEE----LKHQLEEE-TKAKNALAHALQSSRhdcdllREQYEEEQEGKAEL 1360
Cdd:NF041483 751 AQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEEEiAGLRSAAEHAAERTR------TEAQEEADRVRSDA 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1361 QRALSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQR-LQEAEEHVEAVNAKCASLektKQRLQNEVEDLMLDVERSN 1439
Cdd:NF041483 825 YAERERASEDANRLR--------REAQEETEAAKALAERtVSEAIAEAERLRSDASEY---AQRVRTEASDTLASAEQDA 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1440 AACAALDKKQRN---------FDKVLSEWKQKYEETQAELEASQKESRSLSTElfKVKNVYEESLDQLETLRRENKNlqq 1510
Cdd:NF041483 894 ARTRADAREDANrirsdaaaqADRLIGEATSEAERLTAEARAEAERLRDEARA--EAERVRADAAAQAEQLIAEATG--- 968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1511 EISDLTEQIAE--GGKQIHElEKIKKQVEQEKCEIQAALEEAEASLEHEEGKIL-RIQLELNQVKSE----VDRKIAEKD 1583
Cdd:NF041483 969 EAERLRAEAAEtvGSAQQHA-ERIRTEAERVKAEAAAEAERLRTEAREEADRTLdEARKDANKRRSEaaeqADTLITEAA 1047
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1584 EEIDQLKRNHTRvvETMQSTLDAEirSRNDALRVKKKMEgdlnemeiqlnhANRLAAESLrnyRNTQGILKETQLHLDDA 1663
Cdd:NF041483 1048 AEADQLTAKAQE--EALRTTTEAE--AQADTMVGAARKE------------AERIVAEAT---VEGNSLVEKARTDADEL 1108
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1664 LRGQEdlKEQLAIVERRANL---LQAEIEELwatleqTERSRKIAEQELLDASERV-QLLHTQNTSLINTKKKLENDVSQ 1739
Cdd:NF041483 1109 LVGAR--RDATAIRERAEELrdrITGEIEEL------HERARRESAEQMKSAGERCdALVKAAEEQLAEAEAKAKELVSD 1180
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153945790 1740 LQSEVEEV-IQESRNAEEKAKKAITDAAMM---AEELKKEQDTSAhlermkknlEQTVKDLQHRLD 1801
Cdd:NF041483 1181 ANSEASKVrIAAVKKAEGLLKEAEQKKAELvreAEKIKAEAEAEA---------KRTVEEGKRELD 1237
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1663-1931 |
2.55e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1663 ALRGQEDlkeqlaiVERRanllQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLintKKKLEN-----DV 1737
Cdd:COG3096 342 ALRQQEK-------IERY----QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL---KSQLADyqqalDV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1738 SQ---LQseveevIQESRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEQTVKDLQHRLDEAEQlalkgGKKQ 1814
Cdd:COG3096 408 QQtraIQ------YQQAVQALEKARALCGLPDLTPENAEDYL---AAFRAKEQQATEEVLELEQKLSVADA-----ARRQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1815 IQKLEARVRELEGEVENEQKRNAeAVKGLRKHErrvkelTYQTEEDRKNVLR--LQDLvDKLQAKVKSYKRQAEEAEEQS 1892
Cdd:COG3096 474 FEKAYELVCKIAGEVERSQAWQT-ARELLRRYR------SQQALAQRLQQLRaqLAEL-EQRLRQQQNAERLLEEFCQRI 545
|
250 260 270
....*....|....*....|....*....|....*....
gi 153945790 1893 NANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVH 1931
Cdd:COG3096 546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1381-1675 |
2.74e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1381 DAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvERSNAACAAL-----DKKQRNFDKV 1455
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKL----RQAQAELEALkddndEETRETLSTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1456 -LSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETlrrenkNLQ--QEISDLTEQIAEGGKQIHELEKI 1532
Cdd:PRK11281 122 sLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYA------NSQrlQQIRNLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1533 KKQVEQekceiqaALEEAEASLEheegkilRIQLELNQVKSEVDRKI-AEKDEEIDQLkrnhtrvvETMQSTLDAEIRSR 1611
Cdd:PRK11281 196 LLQAEQ-------ALLNAQNDLQ-------RKSLEGNTQLQDLLQKQrDYLTARIQRL--------EHQLQLLQEAINSK 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1612 NDALRvKKKMEGDLNEMEIQLNHANRL-AAESLRNYRNTQGILKETQL-------------HLDDALRGQEDLKEQLA 1675
Cdd:PRK11281 254 RLTLS-EKTVQEAQSQDEAARIQANPLvAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQIS 330
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1279-1586 |
2.76e-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: 42.71 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1279 QRARLQTEAGEYSRQLDEKDALVSQ----LSRSKQASTQQIEELKHQLEEETKAknalahalqssrhdcdlLREQYEEEQ 1354
Cdd:pfam05667 286 GSSTTDTGLTKGSRFTHTEKLQFTNeapaATSSPPTKVETEEELQQQREEELEE-----------------LQEQLEDLE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1355 EGKAELQRALSKANSEVAQwrTKYETDAIQRT-EELEEA---KKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEd 1430
Cdd:pfam05667 349 SSIQELEKEIKKLESSIKQ--VEEELEELKEQnEELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWE- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1431 lmldversnAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELfKVKnvyEESLDQLETlrrENKNLQQ 1510
Cdd:pfam05667 426 ---------KHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEA-KQK---EELYKQLVA---EYERLPK 489
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153945790 1511 EI--SDLTEQIAEggkqihelekIKKQVEQEKCEIQAALEEAEAsleheegkilrIQLELNQVKSEVDRKIAEKDEEI 1586
Cdd:pfam05667 490 DVsrSAYTRRILE----------IVKNIKKQKEEITKILSDTKS-----------LQKEINSLTGKLDRTFTVTDELV 546
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1218-1400 |
2.87e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1218 QKLEKEKSELKmetddlssnaeaisKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEK 1297
Cdd:COG1579 13 QELDSELDRLE--------------HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1298 DALVSQLSRSKqastqQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTK 1377
Cdd:COG1579 79 EEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|...
gi 153945790 1378 YETDAIQRTEELEEAKKKLAQRL 1400
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1731-1923 |
2.91e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1731 KKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELkkeQDTSAHLERMKKNLEQTvkdlQHRLDEAEQLA--- 1807
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRI---QLLEEELERTEERLAEA----LEKLEEAEKAAdes 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1808 ---LKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQ-------AK 1877
Cdd:pfam00261 77 ergRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEeelkvvgNN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153945790 1878 VKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKL 1923
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1842-1934 |
3.22e-03 |
|
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: 42.74 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1842 GLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAE-------------------------EQSNANL 1896
Cdd:TIGR02168 166 GISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAErykelkaelrelelallvlrleelrEELEELQ 245
|
90 100 110
....*....|....*....|....*....|....*...
gi 153945790 1897 SKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKI 1934
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1577-1924 |
3.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1577 RKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKET 1656
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1657 QLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEND 1736
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1737 VSQLQSEVEEVIQEsrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQ 1816
Cdd:COG4372 166 LAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1817 KLEARVRELEGEVENEQKRNAEA-VKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNAN 1895
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340
....*....|....*....|....*....
gi 153945790 1896 LSKFRKLQHELEEAEERADIAESQVNKLR 1924
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1492-1936 |
3.40e-03 |
|
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: 42.31 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1492 EESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLEL--- 1568
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIknd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1569 NQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMqstldaeirsrndalrvkKKMEGDLNEMEIQLNHANRLAaESLRNYRN 1648
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEI------------------KKKEKELEKLNNKYNDLKKQK-EELENELN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1649 TQGILKETQLHLDDALRGQEDLKEQLAIV----ERRANLLQAEIEELwatLEQTERSRKIAEQELLDASERVQLLHTQNT 1724
Cdd:TIGR04523 177 LLEKEKLNIQKNIDKIKNKLLKLELLLSNlkkkIQKNKSLESQISEL---KKQNNQLKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1725 SLINTKKKLENDVSQLQSEVEEVIQESRNAEEKaKKAITDAAMMAEELK--KEQDTSAHLERMKKNLEQTVKDLQHRLDE 1802
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNnqKEQDWNKELKSELKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1803 AEQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERR-------VKELTYQTEEDRKNVLRLQDLVDKLQ 1875
Cdd:TIGR04523 333 NNK-IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKD 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1876 AKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISA 1936
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1493-1752 |
3.92e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1493 ESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVK 1572
Cdd:PLN02939 153 QALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1573 SEvdrKIAEKDeEIDQLKRNHTRVVETMQSTLDAEirsrndalRVKKKMEGDLNEMEIQLNHANrlaAESLRNYRNTQGI 1652
Cdd:PLN02939 233 EE---NMLLKD-DIQFLKAELIEVAETEERVFKLE--------KERSLLDASLRELESKFIVAQ---EDVSKLSPLQYDC 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1653 LKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSR------KIAEQELLDASERVQLLHTQNTSL 1726
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKfssykvELLQQKLKLLEERLQASDHEIHSY 377
|
250 260
....*....|....*....|....*.
gi 153945790 1727 IntkKKLENDVSQLQSEVEEVIQESR 1752
Cdd:PLN02939 378 I---QLYQESIKEFQDTLSKLKEESK 400
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1236-1407 |
4.04e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1236 SNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEqqrLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQI 1315
Cdd:PRK00409 488 SNAFEIAKRLGLPENIIEEAKKLIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1316 EELKHQLEEEtkAKNALAHALQSSRhdcDLLREQYEEEQEGKAElqralskansevaqwrtkyetdaiQRTEELEEAKKK 1395
Cdd:PRK00409 565 DKLLEEAEKE--AQQAIKEAKKEAD---EIIKELRQLQKGGYAS------------------------VKAHELIEARKR 615
|
170
....*....|..
gi 153945790 1396 LAQRLQEAEEHV 1407
Cdd:PRK00409 616 LNKANEKKEKKK 627
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1138-1329 |
4.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1138 QRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVK 1217
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1218 QKLEKEKS-------ELKMETD---------DLSSNAEAISKAKGNLEKMCRSLE---DQVSELKTKEEEQQRLINDLTA 1278
Cdd:PHA02562 262 TAAAKIKSkieqfqkVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEkldTAIDELEEIMDEFNEQSKKLLE 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153945790 1279 QRARLQTEAGEYSRQLDEKD---ALVSQLSRSKQASTQQIEELKHQLEEETKAK 1329
Cdd:PHA02562 342 LKNKISTNKQSLITLVDKAKkvkAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1812-1920 |
5.25e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1812 KKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKEL---TYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEA 1888
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 153945790 1889 EEQSNAnLSKFRKLQH----------------ELEEAEERADIAESQV 1920
Cdd:COG2433 492 KRKLER-LKELWKLEHsgelvpvkvvekftkeAIRRLEEEYGLKEGDV 538
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
940-1180 |
5.45e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 940 TAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDETIAKLSKEKKALQETHqqTLD-DLQAEED 1018
Cdd:PRK05771 71 PLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPWG--NFDlDLSLLLG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1019 KVNILTKAKTKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAqestMDMENDKQQLDEKLEKKEFEISNLISKIE 1098
Cdd:PRK05771 142 FKYVSVFVGTVPEDKLEELKLESDVEN-----VEYISTDKGYVYVVV----VVLKELSDEVEEELKKLGFERLELEEEGT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1099 DEQAVEiQLQKKIKELqarieelgeeieaerasrakaEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLR 1178
Cdd:PRK05771 213 PSELIR-EIKEELEEI---------------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFL 270
|
..
gi 153945790 1179 RD 1180
Cdd:PRK05771 271 KT 272
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1072-1483 |
5.47e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1072 MENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISE 1151
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1152 RleeaggatsaQVELNKKREAEFQKLrRDLEEAtlqheamVAALRKKHADSMAElgeqidnLQRVKQKLEKEKSELKMET 1231
Cdd:pfam07888 116 E----------KDALLAQRAAHEARI-RELEED-------IKTLTQRVLERETE-------LERMKERAKKAGAQRKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1232 DDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTaqraRLQTEAGEYSRQLDEKDALVSQLSRSKQ-- 1309
Cdd:pfam07888 171 AERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTIT----TLTQKLTTAHRKEAENEALLEELRSLQErl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1310 -ASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYeeeqegkAELQRALSKANSEVAQWRTkyetdAIQRTEE 1388
Cdd:pfam07888 247 nASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQL-------ADASLALREGRARWAQERE-----TLQQSAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1389 LEEAK-KKLAQRLQEAEEHVEavnakcaslektKQRLQNEVEDLMLDVERSNAACAaldkkqrnfdkvLSEWKQKYEETQ 1467
Cdd:pfam07888 315 ADKDRiEKLSAELQRLEERLQ------------EERMEREKLEVELGREKDCNRVQ------------LSESRRELQELK 370
|
410
....*....|....*.
gi 153945790 1468 AELEASQKESRSLSTE 1483
Cdd:pfam07888 371 ASLRVAQKEKEQLQAE 386
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1665-1929 |
5.47e-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: 41.65 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1665 RGQEDLKEQLAIVERRANL------LQAEIEE---LWATLEQ--TERSRKIAEQELLDASERVQLLHTQNTSL-INTKKK 1732
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLeeaekaRQAEMDRqaaIYAEQERmaMERERELERIRQEERKRELERIRQEEIAMeISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1733 LENDVSQLQSEVEEVIQESRNA------EEKAKKAITDAAMMAEELKKEQDtSAHLERMKKNLEQTVKDLQH-RLDEAEQ 1805
Cdd:pfam17380 380 LERLQMERQQKNERVRQELEAArkvkilEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERvRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1806 lalkggKKQIQKL---EARVRELEGEVENEQKRNAEAvkglrkHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKsyK 1882
Cdd:pfam17380 459 ------QQQVERLrqqEEERKRKKLELEKEKRDRKRA------EEQRRKILEKELEERKQAMIEEERKRKLLEKEME--E 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 153945790 1883 RQAEEAEEQSNANLSKFRKLQHELEE---AEERADIAESQVNKLRVKSRE 1929
Cdd:pfam17380 525 RQKAIYEEERRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMERE 574
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1387-1756 |
5.55e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1387 EELEEAKKKLAQ-RLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:PRK04778 86 EQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1466 TQAELEasqKESRSLSTELFKVKNV-----YEESLDQLETLRRENKNLQQeisdLTEQIAEggkQIHELEK-IKKQVEqe 1539
Cdd:PRK04778 166 ALDELE---KQLENLEEEFSQFVELtesgdYVEAREILDQLEEELAALEQ----IMEEIPE---LLKELQTeLPDQLQ-- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1540 kcEIQAALEEAEAS---LEHE--EGKILRIQLELNQVKSEVDR-KIAEKDEEIDQLKRNhtrvVETMQSTLDAEIRSRND 1613
Cdd:PRK04778 234 --ELKAGYRELVEEgyhLDHLdiEKEIQDLKEQIDENLALLEElDLDEAEEKNEEIQER----IDQLYDILEREVKARKY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1614 ALRVKKKMEGDLNEMEIQ----------LNHANRLAAESLRNYRNTQGILKETQ---LHLDDALRGQE----DLKEQLAI 1676
Cdd:PRK04778 308 VEKNSDTLPDFLEHAKEQnkelkeeidrVKQSYTLNESELESVRQLEKQLESLEkqyDEITERIAEQEiaysELQEELEE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1677 VERRANLLQAEIEELWATLEQTERSRKIAEQELL------------------------------DASERVQLLHTQ-NTS 1725
Cdd:PRK04778 388 ILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLEryrnklheikryleksnlpglpedylemffEVSDEIEALAEElEEK 467
|
410 420 430
....*....|....*....|....*....|....*..
gi 153945790 1726 LINTKK------KLENDVSQLQSEVEEVIQESRNAEE 1756
Cdd:PRK04778 468 PINMEAvnrlleEATEDVETLEEETEELVENATLTEQ 504
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
840-1337 |
5.96e-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: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 840 KPLLKSAETEKEMATMKEEFQKTKDELAKSEA-------KRKELEEKMVTLLKEKND-------LQLQVQSEADSLADAE 905
Cdd:pfam07111 204 KQLSKTQEELEAQVTLVESLRKYVGEQVPPEVhsqtwelERQELLDTMQHLQEDRADlqatvelLQVRVQSLTHMLALQE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 906 ERCEQLIKNKIQLEAKIkevteraeeeeeinaeltakKRKLEDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEM 985
Cdd:pfam07111 284 EELTRKIQPSDSLEPEF--------------------PKKCRSLLNRWREKVFALMVQLKAQDLEH---RDSVKQLRGQV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 986 AGLDETIAKLSKEKKALqethQQTLDDLQAEEDKVNILTKAktkleqqvddLEGSLEQEKKLRMDLERAKRKLEGDLKLA 1065
Cdd:pfam07111 341 AELQEQVTSQSQEQAIL----QRALQDKAAEVEVERMSAKG----------LQMELSRAQEARRRQQQQTASAEEQLKFV 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1066 QESTMDMENDKQQLDEKLEKKEFEISNLISKIedeqAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRE 1145
Cdd:pfam07111 407 VNAMSSTQIWLETTMTRVEQAVARIPSLSNRL----SYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1146 LEEISE---RL--EEAGGATSAQVELNKKREaEFQKLRRDLEEATLQHEAMVaalrKKHADSMAELGEQIDNLQRVKQKL 1220
Cdd:pfam07111 483 LEQLREernRLdaELQLSAHLIQQEVGRARE-QGEAERQQLSEVAQQLEQEL----QRAQESLASVGQQLEVARQGQQES 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1221 EKEKSELKMEtddLSSNAEAISKAkgnlekmcrsLEDQVSELKTKEEEQ----QRLINDLTAQRARLQTEAGEYSRQLDE 1296
Cdd:pfam07111 558 TEEAASLRQE---LTQQQEIYGQA----------LQEKVAEVETRLREQlsdtKRRLNEARREQAKAVVSLRQIQHRATQ 624
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 153945790 1297 KDALVSQLSR-SKQASTQQIEELKHQLEEETKAKNALAHALQ 1337
Cdd:pfam07111 625 EKERNQELRRlQDEARKEEGQRLARRVQELERDKNLMLATLQ 666
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1782-1900 |
6.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1782 LERMKK-NLEQTVKDLQHRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVkglrkheRRVKELT 1854
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 153945790 1855 YQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEE-------AEEQSNANLSKFR 1900
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1668-1937 |
6.11e-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: 41.65 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1668 EDLKEQLAIVERRANLLQAEIEELWATLEQtERSRKIAEQELLDASERVQLLHTQNTSLINTKKKL------ENDVSQLQ 1741
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaeqERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1742 SEVEEVIQESRNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQiQKLEAR 1821
Cdd:pfam17380 348 RELERIRQEERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ-RKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1822 VRELEgEVENEQKrNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRK 1901
Cdd:pfam17380 419 KVEME-QIRAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270
....*....|....*....|....*....|....*.
gi 153945790 1902 LQHELEEaEERADIAESQVNKLRVKSREVHTKISAE 1937
Cdd:pfam17380 497 LEKELEE-RKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
956-1058 |
6.26e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 956 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVD 1035
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 153945790 1036 DLEGSLEQEKKLRMDLERAKRKL 1058
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
892-1033 |
6.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 892 LQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTeraeeeeeinaeltaKKRKLEDECSELKKDIDDLELTLAK----V 967
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHK---------------LRNEFEKELRERRNELQKLEKRLLQkeenL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153945790 968 EKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQ------AEEDKVNILTKAKTKLEQQ 1033
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKEILLEKVEEEARHE 170
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1544-1699 |
6.52e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1544 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKiAEKDEEIDQLKRNHTRVVETMQSTldaeirsrndalrvkkkmEG 1623
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESEL-AISRQDYDGATAQLRAAQAAVKAA------------------QA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1624 DLNEMEIQLNHANRLAAESL----------RNYRNTQGILKETQLHLDDALRGQE-DLKEQLAIVERRANLLQAEIEELW 1692
Cdd:pfam00529 118 QLAQAQIDLARRRVLAPIGGisreslvtagALVAQAQANLLATVAQLDQIYVQITqSAAENQAEVRSELSGAQLQIAEAE 197
|
....*..
gi 153945790 1693 ATLEQTE 1699
Cdd:pfam00529 198 AELKLAK 204
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
998-1158 |
7.01e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 998 EKKALQETHQQTldDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEqekklrmDLERAKRKLEGDLKLAQEStmdmENDKQ 1077
Cdd:COG2433 395 PEAEREKEHEER--ELTEEEEEIRRLEEQVERLEAEVEELEAELE-------EKDERIERLERELSEARSE----ERREI 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1078 QLDEKLEKKEFEISNLISKIEDEQaveiqlqKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRE-LEEISERLEEA 1156
Cdd:COG2433 462 RKDREISRLDREIERLERELEEER-------ERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEaIRRLEEEYGLK 534
|
..
gi 153945790 1157 GG 1158
Cdd:COG2433 535 EG 536
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1268-1539 |
7.03e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.21 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1268 EQQRLINDlTAQR------ARLQTEAGEYS---RQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAknalahALQS 1338
Cdd:COG0497 133 EHQSLLDP-DAQRelldafAGLEELLEEYReayRAWRALKKELEELRADEAERARELDLLRFQLEELEAA------ALQP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1339 srhdcdllreqyEEEQEGKAELQRAlskANSEvaqwrtKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLE 1418
Cdd:COG0497 206 ------------GEEEELEEERRRL---SNAE------KLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1419 KTKQRLQN---EVEDLMLDVERsnaACAALDKKQRNFDKV---LSEW---KQKYEETQAELEASQKEsrsLSTELFKVKN 1489
Cdd:COG0497 265 ELAERLESaliELEEAASELRR---YLDSLEFDPERLEEVeerLALLrrlARKYGVTVEELLAYAEE---LRAELAELEN 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1490 vYEESLDQLEtlrrenknlqQEISDLTEQIAEGGKQIHEL-----EKIKKQVEQE 1539
Cdd:COG0497 339 -SDERLEELE----------AELAEAEAELLEAAEKLSAArkkaaKKLEKAVTAE 382
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1676-1830 |
7.48e-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: 40.05 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1676 IVERRANLLQAEIEELwatLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEViqesrnaE 1755
Cdd:pfam04012 1 IFKRLGRLVRANIHEG---LDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKL-------E 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153945790 1756 EKAKKAITDAAmmaEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLEARVRELEGEVE 1830
Cdd:pfam04012 71 EKAQAALTKGN---EELARE------ALAEKKSLEKQAEALETQLAQQRSAVEQL-RKQLAALETKIQQLKAKKN 135
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1162-1565 |
8.66e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1162 AQVELNKKREaEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQI--DNLQRVKQKLEKEKSELKMETDDLSSNAE 1239
Cdd:pfam13166 94 IQEKIAKLKK-EIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIkrKKNSALSEALNGFKYEANFKSRLLREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1240 AISKAKGNLekmcrSLEDQVSELKTKEEEQQRLINDLTAQrarlqteageySRQLD--EKDALvsqLSRSKQASTQQIEE 1317
Cdd:pfam13166 173 DNFNAGVLL-----SDEDRKAALATVFSDNKPEIAPLTFN-----------VIDFDalEKAEI---LIQKVIGKSSAIEE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1318 LKHQLEEETKAKNALAHALQSSRHdC--------DLLREQYE-----EEQEGKAELQRALSKANSEVAQWRTKYeTDAIQ 1384
Cdd:pfam13166 234 LIKNPDLADWVEQGLELHKAHLDT-CpfcgqplpAERKAALEahfddEFTEFQNRLQKLIEKVESAISSLLAQL-PAVSD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1385 RTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVE--DLMLDVERSNAACAALDKKQRNFDKVLSEWKQK 1462
Cdd:pfam13166 312 LASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKSIEldSVDAKIESINDLVASINELIAKHNEITDNFEEE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1463 YEETQAELEASQ-KESRSLSTELFKVKNVYEESLDQLETlrrENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEkc 1541
Cdd:pfam13166 392 KNKAKKKLRLHLvEEFKSEIDEYKDKYAGLEKAINSLEK---EIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKL-- 466
|
410 420
....*....|....*....|....*
gi 153945790 1542 eiQAALEEAEASLE-HEEGKILRIQ 1565
Cdd:pfam13166 467 --LKAFGFGELELSfNEEGKGYRII 489
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1059-1186 |
8.94e-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: 40.51 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1059 EGDLKLAQESTMDME---NDKQQLDEKLEKKEFEISNLISKIEDeqaVEIQLQKKIKELQARIEELGEEIEAERASRAKA 1135
Cdd:pfam09787 36 VEGLDSSTALTLELEelrQERDLLREEIQKLRGQIQQLRTELQE---LEAQQQEEAESSREQLQELEEQLATERSARREA 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 153945790 1136 EkqrSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATL 1186
Cdd:pfam09787 113 E---AELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQ 160
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1129-1937 |
9.80e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1129 RASRAKAEKQrsdLSRELEEISERLEEAGGATSAQVELNKKREAefqklrRDLEEATLQHEAMVAALRKKHADSMAElge 1208
Cdd:NF041483 275 REARAEAEKV---VAEAKEAAAKQLASAESANEQRTRTAKEEIA------RLVGEATKEAEALKAEAEQALADARAE--- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1209 qidnlqrvKQKLEKEKSElKMETDDLSSNAEAISKAKGNLEKMC-RSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEA 1287
Cdd:NF041483 343 --------AEKLVAEAAE-KARTVAAEDTAAQLAKAARTAEEVLtKASEDAKATTRAAAEEAERIRREAEAEADRLRGEA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1288 GEYSRQLD--EKDAlvsqlSRSKQASTQQIEELKHQLEEETKAKNALAHAlQSSRHDCDLLREQYEEEQEGKAELQRALS 1365
Cdd:NF041483 414 ADQAEQLKgaAKDD-----TKEYRAKTVELQEEARRLRGEAEQLRAEAVA-EGERIRGEARREAVQQIEEAARTAEELLT 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1366 KANSEVAQWRT-------KYETDAIQRT--------EELEEAKKKLAQRLQEAEEHVEAVNAKCaslEKTKQRLQNEVED 1430
Cdd:NF041483 488 KAKADADELRStataeseRVRTEAIERAttlrrqaeETLERTRAEAERLRAEAEEQAEEVRAAA---ERAARELREETER 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1431 LMLDveRSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQK----ESRSLSTELF-KVKNVYEESLDQLETLRREn 1505
Cdd:NF041483 565 AIAA--RQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRReaaeETERLRTEAAeRIRTLQAQAEQEAERLRTE- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1506 knlqqEISDLTEQIAEG--------GKQIHELEKIKKQVEQE----KCEIQAALE--EAEASLE----HEEGKILRIQLE 1567
Cdd:NF041483 642 -----AAADASAARAEGenvavrlrSEAAAEAERLKSEAQESadrvRAEAAAAAErvGTEAAEAlaaaQEEAARRRREAE 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1568 --LNQVKSEVDR---KIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSR---------NDALRVKKKMEG--DLNEMEIQ 1631
Cdd:NF041483 717 etLGSARAEADQereRAREQSEELLASARKRVEEAQAEAQRLVEEADRRatelvsaaeQTAQQVRDSVAGlqEQAEEEIA 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1632 -LNHANRLAAESLRnyrntqgilKETQLHLD----DALRGQEDLKEQLAIVERRAnllQAEIEELWATLEQTErSRKIAE 1706
Cdd:NF041483 797 gLRSAAEHAAERTR---------TEAQEEADrvrsDAYAERERASEDANRLRREA---QEETEAAKALAERTV-SEAIAE 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1707 QELL--DASERVQLLHTQNTSLINTKkklENDVSQLQSEveeviqesrnAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1784
Cdd:NF041483 864 AERLrsDASEYAQRVRTEASDTLASA---EQDAARTRAD----------AREDANRIRSDAAAQADRLIGEATSEAERLT 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1785 mkknlEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVK------------E 1852
Cdd:NF041483 931 -----AEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRteaervkaeaaaE 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153945790 1853 LTYQTEEDRKNVLRLQDLVDKLQAKVKSykRQAEEAEEQSNANLSKFRKLQHEL-EEAEERADIAESQVNKLRVKSREVH 1931
Cdd:NF041483 1006 AERLRTEAREEADRTLDEARKDANKRRS--EAAEQADTLITEAAAEADQLTAKAqEEALRTTTEAEAQADTMVGAARKEA 1083
|
....*.
gi 153945790 1932 TKISAE 1937
Cdd:NF041483 1084 ERIVAE 1089
|
|
| |
