|
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: 1345.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1331883584 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: 1338.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1331883584 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: 1322.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDEsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES-GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKP-LGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKvvKGKAEAHF 580
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAdssAKKGAKKKGSSFQTVSALFRENLNK 660
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---GGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 661 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFiD 740
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 1331883584 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: 1256.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 580 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADS-SAKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1331883584 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: 1252.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 580 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSS---AKKGAKKKGSSFQTVSALFRE 656
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAgggAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 657 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEG 736
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 1331883584 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: 1244.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEaaSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 580 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAD-SSAKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1331883584 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: 1214.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKD-ESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEqQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 580
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSS--AKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1331883584 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: 1158.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14927 3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESG----KMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14927 83 GAGKTVNTKRVIQYFAIVAALGDGPGKKAQflatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14927 163 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14927 243 DILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14927 323 VEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFIL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 578
Cdd:cd14927 403 EQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEA---DSSAKKGAKKKGSSFQTVSALFR 655
Cdd:cd14927 483 HFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLHK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 656 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 735
Cdd:cd14927 563 ENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPD 642
|
650 660 670
....*....|....*....|....*....|....
gi 1331883584 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: 1158.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1331883584 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 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEK-KKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 580
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEA-DSSAKKGAKKKGSSFQTVSALFRENLN 659
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 660 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 739
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 1331883584 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: 1034.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-----LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 581
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 582 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKL 661
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 662 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 741
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 1331883584 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: 1032.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 90 IEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFML 169
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 170 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKdesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSIDD 328
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 329 QEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 409 VGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANF 566
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 567 QKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKK---- 642
Cdd:pfam00063 472 QKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrt 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 643 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 722
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1331883584 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: 995.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 83 NPPKYDKIEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISD 162
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 163 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRND 242
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS--------GSNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 243 NSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQG-EI 321
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 322 TVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLQSLNSADLLK 400
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 401 ALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLC 480
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 481 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYdQH 559
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 560 LGKSANFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEadssakkg 639
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNA-------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 640 akKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 719
Cdd:smart00242 539 --GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 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: 991.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14934 3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDEsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14934 83 GAGKTENTKKVIQYFANIGGTGKQSSDG----KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 344 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 423
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 424 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 503
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 504 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGK-AEAHFSL 582
Cdd:cd14934 399 YKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFEL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 583 IHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAdssakKGAKKKGSSFQTVSALFRENLNKLM 662
Cdd:cd14934 479 VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLNKLM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 663 TNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSK 742
Cdd:cd14934 554 TTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNK 632
|
650 660
....*....|....*....|....*..
gi 1331883584 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: 977.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTgeKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGAS--KKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVK-GKAEAHF 580
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 581 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKG-SSFQTVSALFRENLN 659
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKgGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 660 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQfi 739
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 1331883584 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: 835.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAvtgEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS---GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDY----AFVSQGEITVPSIDDQEELMATD 336
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYylndYLNSSGCDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 415 TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 493 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKv 571
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 572 vkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKsamktlaslfstyasaeadssakkgakkkgssfqtvS 651
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------------------------------------G 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 652 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd00124 517 SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 1331883584 732 AiPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd00124 597 A-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1115 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 818.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 32 KPFDAKTSVFVAEPKESYVKSTIqskeggKITVKTEGGATLTVREDQV--FPMNPPKYDKIEDMAMMTHLHEPGVLYNLK 109
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKV------TEEGKKEDGESVSVKKKVLgnDRIKLPKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 110 ERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTV 189
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 190 NTKRVIQYFATIAvtgekkkDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETY 269
Cdd:COG5022 168 NAKRIMQYLASVT-------SSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 270 LLEKSRVTFQLKAERSYHIFYQITSNKkPDLIEMLLITTNPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDILGFTPEE 348
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 349 KVSIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVG 428
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 429 ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 508
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 509 IEWTFIDFgMDLAACIELIEK--PLGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSANFQKPKVVKGKaeahFSLIHY 585
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 586 AGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEadssakkgakkKGSSFQTVSALFRENLNKLMTNL 665
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-----------SKGRFPTLGSRFKESLNSLMSTL 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 666 RSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI---DSK 742
Cdd:COG5022 623 NSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 743 KASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQIITRTQAVCRGFLMRVEYQKMLQRREALFCIQYNVR 822
Cdd:COG5022 703 NAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFR 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 823 AFMNVKHWPWMKLFFKIKPLLKSAETEKEMatmkEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEAdslA 902
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSRKEY----RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRS---L 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 903 DAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRK-----LEDECSELKKDID-----DLELTLAKVEKEKH 972
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKlvnleLESEIIELKKSLSsdlieNLEFKTELIARLKK 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 973 ATEN-KVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQekklRMDL 1051
Cdd:COG5022 936 LLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGAL 1011
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1052 ERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKefEISNLISKIEDEQAveiQLQKKIKELQ 1115
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSASKIISSESTELSILK--PLQKLKGLLLLENN---QLQARYKALK 1070
|
|
| 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: 780.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14911 3 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESGK-------MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 256
Cdd:cd14911 83 GAGKTENTKKVIQFLAYVAASKPKGSGAVPHpavnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 257 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATD 336
Cdd:cd14911 163 ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14911 242 KSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 416 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 495 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLgksanfQKPKVVKG 574
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMKT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 575 --KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----STYASAEADSSAKKGAKKKGSSFQ 648
Cdd:cd14911 475 dfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaeIVGMAQQALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 649 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1331883584 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 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14920 3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14920 83 GAGKTENTKKVIQYLAHVASSHKGRKD--HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 342
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 343 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14920 318 QADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKA 576
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKDKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 577 EahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF--------STYASAEADSSAKKGAKKKGSSFQ 648
Cdd:cd14920 476 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivgLDQVTGMTETAFGSAYKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 649 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1331883584 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: 716.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14932 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESGKM--QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14932 83 GAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14932 163 VGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14932 242 MSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKA 576
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSSAKKGAKKKGSSFQT 649
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldKVAGMGESLHGAFKTRKGMFRT 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 650 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 729
Cdd:cd14932 558 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 637
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1331883584 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 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14921 3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14921 83 GAGKTENTKKVIQYLAVVASSHKGKKDTS--ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIMG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 344 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 422
Cdd:cd14921 240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 423 VYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 501
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 502 EEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEa 578
Cdd:cd14921 399 EEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDKTE- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 hFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSSAKKGAKKKGSSFQTV 650
Cdd:cd14921 477 -FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRTV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 651 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 730
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 1331883584 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: 675.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATiaVTGekkkdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGG------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd01380 313 QQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGK-SANFQKPKVVKGKae 577
Cdd:cd01380 393 LEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 578 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKtlaslfstyasaeadssakkgakkkgssFQTVSALFREN 657
Cdd:cd01380 470 --FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR----------------------------KKTVGSQFRDS 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 658 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAipEGQ 737
Cdd:cd01380 520 LILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--EWL 597
|
650 660 670
....*....|....*....|....*....|..
gi 1331883584 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: 673.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14919 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14919 83 GAGKTENTKKVIQYLAHVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 342
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 343 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14919 315 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 577
Cdd:cd14919 395 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKAD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 578 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSSAKKGAKKKGSSFQT 649
Cdd:cd14919 474 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTRKGMFRT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 650 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 729
Cdd:cd14919 552 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1331883584 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 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd15896 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESGKM--QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd15896 83 GAGKTENTKKVIQYLAHVASSHKTKKDQNSLAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd15896 163 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 421
Cdd:cd15896 242 MGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 422 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd15896 322 QAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAE 577
Cdd:cd15896 402 QEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLKDE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 578 AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYAS------AEADSSAKKGAKKKGSSFQTVS 651
Cdd:cd15896 479 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldkVSGMSEMPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 652 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*...
gi 1331883584 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: 659.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14930 3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDESgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14930 83 GAGKTENTKKVIQYLAHVASSPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIDILG 343
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 344 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 422
Cdd:cd14930 239 FSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 423 VYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14930 318 ADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKAE 577
Cdd:cd14930 397 QEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 578 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKG------AKKKGSSFQTVS 651
Cdd:cd14930 476 --FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppgGRPRRGMFRTVG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 652 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 731
Cdd:cd14930 554 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 1331883584 732 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14930 634 AIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| 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 1331883584 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 183 SGAGKTVNTKRVIQYFATIavtgekkkdeSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI----------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDI 341
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRH 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPkvvKG 574
Cdd:cd01381 389 IFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP---KS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 575 KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKgakkkgssfQTVSALF 654
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS---------PTLSSQF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 655 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnASAIP 734
Cdd:cd01381 535 RKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGIP 613
|
650 660 670
....*....|....*....|....*....|....*
gi 1331883584 735 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01381 614 PAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| 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: 630.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGekkkdesgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-----------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAID 340
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFqkpkvvKGKAEA 578
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENL 658
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660 670
....*....|....*....|....*....|.
gi 1331883584 739 IDSkkASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd01383 619 PLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| 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: 629.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 107 NLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 186
Cdd:cd01378 6 NLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 187 KTVNTKRVIQYFAtiAVTGekkkDESGKMQGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 266
Cdd:cd01378 86 KTEASKRIMQYIA--AVSG----GSESEVERV-KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 267 ETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTP 346
Cdd:cd01378 159 TNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 347 EEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLQSLNSADLLKALCYPRVKVGNEY---VTKGQTVQQV 423
Cdd:cd01378 239 EEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 424 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhmFVL--E 500
Cdd:cd01378 318 AYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTLkaE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 501 QEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSANFQKPKVVKGKAEA 578
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFELRRG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyasaEADSSAKKGAKKkgssfqTVSALFRENL 658
Cdd:cd01378 474 EFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP-----EGVDLDSKKRPP------TAGTKFKNSA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd01378 543 NALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG 622
|
650 660 670
....*....|....*....|....*....|.
gi 1331883584 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: 611.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 183 SGAGKTVNTKRVIQYFAtiAVTGEkkkdesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN---------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNPYDYAFVSQ-GEITVPSIDDQEELMATDSAID 340
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGaKHSKELKEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14883 231 VLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14883 311 VQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 500 EQEEYKKEGIEWTFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKvvKGKAEA 578
Cdd:cd14883 391 EQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQ-----TVSAL 653
Cdd:cd14883 467 EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTskgkpTVGDT 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 654 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAI 733
Cdd:cd14883 547 FKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRAR 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1331883584 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: 585.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAvtgekKKDESGkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----GRAVTE--GRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAI 339
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAAYLQSLNSADLL--------KALCYPRVKVGN 411
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVTPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 412 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01384 308 GIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 492 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQKPK 570
Cdd:cd01384 388 FNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 571 vvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAdssakkgakKKGSSFQTV 650
Cdd:cd01384 466 ----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT---------SSSSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 651 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnA 730
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL-A 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 1331883584 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 |
5.01e-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: 538.76 E-value: 5.01e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 105 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFAtiavtgekkkdES-GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01382 84 GAGKTESTKYILRYLT-----------ESwGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLittnpydyafvsqgeiTVPSIDDQEELMATDSAIDIL 342
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 343 GFTPEEKVSIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLQSLNSADLLKALCYpRVKVGNEY 413
Cdd:cd01382 217 GLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 414 VTKGQ------TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd01382 291 GAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLgKSANF 566
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRL 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 567 QKPKvvKGKAEAH--------FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADssakK 638
Cdd:cd01382 448 SIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKD----S 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 639 GAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 718
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 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 |
7.07e-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: 7.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSIL 178
Cdd:cd14890 3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 179 ITGESGAGKTVNTKRVIQYFATI--------AVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14890 83 ISGESGAGKTEATKIIMQYLARItsgfaqgaSGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 251 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQE 330
Cdd:cd14890 163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 331 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLQSLNSADLLKALCYPRVKV 409
Cdd:cd14890 242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 410 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd14890 322 GGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPlGIFSILEEECMFPKA-TDTSFKNKLYDQHLGKS 563
Cdd:cd14890 402 RHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 564 ------------ANFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAmKTLASLfstyasae 631
Cdd:cd14890 480 gsggtrrgssqhPHFVHPKF---DADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-RSIREV-------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 632 adssakkgakkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 711
Cdd:cd14890 548 -----------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 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 |
1.21e-169 |
|
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: 533.12 E-value: 1.21e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAVTGEKKKDesgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF----- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 256 ----GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS-----------------------NKKPDLIEMLLITT 308
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFEP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 309 -NPYDYAFVSqGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVA 384
Cdd:cd14888 233 hLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 385 DKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVL 463
Cdd:cd14888 312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 464 DIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPLGIFSILEEECM 542
Cdd:cd14888 392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 543 FPKATDTSFKNKLYDQHlgksANFQKPKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLAS 622
Cdd:cd14888 471 VPGGKDQGLCNKLCQKH----KGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 623 LFSTYASAEADssakkgAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 702
Cdd:cd14888 546 LFSAYLRRGTD------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 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 |
1.95e-165 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 520.49 E-value: 1.95e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTgekkkdesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS-----------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSnkKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMATDSAID 340
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEP----DGTEVADKAAYLQsLNSADLLKALCYPRVKVgneyvtK 416
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVATLLG-VDAATLEEALTSRLMEI------K 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 417 GQ-------TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14872 300 GCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQ 567
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAAKSTFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 568 KPKVvkGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYasaEADSSAKKGakkkgssf 647
Cdd:cd14872 458 YAEV--RTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPS---EGDQKTSKV-------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 648 qTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 727
Cdd:cd14872 525 -TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1331883584 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 |
1.07e-163 |
|
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: 516.26 E-value: 1.07e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 173
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 174 --NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 252 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNP-YDYAFVSQGEITVPSIDDQE 330
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 331 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LQSLNSADLLKALCYPRVKV 409
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 410 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANF 566
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 567 QKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASlfstyasaeadssakkgakkkgss 646
Cdd:cd14901 477 SVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 647 fqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14901 531 --TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1331883584 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 |
1.76e-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: 1.76e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAvtgekkkdeSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLiEMLLITTNPYDYAFvSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14903 151 LVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14903 229 LIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 419 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14903 309 KKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKgkaeA 578
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR----T 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSS-----FQTVSAL 653
Cdd:cd14903 464 QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggaltTTTVGTQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 654 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnasaI 733
Cdd:cd14903 544 FKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF----L 619
|
650 660 670
....*....|....*....|....*....|....*....
gi 1331883584 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 |
7.08e-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: 510.00 E-value: 7.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 105 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 184
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 185 AGKTVNTKRVIQYFATIavtgekkkdeSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd01385 84 SGKTESTNFLLHHLTAL----------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGE-ITVPSIDDQEELMATDSAIDIL 342
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 343 GFTPEEKVSIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKlYDQHLGKSANFQKPKvvkgK 575
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----V 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 576 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKS--------------AMKTLASLFSTYASAEADSSAKKGAK 641
Cdd:cd01385 467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSssafvreligidpvAVFRWAVLRAFFRAMAAFREAGRRRA 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 642 KKGSSFQ---------------------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNG 700
Cdd:cd01385 547 QRTAGHSltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 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 |
8.45e-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: 8.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd01387 3 VLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIAVTGEKKKDEsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKLAS 263
Cdd:cd01387 83 GSGKTEATKLIMQYLAAVNQRRNNLVTE----------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQI------TSNKKPDLIEmllittnPYDYAFVSQG-EITVPSIDDQEELMATD 336
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELlaglpaQLRQKYGLQE-------AEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLQSLNSADLLKALCYPRVKVGN 411
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 412 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 491
Cdd:cd01387 303 ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 492 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPK 570
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 571 VvkGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYAsAEADSSAKKGAKKKGSSFQ-- 648
Cdd:cd01387 461 M--PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR-AQTDKAPPRLGKGRFVTMKpr 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 649 --TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd01387 536 tpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1331883584 727 VLNASAIPEGQFIDSKKASEKLLASIDIDhTQYKFGHTKVFFK 769
Cdd:cd01387 616 CLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
104-769 |
1.07e-159 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 504.50 E-value: 1.07e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd01379 3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFATIavtgekkkdesGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd01379 83 GAGKTESANLLVQQLTVL-----------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKpdLIEMLLITTNPYDYAFVSQGEITVPSIDD--QEELMATD 336
Cdd:cd01379 152 GARISEYLLEKSRVVHQAIGERNFHIFYYIyaglAEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNE 412
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 413 YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd01379 310 TIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlgKSA 564
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 565 NFQKPKvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLAslfstyasaeadssakkgakkkg 644
Cdd:cd01379 463 YYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR----------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 645 ssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 724
Cdd:cd01379 516 ---QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKR 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1331883584 725 YKVL--NASAIPEGqfidSKKASEKLLASIDIDHtqYKFGHTKVFFK 769
Cdd:cd01379 593 YYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
849-1926 |
2.61e-158 |
|
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: 516.27 E-value: 2.61e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 849 EKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTER 928
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 929 AEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQ 1008
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1009 TLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEF 1088
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1089 EISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNK 1168
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1169 KREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNL 1248
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1249 EKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKA 1328
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1329 KNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEHVE 1408
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1409 AVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQ---KY--EETQAELEASQKESRSLSte 1483
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaRYaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1484 lfkVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILR 1563
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1564 IQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESL 1643
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1644 RNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQN 1723
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1724 TSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1803
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1804 EQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKR 1883
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 1331883584 1884 QAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVK 1926
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
104-769 |
4.58e-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: 498.17 E-value: 4.58e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd14873 3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 183 SGAGKTVNTKRVIQYFATIAVTGEKKKdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd14873 83 SGAGKTESTKLILKFLSVISQQSLELS--LKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQ-GEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITAMEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14873 240 MQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEEILT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 417 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14873 312 PLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvkgkA 576
Cdd:cd14873 391 FSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRV----A 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGssfQTVSALFRE 656
Cdd:cd14873 465 VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR---PTVSSQFKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 657 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL-NASAIPE 735
Cdd:cd14873 542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNLALPE 621
|
650 660 670
....*....|....*....|....*....|....
gi 1331883584 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 |
2.17e-155 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 493.89 E-value: 2.17e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 108 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKpevVAAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 178 LITGESGAGKTVNTKRVIQYFATI--AVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATAskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGE-ITVPSIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 335 TDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLQSLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 413 yvTKGQ------TVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14892 320 --ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PLGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 555 LYDQHLGKSANFQKPKVvkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMktlaslfstyasaeads 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 635 sakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 714
Cdd:cd14892 536 -------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPI 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 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 |
4.88e-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: 475.33 E-value: 4.88e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 183 SGAGKTVNTKRVIQYFATIavtgekkkdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 262
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL----------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEEL-----MATDS 337
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 338 aIDIL---GFTPEEKVSIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLQSLNSADLLKALCYPRVKV 409
Cdd:cd14897 232 -TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 410 GNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCINFT 484
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 485 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDqHLGKS 563
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGES 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 564 ANFQKPKvvKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYasaeadssakkgakkk 643
Cdd:cd14897 464 PRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 644 gssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 723
Cdd:cd14897 524 ----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 724 RYKVLnasaipegqFIDSKKASE-KLLASIDIDHTQ----YKFGHTKVFFK 769
Cdd:cd14897 594 RYKEI---------CDFSNKVRSdDLGKCQKILKTAgikgYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
104-728 |
6.65e-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: 6.65e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 168
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 169 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 248 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYqitsnkkpdliEMLLittnpydyafvSQGEITVPSiD 327
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFY-----------EMAI-----------GASEAARKR-D 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 328 DQEELMAtdsAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLQSLNSADLLK 400
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 401 ALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFDFNS 475
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 476 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNK 554
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 555 LYdQHLGKSANFQKPKVVKGKaeAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMktlaslfstyasaeads 634
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ----------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 635 sakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPS 714
Cdd:cd14900 516 -------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650
....*....|....
gi 1331883584 715 RILYGDFKQRYKVL 728
Cdd:cd14900 577 RLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
104-769 |
7.88e-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: 462.19 E-value: 7.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 174
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 175 QSILITGESGAGKTVNTKRVIQYFATIA---------VTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseevLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNP--YDYAFVSQGE-I 321
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 322 TVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 400 KALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PLGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 549 TSFKNKLYDQHlgksANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA 628
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 629 SAEADSSAKKGAKKKGSSFqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIC 708
Cdd:cd14907 558 GSQQQNQSKQKKSQKKDKF--LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 709 RKGFPSRILYGDFKQRYKVLNasaipegqfidskkasekllasididhTQYKFGHTKVFFK 769
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
104-769 |
5.50e-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: 445.89 E-value: 5.50e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 179
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 180 TGESGAGKTVNTKRVIQYFAtiavtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML-LITTNPYDYAFVSQGEITVPSI--DDQEELMatd 336
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYgLLDPGKYRYLNNGAGCKREVQYwkKKYDEVC--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 337 SAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14889 228 NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 416 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd14889 308 RHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFqkp 569
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYY--- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 570 KVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYAS------AEADSSAKKGAKKK 643
Cdd:cd14889 461 GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSrtgtlmPRAKLPQAGSDNFN 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 644 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 723
Cdd:cd14889 540 STRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1331883584 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 |
1.45e-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: 444.39 E-value: 1.45e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAvtgekkkdesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA----------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 339
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSANFQKPKVVKgka 576
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 577 eAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyaSAEADSSAKKGAK-KKGSSFQTVSALFR 655
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG---SSEAPSETKEGKSgKGTKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 656 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 735
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|....*
gi 1331883584 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 |
7.74e-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: 7.74e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyKPEVvAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 176
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 177 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQG--------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSkkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 249 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQ-GEITVPSI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 327 DDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLQSLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 403 CYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 561 GKSANFQKPKvVKGKAEAhFSLIHYAGTVDYNITGWLDKNkdplNDTVVglyqksamKTLASLFSTyasaeadssakkga 640
Cdd:cd14891 475 KRHPCFPRPH-PKDMREM-FIVKHYAGTVSYTIGSFIDKN----NDIIP--------EDFEDLLAS-------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 641 kkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGD 720
Cdd:cd14891 527 ----------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 721 FKQRYKVLNASAI------PEGQFIdskkasEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14891 597 LVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
26-828 |
1.22e-129 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 427.91 E-value: 1.22e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 26 RIEAQNKPFDAKTSVFV-------------AEPKESYVKSTIQ-SKEGGKITVK---TEGGATLTVREDQVF----PMNP 84
Cdd:PTZ00014 16 RRNSNVEAFDKSGNVLKgfyvwtdkapavkEDPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 85 PKYDkieDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR-GKKRQEAPPHIFSISDN 163
Cdd:PTZ00014 96 MTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 164 AYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiavtgekkkDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDN 243
Cdd:PTZ00014 173 ALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS---------SKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 244 SSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITV 323
Cdd:PTZ00014 244 SSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCLDV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 324 PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-----PDGTEVADKAAYLQSLNSADL 398
Cdd:PTZ00014 323 PGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 399 LKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:PTZ00014 403 KKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKPLGIFSILEEECMFPKATDTSFK 552
Cdd:PTZ00014 483 LFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 553 NKLYDQhLGKSANFQKPKVVKGKaeaHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaEA 632
Cdd:PTZ00014 557 SSCNTN-LKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF------EG 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 633 DSSAKKGAKKKgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 712
Cdd:PTZ00014 627 VEVEKGKLAKG----QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGF 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 713 PSRILYGDFKQRYKVLNAsAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQ---IIT 789
Cdd:PTZ00014 703 SYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVS 781
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1331883584 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 |
7.49e-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: 7.49e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 171
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 172 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKM-QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 251 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---TSNKKPDLIEMLLITTN----PYDYAFVSQGEI-T 322
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLlrgGDEEEHEKYEFHDGITGglqlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 323 VPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLQSLNSADLL 399
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 400 KALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLE 477
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 478 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFP-KATDTSFKNKL 555
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 556 YDQHL-------GKSANFQKPKVVKGKaeAHFSLIHYAGTVDYNI-TGWLDKNKDPLNdtvvglyqksamKTLASLFSTy 627
Cdd:cd14908 480 YETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIP------------LTADSLFES- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 628 asaeadssakkgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 707
Cdd:cd14908 545 -----------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 708 CRKGFPSRILYGDFKQRYKVLnASAIPE----------------GQFIDSKKA----SEKLLASIDIDHTQYKFGHTKVF 767
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldpqklcVKKMCKDLVkgvlSPAMVSMKNIPEDTMQLGKSKVF 680
|
..
gi 1331883584 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 |
5.54e-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: 5.54e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP---------VYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFML-TD 171
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 172 RENQSILITGESGAGKTVNTKRVIQYFATIAVT---GEKKKDESGKMQgtleDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDqssTEQEGSDAVEIG----KRILQTNPILESFGNAQTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 249 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEmLLITTNPYDYAFVSQGEIT-----V 323
Cdd:cd14902 157 KFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSfarkrA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 324 PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLQSLNSA 396
Cdd:cd14902 236 VADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 397 DLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAG 467
Cdd:cd14902 312 KLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 468 FEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKA 546
Cdd:cd14902 392 FESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 547 TDTSFKNKLYDQHLGksanfqkpkvvkgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS- 625
Cdd:cd14902 471 SNQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAd 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 626 -TYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 704
Cdd:cd14902 536 eNRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEA 615
|
650 660
....*....|....*....|..
gi 1331883584 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 |
5.08e-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: 5.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKpevVAAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 171
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 172 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSS-SKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 252 RIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPD-LIEMLLITTNPYDYAFVSQGEITV-- 323
Cdd:cd14895 157 RMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQrn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 324 PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------------D 385
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 386 KAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY------- 458
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 459 ----FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGI 533
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 534 FSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQ 613
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 614 KSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVS----ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEH 689
Cdd:cd14895 553 KTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSvgigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 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 |
7.49e-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: 7.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAvtgekkkdeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAK---------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTnPYDYAFVSQGEITVPSIDDQEELMATDSAID 340
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLESLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14876 231 SMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 416 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 496 MFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQKP 569
Cdd:cd14876 391 VFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFKPA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 570 KVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFstyasaeadsSAKKGAKKKGSSFQT 649
Cdd:cd14876 464 KV---DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF----------EGVVVEKGKIAKGSL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 650 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 729
Cdd:cd14876 531 IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1331883584 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 |
1.19e-120 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 396.46 E-value: 1.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIavtgEKKKDESGKMQgtLEDQIisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKL 261
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQ--PEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEI-TVPSIDDQEELMATDSAID 340
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLQSlnSADLLKALCYPRVKVGN-EYVTK 416
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQV--PPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 417 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 495 HMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvk 573
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 574 gkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKgakkkgssfqTVSAL 653
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------TLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 654 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAI 733
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*.
gi 1331883584 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 |
1.75e-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: 1.75e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 179
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 180 TGESGAGKTVNTKRVIQYFATIAVTgeKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS--PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVpsidDQEELMATDSAI 339
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGA-AFSWLPNPERNL----EEDCFEVTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 340 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEyvtk 416
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQ---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 417 gqtvQQVYNAV----------GALAKAVYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14880 312 ----QQVFKKPcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYAN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSA 564
Cdd:cd14880 388 EKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 565 NFQKPKVVKgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyasAEADSSAKKGAKKKG 644
Cdd:cd14880 467 CLGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPA---NPEEKTQEEPSGQSR 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 645 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 724
Cdd:cd14880 541 APVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVER 620
|
....
gi 1331883584 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 |
5.08e-108 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 362.76 E-value: 5.08e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTGK 260
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 LASADIETYLLEKSRVTFQL-KAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQ---------- 329
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 330 -----EELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLQSLNSADLLKA 401
Cdd:cd14906 243 ktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 402 LCYPRVKVGNE--YVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIAGF 468
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKAT 547
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 548 DTSFKNKLYDQHLGKSANFQKPkvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY 627
Cdd:cd14906 482 EQSLLEKYNKQYHNTNQYYQRT-----LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 628 ASAEADSSAKKGAKKkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRI 707
Cdd:cd14906 557 ITSTTNTTKKQTQSN------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKV 630
|
650 660
....*....|....*....|....
gi 1331883584 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 |
1.73e-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: 353.04 E-value: 1.73e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 108 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 181
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYFATIAVTGEKKkdesgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD----------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEI-TVPSIDDQEELMATDSAID 340
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 341 ILgFTPEEKVSIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 418 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-LGIFSILEEECMFPKATDTSFKNKLyDQHLgKSANFqkpkvVKGK- 575
Cdd:cd14886 395 KSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPGKg 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 576 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAkkgakkkgssfQTVSALFR 655
Cdd:cd14886 467 SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG-----------KFLGSTFQ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 656 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL---NASA 732
Cdd:cd14886 536 LSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSS 615
|
650 660 670
....*....|....*....|....*....|....*..
gi 1331883584 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 |
4.75e-105 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 354.02 E-value: 4.75e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAY----------RGKKRQEAPPHIFSISDNAYQFMLTDR 172
Cdd:cd14899 3 ILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 173 ENQSILITGESGAGKTVNTKRVIQYFA-------TIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14899 83 RSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 246 RFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNK----KPDLIEMLLITTNPYDYAFVSQGE 320
Cdd:cd14899 163 RFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 321 ITV--PSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------DK 386
Cdd:cd14899 243 CSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfTK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 387 AAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL---------------D 451
Cdd:cd14899 323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdvD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 452 TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KP 530
Cdd:cd14899 403 DEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhRP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 531 LGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVG 610
Cdd:cd14899 482 IGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQ 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 611 LYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSAL--------FRENLNKLMTNLRSTHPHFVRCIIPNETK 682
Cdd:cd14899 562 LLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDSH 641
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1331883584 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 |
1.00e-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: 351.42 E-value: 1.00e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 180
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFatiavtGEKKKDESGK-MQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14875 83 GESGSGKTENAKMLIAYL------GQLSYMHSSNtSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 256 -GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITV------PSIDD 328
Cdd:cd14875 157 dPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 329 QEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQsLNSADLLKalCYpRVK 408
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LVK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 409 VGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINFT 484
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 485 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKS 563
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 564 ANFQKPkvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASaEADSSakkgakkk 643
Cdd:cd14875 470 PYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKG-LARRK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 644 gssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF-K 722
Cdd:cd14875 538 ----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 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 |
4.16e-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: 4.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 182
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 183 SGAGKTVNTKRVIQYFATIA------VTGEKkkdesgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 256
Cdd:cd01386 82 SGSGKTTNCRHILEYLVTAAgsvggvLSVEK---------------LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 257 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvsqgeITVPSIDDQE------ 330
Cdd:cd01386 147 QAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF-----GIVPLQKPEDkqkaaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 331 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLQSLNSADLLKALCYPRV 407
Cdd:cd01386 222 AFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 408 KVGNEYVT---------------KGQTVQQvynAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD 472
Cdd:cd01386 299 SGGPQQSTtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 473 FN------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL--------------- 531
Cdd:cd01386 376 HSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedrr 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 532 GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKgKAEA--HFSLIHYAGT--VDYNITGWLDKNK-DPLND 606
Cdd:cd01386 456 GLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 607 TVVGLYQKSAMKTLA----SLFStyasaeadssakkgakkkGSSFQtvsalfrenLNKLMTNLRSTHPHFVRCIIPN--- 679
Cdd:cd01386 534 NATQLLQESQKETAAvkrkSPCL------------------QIKFQ---------VDALIDTLRRTGLHFVHCLLPQhna 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 680 ---ETKTPGAMEHELVLH------QLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL----NASAIPEGQFIDSKKASE 746
Cdd:cd01386 587 gkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVE 666
|
730 740
....*....|....*....|...
gi 1331883584 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 |
2.15e-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: 2.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvykpEVVAAYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSIL 178
Cdd:cd14898 3 TLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 179 ITGESGAGKTVNTKRVIQYFAtiavtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgtT 258
Cdd:cd14898 74 ISGESGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpdliemLLITTNPYDYAFVSQGEITVpsIDDQEELMATDSA 338
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 339 IDILGFTPEEkvSIYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14898 213 MKSLGIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 419 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 499 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKAT--DTSFKNKLYDQHLgksanfqkpkvVKGKA 576
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGF-----------INTKA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGlyqksamktlASLFSTYASAEadssakkgakkkgssfqTVSALFRE 656
Cdd:cd14898 434 RDKIKVSHYAGDVEYDLRDFLDKNREKGQLLIFK----------NLLINDEGSKE-----------------DLVKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 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 |
2.89e-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: 2.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14878 3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATiavtgekkkdESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14878 83 GERGSGKTEASKQIMKHLTC----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 261 -LASADIETYLLEKSRVTFQLKAERSYHIFY----QITSNKKPDLIemlliTTNPYDYAFVSQGE----ITVPSIDDQEE 331
Cdd:cd14878 153 hLTGARIYTYMLEKSRLVSQPPGQSNFLIFYllmdGLSAEEKYGLH-----LNNLCAHRYLNQTMredvSTAERSLNREK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 332 LMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGN 411
Cdd:cd14878 228 LAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 412 EYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14878 308 DMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 488 LQQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANF 566
Cdd:cd14878 388 MHHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNA 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 567 QKPKVVKGKAE-------AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyasaeadssakkg 639
Cdd:cd14878 468 VYSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 640 akkkgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYG 719
Cdd:cd14878 535 ------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFS 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 720 DFKQRYKVLnASAIPEGQfidsKKASEKLLASIDIDHTQ---YKFGHTKVFFK 769
Cdd:cd14878 609 DFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
102-769 |
8.84e-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: 8.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 173
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 174 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkdesGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 253
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH----GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 254 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpdliemllittnpydyafVSQGEITVPSIDDQE--E 331
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAV------------------AAATQKSSAGEGDPEstD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 332 LMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLQSLNS----- 395
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 396 -------ADLLKALCYPRVKVGNEYVTKGQTVQQV------YNAVGALA------KAVYEKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVretrsfFDLDGAAAardaacKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 516 FGMDLAAC--------IELIEKP--------------LGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SANFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 569 PKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVvglyqksamKTLASLFSTYASaEADSSAKKGAKKKGSSFQ 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDEL---------ERLFLACSTYTR-LVGSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 649 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 728
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1331883584 729 NASAIPEgqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 769
Cdd:cd14887 687 LPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
104-769 |
1.16e-87 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 300.78 E-value: 1.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEvvaaYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYFatiaVTGEKKKDEsgkMQGTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNE---ISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPyDYAFVSQGEITVPSIDDQEELMATDSAIDILG 343
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 344 FTPEEKVSIYKLTGAVMhYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14937 227 MHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 419 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 499 LEQEEYKKEGIEWTFIDFGMDlAACIELIEKPLGIFSILEEECMFPKATDTSfknkLYDQHLGKSANFQKPKVVKGKAEA 578
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 579 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLfstYASAEADSSAKKGakkkgssfQTVSALFRENL 658
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL---YEDVEVSESLGRK--------NLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 659 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYGDFKQRYKVLNASAIPEGQF 738
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 1331883584 739 IDSKKASEKLLASIDIDhtQYKFGHTKVFFK 769
Cdd:cd14937 609 TDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| 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 1331883584 108 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYKPEVVAAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 177
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 178 LITGESGAGKTVNTKRVIQYFATIAVTGEKkkdesgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 256
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK---------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 257 TTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFV--SQGEITV--PSIDDQE- 330
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPlgPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 331 --ELMAtdsAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR 406
Cdd:cd14879 237 fqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 407 VKVGNEYVTkgqtvqqVY-NAVGA------LAKAVYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---FNS 475
Cdd:cd14879 314 KLVRKELCT-------VFlDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGNS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 476 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEEC-MFPKATDTSFKN 553
Cdd:cd14879 387 LDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 554 KLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLN-DTVvglyqksamktlaSLFSTyasaea 632
Cdd:cd14879 466 ALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSpDFV-------------NLLRG------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 633 dssakkgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGF 712
Cdd:cd14879 527 ------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEY 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 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 |
1.90e-75 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 266.39 E-value: 1.90e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 173
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 174 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkdeSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRINL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 253 IHFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGE--- 320
Cdd:cd14884 151 LIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 321 ---------ITVPSIDDQEELMATDSA-----IDILGFTPEEKVSI---YKLTGAVMHYGNMKFKQkqreeqaepdgtev 383
Cdd:cd14884 231 krsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA-------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 384 adkAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRIN---------QQLDTKQ 454
Cdd:cd14884 297 ---AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDNED 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 455 PRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF--GMDLAACIELIEK 529
Cdd:cd14884 374 IYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAKIFR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 530 PLGIFSILEEECMfpKATDTSFKNKLYD----QHLGK--SANFQKPKVVKGKAEAH------FSLIHYAGTVDYNITGWL 597
Cdd:cd14884 454 RLDDITKLKNQGQ--KKTDDHFFRYLLNnerqQQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRINNWI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 598 DKNKDPLNDTVVGLYQKSAMKTLaslfstyasaeadssAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCII 677
Cdd:cd14884 532 DKNSDKIETSIETLISCSSNRFL---------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFL 596
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1331883584 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 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyKPEVVAAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14881 3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVI-QYFAtiaVTGEKKKDESGKmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKLA 262
Cdd:cd14881 78 GSGKTYASMLLLrQLFD---VAGGGPETDAFK-------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGALY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 263 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPD-LIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14881 147 RTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEeRVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLGI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LG--FTpeekvSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLqSLNSADLLKALcYPRVKVgneyvTKGQT 419
Cdd:cd14881 227 LGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----ARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 420 VQQVYNA------VGALAKAVYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14881 295 VKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 489 QQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PLGIFSILEEECMfPKATDTSFKNKLYDQHLGkSANF 566
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-NPRL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 567 QKPKVVKGKAeahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKsamKTLASLFSTYASaeadssakkgakkkgsS 646
Cdd:cd14881 452 FEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK---QNCNFGFATHTQ----------------D 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 647 FQTvsalfreNLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14881 510 FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYR 582
|
650 660
....*....|....*....|....*
gi 1331883584 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 |
9.25e-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: 239.39 E-value: 9.25e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 103 GVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 181
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 182 ESGAGKTVNTKRVIQYfatiaVTGEKKKDESGKMQGTLEDqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14874 72 ESGSGKSYNAFQVFKY-----LTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 341
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 342 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLQSLNSADLLKALCyPRVKVGNEYvtk 416
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 417 gqTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 496 MFVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSAnFQKpk 570
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK-- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 571 vVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADssakkgakkkgsSFQTV 650
Cdd:cd14874 444 -ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSD------------MIVSQ 510
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 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 1331883584 108 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYKPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 186
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 187 KTVNTKRVIQYFATIAVTGEKkkdesgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 266
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK----------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 267 ETYLLEKSRVTFQLKAERSYHIFYQ----ITSNKKPdliEMLLITTNPYDYaFVSQGEITVPSIDDQEELMATDSAIDIL 342
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQflkgITDEEKA---AYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 343 GFtPEEKVS-IYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKaAYLQSLNsadllKALCYPRVKVGNEYVT-KGQTV 420
Cdd:cd14905 231 DF-PSEKIDlIFKTLSFIIILGNVTFFQKNGK-------TEVKDR-TLIESLS-----HNITFDSTKLENILISdRSMPV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 421 QQVYNAVGALAKAVYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14905 297 NEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 499 LEQEEYKKEGIEW-TFIDFgMDLAACIELIEKplgIFSILEEECMFPKATDTSFKNKLydqhlgksANFQKPKVVKGKAE 577
Cdd:cd14905 374 QEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 578 AHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLAS---LFSTYAS-AEADSSAKKGAKKKGSSFQTVSAL 653
Cdd:cd14905 442 NKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATvAELNQMFDAKNTAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 654 FR------ENLNK-----------------------LMTNLRSTHP---------HFVRCIIPNETKTPGAMEHELVLHQ 695
Cdd:cd14905 522 LScgsnnpNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQ 601
|
650
....*....|....*..
gi 1331883584 696 LRCNGVLEGIRICRKGF 712
Cdd:cd14905 602 IKSLCLLETTRIQRFGY 618
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
105-726 |
9.59e-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: 9.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 105 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 174
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 175 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGK--MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGAsgVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 253 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK--PDLIEMLLITTNPYDYAFVSQG--EITVPSID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 328 -DQEELMATDSAIDIlgfTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYL-----QSLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 400 KAlcYPRV------------KVGNEYVT--KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 528 E-KPLGIFSILEEECMFPKATDTSFKNKLY--DQHLG------KSANFQKPKVVKGKA-EAHFSLIHYAGTVDYNITGWL 597
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglsrpnMGADTTNEYLAPSKDwRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 598 DKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSSAKKGAKKKGSSFQTVSALFRENLN--------------K 660
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaaASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 661 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 726
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
104-769 |
1.08e-65 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 236.56 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 104 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 183
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 184 GAGKTVNTKRVIQYfatIAVTGEKKKDESGKmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 263
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGDGNRGATGR--------VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 264 ADIETYLLEKSRVTFQLKAERSYHIFYQI--TSNKKPDLIEMLLITTNPYDYAFVSQG-------------EITVPSIDD 328
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFydFIEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 329 QEELMAtdsaidILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLQSLNSADLLKALCYPRVK 408
Cdd:cd14882 232 FEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 409 VGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEecmfpKATDTSFKNKLYDQHLGKS 563
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 564 ANFQKPkvvkgkAEAH-FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTyasaeadssakkgakK 642
Cdd:cd14882 457 SQFVKK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------S 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 643 KGSSFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 718
Cdd:cd14882 516 QVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 719 GDFKQRYKVLnasAIPEGQFIDSKKASEKLLAsIDIDHTQYKFGHTKVFFK 769
Cdd:cd14882 596 QEFLRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
124-253 |
4.06e-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: 4.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 124 FCVTVNPYKWLPVYKPEVV-AAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 202
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 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 |
1.47e-43 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 171.17 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 102 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 180
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 181 GESGAGKTVNTKRVIQYFATIAVTGE-------------KKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRrlptnlndqeednIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 248 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 328 DQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 384
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 385 DKAAYLQS-LNSADLLKALCYPRVK-VGNEYV-TKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-- 459
Cdd:cd14938 319 VKNLLLACkLLSFDIETFVKYFTTNyIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtn 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 460 -IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL--GIFSI 536
Cdd:cd14938 399 yINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 537 LEEECMfPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSA 616
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 617 MKTLASLFSTYasaEADSSAKKGAKKKGSSFQTVSALF---------------RENLNKLMTNLRSTHPHFVRCIIPNET 681
Cdd:cd14938 557 NEYMRQFCMFY---NYDNSGNIVEEKRRYSIQSALKLFkrrydtknqmavsllRNNLTELEKLQETTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 682 KTP-GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAsaipegqfiDSKKASEKLLASIDIDHTQYK 760
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 1331883584 761 FGHTKVF 767
Cdd:cd14938 705 IGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1147-1929 |
2.39e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 137.88 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1147 EEISERLEEAGGATsaqvelnkkreaefqKLRRDLEEATLQHEAMAAALrKKHADSMAELAEQIDNLQRVKQKLEK---- 1222
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykel 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1223 -------EKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLD 1295
Cdd:TIGR02168 219 kaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1296 EKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWR 1375
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1376 TKYETDAiQRTEELEEAKKKLAQRLQEAEEHVEavnakcaSLEKTKQRLQNEVEDLmlDVERSNAACAALDKKQRNFDKV 1455
Cdd:TIGR02168 379 EQLETLR-SKVAQLELQIASLNNEIERLEARLE-------RLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1456 LSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEES---LDQLETLRRENKNLQQEISDLTEQiAEGGKQIHEL--E 1530
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVlsE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1531 KIKKQVEQEKCeIQAALEEAEASL--EHEEGKILRIQLeLNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEI 1608
Cdd:TIGR02168 528 LISVDEGYEAA-IEAALGGRLQAVvvENLNAAKKAIAF-LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1609 RSRNDALRVKKKMEGDLNEMEI--QLNHANRLAAESLRNYRNtqgILKETQLHLDDALQGQEDLKEQLAIVERRAnllqa 1686
Cdd:TIGR02168 606 DLVKFDPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRI---VTLDGDLVRPGGVITGGSAKTNSSILERRR----- 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1687 EIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAA 1766
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1767 MMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVENEQKRNAEAVKGLRKH 1846
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAANLRERLESL 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1847 ERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVK 1926
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
...
gi 1331883584 1927 SRE 1929
Cdd:TIGR02168 910 RSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
966-1902 |
7.46e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 133.26 E-value: 7.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 966 KVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLD--DLQAEEDKVNI--LTKAKTKLEQQVDDLEGSL 1041
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELELalLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1042 EQEKKLRMDLERAKRKLEGDLklaqESTMDIENDKQQLDEKLKKKEFEISNLISKIEdeqaveiqlqKKIKELQARIEEL 1121
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKL----EELRLEVSELEEEIEELQKELYALANEISRLE----------QQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1122 EEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHAd 1201
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1202 SMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEviskakgnlekmcrslEDQVSELKTKEEEQQRLINDLTAQRA 1281
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE----------------EAELKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1282 HLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETK----AKNALAHALQSSRHDGdLLREQYEEEQEGK 1357
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLSGILG-VLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1358 AELQRALSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEEHVEAVNAKCASLEKTKQR 1423
Cdd:TIGR02168 537 AAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1424 LQNEVEDLM---LDVERSNAACAALDKKQRNF-------DKVLSEW--KQKYEETQAELEASQKESRSLSTELFKVKNAY 1491
Cdd:TIGR02168 614 LRKALSYLLggvLVVDDLDNALELAKKLRPGYrivtldgDLVRPGGviTGGSAKTNSSILERRREIEELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1492 EESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEkceiQAALEEAEASLEHEegkilriQLELNQV 1571
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKE-------LTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1572 KSEVDRKIAEKDEEIDQLKRNhtrvvetmqstldaeirsrndalrvKKKMEGDLNEMEIQLNhANRLAAESLRNyrntqg 1651
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAE-------------------------IEELEAQIEQLKEELK-ALREALDELRA------ 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1652 ILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQtersrkiAEQELLDASERVQLLHTQNTSLINTKK 1731
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERA 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1732 KLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEQTVKDL--QHRLDEAEQLALK 1809
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseEYSLTLEEAEALE 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1810 -GGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSykrQAEEA 1888
Cdd:TIGR02168 961 nKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE---RFKDT 1037
|
970
....*....|....*
gi 1331883584 1889 EEQSNANLSK-FRKL 1902
Cdd:TIGR02168 1038 FDQVNENFQRvFPKL 1052
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1133-1912 |
3.62e-29 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 127.49 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1133 SKAEKQRsdlsRELEEISERLEEAggatsaQVELNKKREaEFQKLRRDLEEAtlqhEAMAAALRKKHADSMAELAEQIDN 1212
Cdd:TIGR02169 170 RKKEKAL----EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1213 LQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQ-QRLINDLTAQRAHLQTEAGEYS 1291
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1292 RLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRalskansEV 1371
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------EL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1372 AQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRN 1451
Cdd:TIGR02169 388 KDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1452 FDKVLSEWKQKYEETQAELEASQKEsrslstelfkvknayeesLDQLETLRRENKNLQQEISDLTEQIAEGGKQIH---- 1527
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRE------------------LAEAEAQARASEERVRGGRAVEEVLKASIQGVHgtva 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1528 ELEKIKKQVeQEKCEIQAALEEAEASLEHEEGKILRIQ------------LELNQVKSE-VDRKIAEKDE---------E 1585
Cdd:TIGR02169 529 QLGSVGERY-ATAIEVAAGNRLNNVVVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGvigfavdlvE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1586 IDQLKRN-------HTRVVETMQS-----------TLDAEI-----------RSRNDALRVKKKMEGDLNEMEIQLNHAN 1636
Cdd:TIGR02169 608 FDPKYEPafkyvfgDTLVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLK 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1637 RLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV 1716
Cdd:TIGR02169 688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1717 QLLHTQntsLINTKKKLEN-DVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKD 1795
Cdd:TIGR02169 768 EELEED---LHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1796 LQHRLDE--AEQLALKGGKK----QIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQD 1869
Cdd:TIGR02169 845 LKEQIKSieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1331883584 1870 LVDKLQAKVKSYKRQAEEAEEQSNANLSkFRKLQHELEEAEER 1912
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1592 |
6.09e-27 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 120.56 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 843 LKSAETEKEMATMKEDFQKTKDELAKSE--AKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEA 920
Cdd:TIGR02169 200 LERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 921 KIKEVTERAEEEEEIN-AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEK 999
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1000 KALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQL 1079
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1080 DEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLS---------------- 1143
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggraveevlkas 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1144 --------RELEEISER----LEEAGGATSAQV----ELNKKREAEFQKlRRDLEEAT-LQHEAMAAALRKKHADSMAEL 1206
Cdd:TIGR02169 520 iqgvhgtvAQLGSVGERyataIEVAAGNRLNNVvvedDAVAKEAIELLK-RRKAGRATfLPLNKMRDERRDLSILSEDGV 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1207 AEQIDNLQRVKQKLEK------------EKSE-------------LKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSE 1261
Cdd:TIGR02169 599 IGFAVDLVEFDPKYEPafkyvfgdtlvvEDIEaarrlmgkyrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1262 LKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRH 1341
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1342 DGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTK 1421
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1422 QRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETL 1501
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1502 RRENKNLQQEISDLTEQIAEGGKQIHELEKIK------KQVEQEKCEIQAALEEAE-----ASLEHEEGKILRIQLELNQ 1570
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDELKEKR 995
|
810 820
....*....|....*....|...
gi 1331883584 1571 VKSEVDRK-IAEKDEEIDQLKRN 1592
Cdd:TIGR02169 996 AKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1315-1936 |
9.97e-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: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1315 IEELKHQLEE-ETKAKNALA-HALQS--SRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdAIQRTEELE 1390
Cdd:TIGR02168 195 LNELERQLKSlERQAEKAERyKELKAelRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1391 EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAEL 1470
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1471 EASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEA 1550
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1551 EASLEHEEGKILRIQLE--------LNQVKSEVDRKIAEKDEEIDQLKRNHTR------VVETMQSTLDAEIRSRNDALR 1616
Cdd:TIGR02168 434 ELKELQAELEELEEELEelqeelerLEEALEELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1617 VKKKMEGDLN--------------EMEIQL-NHANRLAAESLRNYRNTQGILKETQLH---------------------- 1659
Cdd:TIGR02168 514 NQSGLSGILGvlselisvdegyeaAIEAALgGRLQAVVVENLNAAKKAIAFLKQNELGrvtflpldsikgteiqgndrei 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1660 -------------------------------------LDDALQGQEDLKEQLAIV------------------ERRANLL 1684
Cdd:TIGR02168 594 lkniegflgvakdlvkfdpklrkalsyllggvlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsaKTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1685 --QAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAI 1762
Cdd:TIGR02168 674 erRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1763 TDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKG 1842
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1843 LRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNK 1922
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
730
....*....|....
gi 1331883584 1923 LRVKSREVHTKVSA 1936
Cdd:TIGR02168 913 LRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1611 |
3.84e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.85 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 846 AETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEV 925
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 926 TERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQET 1005
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1006 HQQTLDDLQAEEDKVNILTKAKTKL-----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLD 1080
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1081 EKLKKKEFEISNLISKIEDEQaveiQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEE-----ISERLEE 1155
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLE----GFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNA 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1156 AGGATSAQVELNKKREA--------EFQKLRRDLEEATLQHEAMAAALRKKHADSMAELA-----------EQIDNLQRV 1216
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvDDLDNALEL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1217 KQKLEKEKSELKMEiDDLSSNAEVISK--AKGNLEKMCRSLEdqVSELKTKEEEQQRLINDLTAQRAHLQTEageysrlL 1294
Cdd:TIGR02168 638 AKKLRPGYRIVTLD-GDLVRPGGVITGgsAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKE-------L 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1295 DEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQW 1374
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1375 RtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDK 1454
Cdd:TIGR02168 788 E--------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1455 VLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELE-KIK 1533
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvRID 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1534 KQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-------------KIAEKDEEIDQLKRNHTRVVETM 1600
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeyeELKERYDFLTAQKEDLTEAKETL 1019
|
810
....*....|....
gi 1331883584 1601 QST---LDAEIRSR 1611
Cdd:TIGR02168 1020 EEAieeIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
981-1806 |
4.14e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.48 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 981 LTEEMAGLDEIIAKLSKEKKALQETHQQtLDDLQAEEDKVNiltkaktkleQQVDDLEGslEQEKKLR-MDLERAKRKLE 1059
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1060 GDLKLAQESTMD-----IENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERAS-RS 1133
Cdd:TIGR02169 225 GYELLKEKEALErqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1134 KAEKQRSDLSRELEEISERLEEAggatsaQVELNKKREaEFQKLRRDLEEATLQHEAMA---AALRKKHADSMAELAEQI 1210
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKL------EAEIDKLLA-EIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1211 DNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEY 1290
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1291 SRLLDEKDALVSQLsRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEG-----------KAE 1359
Cdd:TIGR02169 458 EQLAADLSKYEQEL-YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaqlgsvGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1360 LQRALSKA-----------NSEVAQWRTKYETD------------AIQRTEELEEAKKK-----LAQRLQEAEEHVEAVN 1411
Cdd:TIGR02169 537 YATAIEVAagnrlnnvvveDDAVAKEAIELLKRrkagratflplnKMRDERRDLSILSEdgvigFAVDLVEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1412 AKC-------ASLEkTKQRLQNEVEDLMLD---VERSNAACAALDKKQRNFDKVLSEwKQKYEETQAELEASQKESRSLS 1481
Cdd:TIGR02169 617 KYVfgdtlvvEDIE-AARRLMGKYRMVTLEgelFEKSGAMTGGSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1482 TELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKI 1561
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1562 LRIQLELNQVKSEVDR-KIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEG---DLNEMEIQLNHANR 1637
Cdd:TIGR02169 775 HKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElqeQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1638 LAAESLRNYRNTQGILKETQLHLddalqgqEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1717
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1718 LLHTQNTSLINTKKKLENDVSqlQTEVEEVIQESRNAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKNLEQTVKDL 1796
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPE--EELSLEDVQAELQRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
890
....*....|
gi 1331883584 1797 QHRLDEAEQL 1806
Cdd:TIGR02169 1006 LERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
945-1750 |
1.18e-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: 116.31 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 945 KLEDECSELKKDIDDLELTLAKVEK--EKHATENKVKN--LTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKV 1020
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQAEKAERykELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1021 NILTKAKTKLEQQVDDLEGSLEQEK----KLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLD---EKLKKKEFEISNL 1093
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALAneisRLEQQKQILRERLANLERQLEELEAQLEELESKLDelaEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1094 ISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAE 1173
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1174 FQKLRRDLEEATL-QHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKmeidDLSSNAEVISKAKGNLEKMC 1252
Cdd:TIGR02168 430 LEEAELKELQAELeELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA----QLQARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1253 RSLE-------------DQVSELKTKEEEQQRLINdlTAQRAHLQteageySRLLDEKDALVSQLSRRKQASTQQIEELK 1319
Cdd:TIGR02168 506 EGVKallknqsglsgilGVLSELISVDEGYEAAIE--AALGGRLQ------AVVVENLNAAKKAIAFLKQNELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1320 HQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKA-------------ELQRALSKANSEVAQWR----------- 1375
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrp 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1376 ----TKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRN 1451
Cdd:TIGR02168 658 ggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1452 FDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEK 1531
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1532 -------IKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDrKIAEKDEEIDQLKRNHTRVVETMQSTL 1604
Cdd:TIGR02168 818 eaanlreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1605 DAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKET-QLHLDDALQGQEDLKEQLAIVERRANL 1683
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKR 976
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1684 LQAEIEEL-RATLEqtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQE 1750
Cdd:TIGR02168 977 LENKIKELgPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1315-1924 |
1.24e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1315 IEELKHQLEE-ETKAKNAL-AHALQSS--RHDGDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdAIQRTEELE 1390
Cdd:COG1196 195 LGELERQLEPlERQAEKAErYRELKEElkELEAELLLLKLRELEAELEELEAELEELEAELEE--------LEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1391 EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAEL 1470
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1471 EASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEA 1550
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1551 EASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRnhtrvvetmqstLDAEIRSRNDALRVKKKMEGDLNEMEI 1630
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE------------LLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1631 QLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKiaeQELL 1710
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK---AAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1711 DASERVQLlhtqntSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLE 1790
Cdd:COG1196 572 GRATFLPL------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1791 QTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAvkgLRKHERRVKELTYQTEEDRKNVLRLQDL 1870
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE---LEEALLAEEEEERELAEAEEERLEEELE 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1871 VDKLQAKVKSYKRQAEEAEEQSNANLSkfrKLQHELEEAEERADIAESQVNKLR 1924
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLE 773
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-714 |
4.14e-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: 104.05 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 292 ITS--NKKP--------------DLIEMLLITTNPYDYA-FVSQGEITVPSIDDQEELMatdSAIDILGFTPEEKVSIYK 354
Cdd:cd14894 329 MVAgvNAFPfmrllakelhldgiDCSALTYLGRSDHKLAgFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 355 LTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLQSLNSADLL-KALCYPRVKVGNEYVTKGQTVQ--QVYNAVG 428
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 429 ALAKAVYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLqqF 491
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--Y 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 492 FNHHMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPLGIFSILEEECMFPKATDTSF-----KNKLYDQHL--GKSA 564
Cdd:cd14894 564 AREEQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 565 NFQKPKVVKGKAEAH---------FSLIHYAGTVDYNITGWLDKNKDPL-NDTVVGLYQKSAMKTLASLFSTYA---SAE 631
Cdd:cd14894 638 RLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQlgwSPN 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 632 ADSSAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKG 711
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNS 797
|
...
gi 1331883584 712 FPS 714
Cdd:cd14894 798 SSS 800
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1138-1750 |
4.79e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 4.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1138 QRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHAdSMAELAEQIDNLQRVK 1217
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1218 QKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEE-QQRLINDLTAQRAHLQTEAGEYSRLLDE 1296
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1297 KDALVSQLSRRKQAStQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRT 1376
Cdd:COG1196 392 LRAAAELAAQLEELE-EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1377 KYETDA---IQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERS------NAACAALDK 1447
Cdd:COG1196 471 EAALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeaaleAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1448 KQRNFDKVLS---EWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGK 1524
Cdd:COG1196 551 IVVEDDEVAAaaiEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1525 QIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTL 1604
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1605 DAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAEslrnyrntqgilketqlhLDDALQGQEDLKEQLAIVERRANLL 1684
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL------------------LEEEALEELPEPPDLEELERELERL 772
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 1685 QAEIEEL-----RatleqtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQE 1750
Cdd:COG1196 773 EREIEALgpvnlL------------AIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1431 |
9.29e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.09 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 843 LKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKI 922
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 923 KEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKAL 1002
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1003 QETHQQTLDDLQAEEdkvniltKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEK 1082
Cdd:COG1196 378 EEELEELAEELLEAL-------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1083 LKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEeleeeieaerasrskAEKQRSDLSRELEEISERLEEAGGATSA 1162
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELA---------------EAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1163 QVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAE--- 1239
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALarg 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1240 VISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELK 1319
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1320 HQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQwrtKYETDAIQRTEELEEAKKKLAQR 1399
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ---LEAEREELLEELLEEEELLEEEA 752
|
570 580 590
....*....|....*....|....*....|..
gi 1331883584 1400 LQEAEEHVEAvnakcASLEKTKQRLQNEVEDL 1431
Cdd:COG1196 753 LEELPEPPDL-----EELERELERLEREIEAL 779
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
966-1866 |
1.79e-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: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 966 KVEKEKHATENKVKNLTEEMAGLDEIIaklsKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEK 1045
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKR----KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1046 KLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEI 1125
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1126 EAErasRSKAEKQRSDLSRELEEISERLEEAggatSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAE 1205
Cdd:pfam02463 299 KSE---LLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1206 LAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQT 1285
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1286 EAgEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALS 1365
Cdd:pfam02463 452 EL-EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1366 KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAAL 1445
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1446 DKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNA-----YEESLDQLETLRRENKNLQQEISDLTEQIA 1520
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1521 EGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrvVETM 1600
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK----EEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1601 QSTLDAEIRSRndalrvkKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERR 1680
Cdd:pfam02463 767 SELSLKEKELA-------EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1681 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENdvsqLQTEVEEVIQESRNAEEKAKK 1760
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK----EKEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1761 AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAV 1840
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890 900
....*....|....*....|....*.
gi 1331883584 1841 KGLRKHERRVKELTYQTEEDRKNVLR 1866
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1432 |
2.45e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.94 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 842 LLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAK 921
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 922 IKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKA 1001
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1002 LQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDE 1081
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1082 KLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQ--RSDLSRELEEISERLEEAGGA 1159
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvlIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1160 TSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDnlqRVKQKLEKEKSELKMEIDDLSSNAE 1239
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1240 VISKAKGNLEKMCRSLEDQVSElkTKEEEQQRLINDLTAQRAHLQTEAgeysrlLDEKDALVSQLSRRKQASTQQIEELK 1319
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAA------LLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1320 HQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQR 1399
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1331883584 1400 LQE-------AEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1432
Cdd:COG1196 776 IEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
939-1536 |
7.97e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.01 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 939 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEED 1018
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1019 KVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIE 1098
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1099 DEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLR 1178
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1179 RDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKlekeksELKMEIDDLSSNAEVISKAKGNLekmcrsLEDQ 1258
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG------AVAVLIGVEAAYEAALEAALAAA------LQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1259 VSELktkEEEQQRLINDLTAQRAHLQTEAgeysRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEEtKAKNALAHALQS 1338
Cdd:COG1196 552 VVED---DEVAAAAIEYLKAAKAGRATFL----PLDKIRARAALAAALARGAIGAAVDLVASDLREA-DARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1339 SRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLE 1418
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1419 KTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEE----- 1493
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvn 783
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1331883584 1494 --SLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQV 1536
Cdd:COG1196 784 llAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
833-1438 |
3.88e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 833 MKLFFKIKPLLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLI 912
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 913 KNKIQLEAKikevteraeeeeeinaelTAKKRKLEDECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDEII 992
Cdd:PTZ00121 1342 KKAAEAAKA------------------EAEAAADEAEAAEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 993 AKLSKEKKALQETHQQTLDDLQAEEdkvnilTKAKTKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEGDLKlaqestmdI 1072
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKK--------A 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1073 ENDKQQLDEKLKKKEfeisnLISKIEDEQAVEiQLQKKIKELQarieELEEEIEAERASRSKAEKQRSDLSRELEEISER 1152
Cdd:PTZ00121 1460 EEAKKKAEEAKKADE-----AKKKAEEAKKAD-EAKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1153 LEEAGGATSAQVELNKKREAEFQKLR--RDLEEATLQHEAMAAALRKKHADSMAELAEQIDNlQRVKQKLEKEKSELKME 1230
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1231 IDDLSSNAEVISKAKgnlekmcrsledqvsELKtKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQA 1310
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAE---------------ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1311 STQQIEELKHQLEEETKAKNALAHALQSSRhDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL- 1389
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAk 1750
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 1390 --EEAKKKLAQRLQEAEEHVEAVNAKCASLekTKQRLQNEVEDLMLDVERS 1438
Cdd:PTZ00121 1751 kdEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1599 |
1.74e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 856 KEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvQSEADSLADAEERCEQLIK----NKIQLEAKIKEVTERAEE 931
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDAR---KAEAARKAEEERKAEEARKaedaKKAEAVKKAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 932 EEEINaeltaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlTEEMAGLDEiiAKLSKEKKALQETHQQTLD 1011
Cdd:PTZ00121 1242 AKKAE-----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADE--AKKAEEKKKADEAKKKAEE 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1012 DLQAEEDKVNI------LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEK--- 1082
Cdd:PTZ00121 1314 AKKADEAKKKAeeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkka 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1083 --LKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGAT 1160
Cdd:PTZ00121 1394 deAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1161 SAQVELNKKREAEfqKLRRDLEEATLQ-HEAMAAALRKKHADSM--AELAEQIDNLQRVKQKL---EKEKSELKMEIDDL 1234
Cdd:PTZ00121 1474 EAKKKAEEAKKAD--EAKKKAEEAKKKaDEAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKkadEAKKAEEKKKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1235 sSNAEVISKA--KGNLEKMCRSLEDQVSELKTKEEEQQrlindltAQRAHLQteagEYSRLLDEKDALVSQLSRRKQAST 1312
Cdd:PTZ00121 1552 -KKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKK-------AEEARIE----EVMKLYEEEKKMKAEEAKKAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1313 QQIEELKHQlEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRalsKANSEvaqwrtKYETDAIQRTEELEEA 1392
Cdd:PTZ00121 1620 IKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK---KAEED------KKKAEEAKKAEEDEKK 1689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1393 KKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSnaacaaldKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1473 SQKESRSLSTELFKVKNAY-EESLDQLETLRR-ENKNLQQEISDLTEQIAEGGKQIHELekIKKQVEQEKCEIQAALEEA 1550
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSK 1839
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1331883584 1551 EASLEhEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVET 1599
Cdd:PTZ00121 1840 NMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1431 |
1.94e-19 |
|
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: 95.89 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 844 KSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 924 EVTERAEEeeeinaeltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQ 1003
Cdd:TIGR02168 425 ELLKKLEE---------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1004 ethqQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLE------------------------------- 1052
Cdd:TIGR02168 496 ----RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggrlqavvvenlnaakkaiaflkqnelg 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1053 ------------RAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKefeISNLIS--KIEDEQAVEIQLQKKIKELQARI 1118
Cdd:TIGR02168 572 rvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA---LSYLLGgvLVVDDLDNALELAKKLRPGYRIV 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1119 EELEEEIEAERASRSKAEKQRSDL---SRELEEISERLEEAGG-ATSAQVELNKKR------EAEFQKLRRDLEEATLQH 1188
Cdd:TIGR02168 649 TLDGDLVRPGGVITGGSAKTNSSIlerRREIEELEEKIEELEEkIAELEKALAELRkeleelEEELEQLRKELEELSRQI 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1189 EAMAAALRK------KHADSMA-------ELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSL 1255
Cdd:TIGR02168 729 SALRKDLARleaeveQLEERIAqlskeltELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1256 EDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHA 1335
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1336 LQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCA 1415
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
650
....*....|....*.
gi 1331883584 1416 SLEKTKQRLQNEVEDL 1431
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1086-1922 |
2.44e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1086 KEFEISNLISKIEDEQAVEiqLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVE 1165
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEE--AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1166 LNKKREAEFQKLR--RDLEEATLQHEA-------MAAALRKKHADSMAELAEQIDNLQRVKqklEKEKSELKMEIDDLSS 1236
Cdd:PTZ00121 1155 EIARKAEDARKAEeaRKAEDAKKAEAArkaeevrKAEELRKAEDARKAEAARKAEEERKAE---EARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1237 NAEVISKAkgnlEKMCRSLEDQVSELKTKEEEQQrlINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIE 1316
Cdd:PTZ00121 1232 AEEAKKDA----EEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1317 ELKHQLEEETKAKNALAHAlQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEE---LEEAK 1393
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1394 KKLAQ--RLQEAEEHVEAVNAKCASLEKtKQRLQNEVEDLMLDVERSNAACAAldKKQRNFDKVLSEWKQKYEETQAELE 1471
Cdd:PTZ00121 1385 KKAEEkkKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1472 ASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQiAEGGKQIHELEKIKKQVEQEKCEIQAALEEAE 1551
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1552 ASLEHEEGKILRIQLELNqvKSEVDRKIAEKDEEiDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDlnemEIQ 1631
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1632 LNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQT----ERSRKIAEQ 1707
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEA 1693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1708 ELLDASErvqllhtqntslintKKKLEndvsqlqtEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1787
Cdd:PTZ00121 1694 LKKEAEE---------------AKKAE--------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1788 NLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVK--------GLRKHERRVKELTYQTEE 1859
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFdnfaniieGGKEGNLVINDSKEMEDS 1830
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1860 DRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEEraDIAESQVNK 1922
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE--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 |
7.93e-18 |
|
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: 90.62 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1258 QVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSR-------------RKQASTQQIEELKHQLEE 1324
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeemraRLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1325 ETKAKNALAHALQSSR-----HDGDlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQR 1399
Cdd:pfam01576 83 RLEEEEERSQQLQNEKkkmqqHIQD-LEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS-KLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1400 LQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRS 1479
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1480 LSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEG 1559
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1560 KILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLA 1639
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1640 AESLRNYRNTQGILKETQLHLDDALQGQEDLKEqlaiverRANLLQAEIEELRATLEQTE----RSRK---IAEQELLDA 1712
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgkniKLSKdvsSLESQLQDT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1713 SERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQT 1792
Cdd:pfam01576 474 QELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1793 VKDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVEN---EQKRNAEAVKGLRKHERRVKELtyqTEEDRKNVLRLQD 1869
Cdd:pfam01576 554 LEALTQQLEEKAA--------AYDKLEKTKNRLQQELDDllvDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAE 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1870 LVDKLQAkvksykrqaeEAEEQSNANLSkfrkLQHELEEAEERADIAESQVNKLR 1924
Cdd:pfam01576 623 ERDRAEA----------EAREKETRALS----LARALEEALEAKEELERTNKQLR 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1136-1852 |
1.08e-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: 90.18 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1136 EKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATlqHEAMAAALRKKhaDSMAELAEQIDNLQR 1215
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV--HELEAAKCLKE--DMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1216 VKQKLEKEKSELKM-----------EIDDLSSNAEVISKAKGN-LEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAH- 1282
Cdd:pfam15921 178 MMLSHEGVLQEIRSilvdfeeasgkKIYEHDSMSTMHFRSLGSaISKILRELDTEISYLKGRIFPVEDQLEALKSESQNk 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1283 ----LQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLE---EETKAKNALahalqSSRHDGDL---------- 1345
Cdd:pfam15921 258 iellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqEQARNQNSM-----YMRQLSDLestvsqlrse 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1346 LREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEHVeavnakcaSLEKTKQR-- 1423
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKREKEL--------SLEKEQNKrl 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1424 -------------LQNEVEDLMLDVERSNAACAALDKKQRnfdkvlSEWKQKYEETQAELEASQKESrSLSTELFKVKNA 1490
Cdd:pfam15921 404 wdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKSECQ------GQMERQMAAIQGKNESLEKVS-SLTAQLESTKEM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1491 YEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIH----ELEKIKKQVEQEKCEIQaaleeaeaSLEHEEGKILRIQL 1566
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQ--------HLKNEGDHLRNVQT 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1567 ELNQVKSEvdrkIAEKDEEIDQLKRNhtrvVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNY 1646
Cdd:pfam15921 549 ECEALKLQ----MAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1647 RNTQGILKETQLHLDDALQ-GQEDLKEQLAIVERRANLLQaEIEELRATLEQTERSRKIAEQELLDASERVQLlhtqnts 1725
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNaGSERLRAVKDIKQERDQLLN-EVKTSRNELNSLSEDYEVLKRNFRNKSEEMET------- 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1726 linTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHrldeaEQ 1805
Cdd:pfam15921 693 ---TTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANK-----EK 764
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1331883584 1806 LALKGGKKQIQKlearvrELEgEVENEQKRNAEAVKGLRKHERRVKE 1852
Cdd:pfam15921 765 HFLKEEKNKLSQ------ELS-TVATEKNKMAGELEVLRSQERRLKE 804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1458 |
1.78e-17 |
|
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: 89.36 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 844 KSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 924 EVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEK---- 999
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGerya 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1000 KALQETHQQTLDDLQAEEDKV-----NILTKAK---------TKLEQQVDDLE-GSLEQEKKLRMDLERAKRKLEGDLKL 1064
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVakeaiELLKRRKagratflplNKMRDERRDLSiLSEDGVIGFAVDLVEFDPKYEPAFKY 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1065 AQESTM---DIENDKQQLDE----KLKKKEFEISNLI-----------SKIEDEQAVEIQLQKKIKELQARIEELEEEIE 1126
Cdd:TIGR02169 619 VFGDTLvveDIEAARRLMGKyrmvTLEGELFEKSGAMtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1127 AERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLE--EATLQH--------EAMAAALR 1196
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEnvKSELKElearieelEEDLHKLE 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1197 KKHADSMAELA-EQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLIND 1275
Cdd:TIGR02169 779 EALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1276 LTAQRAHLQTEageysrlLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQE 1355
Cdd:TIGR02169 859 LNGKKEELEEE-------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1356 GKAELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDL---- 1431
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIleri 1009
|
650 660
....*....|....*....|....*...
gi 1331883584 1432 -MLDVERSNAACAALDKKQRNFDKVLSE 1458
Cdd:TIGR02169 1010 eEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1625-1926 |
2.36e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1625 LNEMEIQLNHANRlAAESLRNYRNTQGILKETQLHLddALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKI 1704
Cdd:COG1196 195 LGELERQLEPLER-QAEKAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1705 AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1784
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1785 MKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEgEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNV 1864
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1865 LRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVK 1926
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
840-1703 |
3.19e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.49 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 840 KPLLKSAETEKEMATMKEDFQKTKDELAKseakrKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQliKNKIQLE 919
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRLKRKKKEALKKL-----IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL--KEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 920 AKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEK 999
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1000 KALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLE--QEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQ 1077
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1078 QLDEKLKKKEFEISN-LISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEA 1156
Cdd:pfam02463 383 SERLSSAAKLKEEELeLKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1157 GGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSS 1236
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1237 NAEVISKAKGNLEKMCRSLEDQVSEL-----------------KTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDA 1299
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRaltelplgarklrllipKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1300 LVSQLSRRKQASTQQIEELKhQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1379
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAK-AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1380 TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErsnaacaALDKKQRNFDKVLSEW 1459
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1460 KQKYEETQAELEASQKESRSLSTEL-FKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQ 1538
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1539 EKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKR--NHTRVVETMQSTLDAEIRSRNDALR 1616
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1617 VKKKMEGDLNEMEIQLNHANRLAAEsLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLE 1696
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
....*..
gi 1331883584 1697 QTERSRK 1703
Cdd:pfam02463 1014 ETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1073-1803 |
5.35e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.38 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1073 ENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISER 1152
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1153 LEeaggatsAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADsMAELAEQIDNLQRVKQKLEKEKSELKMEID 1232
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1233 DLSSNaevISKAKGNLEKmcrsLEDQVSELKTKEEEQQRL---INDLTAQRAHLQTEAGEysrLLDEKDALVSQLSRRKQ 1309
Cdd:TIGR04523 184 NIQKN---IDKIKNKLLK----LELLLSNLKKKIQKNKSLesqISELKKQNNQLKDNIEK---KQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1310 astqQIEELKhqlEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEvaqWRTKYETDAIQRTEEL 1389
Cdd:TIGR04523 254 ----QLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEKKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1390 EEAKKKLAQrlqeAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAE 1469
Cdd:TIGR04523 324 EEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1470 LEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEE 1549
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1550 AEASLEHEEGKILRIQ---LELNQVKSEVDRKIAEKDEEIDQLKRNhTRVVETMQSTLDAEIRSRNDALrVKKKMEGDLN 1626
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1627 EMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAE 1706
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1707 QELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKA----KKAIT------DAAMMAEELKKEQ 1776
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELslhyKKYITrmirikDLPKLEEKYKEIE 717
|
730 740
....*....|....*....|....*..
gi 1331883584 1777 DTSAHLERMKKNLEQTVKDLQHRLDEA 1803
Cdd:TIGR04523 718 KELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
975-1824 |
6.69e-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: 87.48 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 975 ENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEED-KVNILTKAKTKLEQQVDDL---EGSLEQEKKLRMD 1050
Cdd:pfam15921 116 QTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKClKEDMLEDSNTQIEQLRKMMlshEGVLQEIRSILVD 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1051 LERA--KRKLEGDlklaQESTMDIENDKQQLDEKLKKKEFEISNLISKI------------EDEQAVEIQLQKKIKELQA 1116
Cdd:pfam15921 196 FEEAsgKKIYEHD----SMSTMHFRSLGSAISKILRELDTEISYLKGRIfpvedqlealksESQNKIELLLQQHQDRIEQ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1117 RIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVElnkKREAEFQKLRRDLEEATLQHEAMAAALR 1196
Cdd:pfam15921 272 LISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS---DLESTVSQLRSELREAKRMYEDKIEELE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1197 KKHADSMAELAEQI--------------DNLQRVKQKLEKEKSELKMEIDdlsSNAEVISKAKGN---LEKMCRSLEDQV 1259
Cdd:pfam15921 349 KQLVLANSELTEARterdqfsqesgnldDQLQKLLADLHKREKELSLEKE---QNKRLWDRDTGNsitIDHLRRELDDRN 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1260 SELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEEL---KHQLEEETKAKNALAHAL 1336
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakKMTLESSERTVSDLTASL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1337 QssrhdgdllreqyeeeqegkaELQRALSKANSEVAQWRTKYETdaiqRTEELEEAKKKlAQRLQEAEEHVEAVNAKCAS 1416
Cdd:pfam15921 506 Q---------------------EKERAIEATNAEITKLRSRVDL----KLQELQHLKNE-GDHLRNVQTECEALKLQMAE 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1417 LEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE-----TQAELEASQKESRSLSTELFKVK--N 1489
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkilkDKKDAKIRELEARVSDLELEKVKlvN 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1490 AYEESLDQLETLRREN-------KNLQQEISDLTEQIAEGGKQI----HELEKIKKQVEQEKCEIQAALEEAEASLEHEE 1558
Cdd:pfam15921 640 AGSERLRAVKDIKQERdqllnevKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1559 GKilriQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrvVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQlnhANRL 1638
Cdd:pfam15921 720 GS----DGHAMKVAMGMQKQITAKRGQIDALQSK----IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE---KNKM 788
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1639 AAEsLRNYRNTQGILKETQLHLDDALQgqedlkeqlaiverRANLLQAEIEELRATLEQteRSRKIAEQELLDASERVQL 1718
Cdd:pfam15921 789 AGE-LEVLRSQERRLKEKVANMEVALD--------------KASLQFAECQDIIQRQEQ--ESVRLKLQHTLDVKELQGP 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1719 LHTQNTSLintKKKLENDVSQLQTeveeviQESRNAEEKAKKAITDAAMMAEELKkeqdtsahlERMKKNLEQTVKDLQH 1798
Cdd:pfam15921 852 GYTSNSSM---KPRLLQPASFTRT------HSNVPSSQSTASFLSHHSRKTNALK---------EDPTRDLKQLLQELRS 913
|
890 900 910
....*....|....*....|....*....|.
gi 1331883584 1799 RLDEAEQLAL-----KGGKKQIQKLEARVRE 1824
Cdd:pfam15921 914 VINEEPTVQLskaedKGRAPSLGALDDRVRD 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1290-1917 |
8.26e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.28 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1290 YSRLLDEKDalVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQssrhdgdlLREQYEEEQEGKAELQRALSKANS 1369
Cdd:COG4913 214 REYMLEEPD--TFEAADALVEHFDDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1370 EVAQwrTKYETdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMLDVERSNAACAALD 1446
Cdd:COG4913 284 WFAQ--RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1447 KKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELfkvknayEESLDQLETLRREnknLQQEISDLTEQIAEGGKQI 1526
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL-------EEELEALEEALAE---AEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1527 HELEKIKKQVEQEKCEIQAALEEAeASLEHEEgkiLRIQLELNQVKSE--------------------VD-RKIAEKDEE 1585
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEA-LGLDEAE---LPFVGELIEVRPEeerwrgaiervlggfaltllVPpEHYAAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1586 IDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNH--ANRLA------AESLRNYRntQGILKETQ 1657
Cdd:COG4913 505 VNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1658 LH-------LDDALQGQEDL------KEQLAIVERRANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQLLHTQnt 1724
Cdd:COG4913 583 VKgngtrheKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWD-- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1725 slintkkklENDVSQLQTEVEEVIQEsrnaeekakkaitdaammAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAe 1804
Cdd:COG4913 660 ---------EIDVASAEREIAELEAE------------------LERLDASSDDLAALEEQLEELEAELEELEEELDEL- 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1805 qlalkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKnvlRLQDLVDKLQAKVKSYKRQ 1884
Cdd:COG4913 712 -------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEERIDALRAR 781
|
650 660 670
....*....|....*....|....*....|...
gi 1331883584 1885 AEEAEEQSNANLSKFRKlQHELEEAEERADIAE 1917
Cdd:COG4913 782 LNRAEEELERAMRAFNR-EWPAETADLDADLES 813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1042-1806 |
1.16e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1042 EQEKKLrmdLERAKRKLEGDLKLAQEStmdiENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEEL 1121
Cdd:PTZ00121 1094 EEAFGK---AEEAKKTETGKAEEARKA----EEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1122 EEEIEAERASRSKA-----------------------EKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLR 1178
Cdd:PTZ00121 1167 EEARKAEDAKKAEAarkaeevrkaeelrkaedarkaeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1179 --RDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQR---VKQKLEKEKSELKMEIDDLSSNAEVISKAKgNLEKMCR 1253
Cdd:PTZ00121 1247 eeRNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1254 SLEDQVSELKTKEEEQQRLIN------DLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETK 1327
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEaakaeaEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1328 AKNALAHALQSSRHDGDLLREQYE----EEQEGKAELQRALSKANSEVAQWR----TKYETDAIQRTEEL---------- 1389
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEkkkaDEAKKKAEEAKKADEAKKKAEEAKkaeeAKKKAEEAKKADEAkkkaeeakka 1485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1390 EEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAE 1469
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1470 LEASQKESRSLSTELFK---VKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAA 1546
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKaeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1547 LEEAEASLEHEEGKILRIQLElnQVKSEVDRKIAE--KDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDalRVKKKMEGD 1624
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEE--AKKAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA--EEKKKAEEL 1721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1625 LNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEElRATLEQTERSRKI 1704
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE-EDEKRRMEVDKKI 1800
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1705 aeQELLDASERVQLLHTQNTSLINTKKKLENdvsqlqTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1784
Cdd:PTZ00121 1801 --KDIFDNFANIIEGGKEGNLVINDSKEMED------SAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK 1872
|
810 820
....*....|....*....|..
gi 1331883584 1785 MKKNLEQTVKDLQHRlDEAEQL 1806
Cdd:PTZ00121 1873 EKDLKEDDEEEIEEA-DEIEKI 1893
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1239-1937 |
2.24e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1239 EVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQAStQQIEEL 1318
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA-RKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1319 KHQleEETKAKNALAHALQSSRHDgdllrEQYEEEQEGKAELQRALSKAN--SEVAQWRTKYETDAIQRTEEL----EEA 1392
Cdd:PTZ00121 1170 RKA--EDAKKAEAARKAEEVRKAE-----ELRKAEDARKAEAARKAEEERkaEEARKAEDAKKAEAVKKAEEAkkdaEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1393 KKklAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:PTZ00121 1243 KK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1473 SQK--ESRSLSTELfkvKNAYEESLDQLETLRRENKNLQQEisdlteqiAEGGKQIHELEKIKKQVEQEKCEiqAALEEA 1550
Cdd:PTZ00121 1321 KKKaeEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKAEAAEKKKEEAKKKAD--AAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1551 EASLEHEEgkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALrvKKKMEGDLNEMEI 1630
Cdd:PTZ00121 1388 EEKKKADE---AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA--KKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1631 QLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAE----IEELRATLE--QTERSRKI 1704
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkADEAKKAEEakKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1705 AEQELLDASERVQ-LLHTQNTSLINTKKKLENDVSQLQTEVEEVIQ-ESRNAEEKAKKAITDAAMMAEELKKEQDTSAHL 1782
Cdd:PTZ00121 1543 EEKKKADELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1783 ERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRK 1862
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1863 NVLRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVS 1935
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKaeeenkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
..
gi 1331883584 1936 AE 1937
Cdd:PTZ00121 1783 EE 1784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1027-1610 |
2.46e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.74 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1027 KTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlKLAQestmdIENDKQQLDEKLKKKEfEISNLISKIEDEQAveiq 1106
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIE---LLEP-----IRELAERYAAARERLA-ELEYLRAALRLWFA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1107 lQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGAT---------SAQVELNKKRE--AEFQ 1175
Cdd:COG4913 287 -QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRleqlereieRLERELEERERrrARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1176 KLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNL------- 1248
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllal 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1249 -EKMCRSLEDQVSEL---------KTKEEEQQ----RLINDltaQRAHLQTEAGEYSRLLdekdALVSQLSRRKQASTQQ 1314
Cdd:COG4913 446 rDALAEALGLDEAELpfvgelievRPEEERWRgaieRVLGG---FALTLLVPPEHYAAAL----RWVNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1315 IEELKHQLEEETKAKNALAHALQSSRHD-GDLLREQYEEEQ-----EGKAELQRA--------LSKANSEVAQ------W 1374
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLDFKPHPfRAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1375 RTKYET--DAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMLDVERSNAACAALDKKQR 1450
Cdd:COG4913 599 RSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1451 NFDK---VLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIH 1527
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1528 ELEKIKKQVEQekcEIQAALEEAEASLEHEEGKILRIQLELNQV----KSEVDRKIAE-------------------KDE 1584
Cdd:COG4913 759 LGDAVERELRE---NLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESlpeylalldrleedglpeyEER 835
|
650 660
....*....|....*....|....*.
gi 1331883584 1585 EIDQLKRNHTRVVETMQSTLDAEIRS 1610
Cdd:COG4913 836 FKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
975-1592 |
3.06e-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: 85.07 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 975 ENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILtkaktklEQQVDDLEGSLEQEKKLRMDLERA 1054
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL-------EQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1055 KRKLEGDLKlaqestmdieNDKQQLDeklkKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSK 1134
Cdd:TIGR04523 105 LSKINSEIK----------NDKEQKN----KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1135 AEKQRSDLSRELEEISERLEEaggatsaqveLNKKREAEFQKLRrDLEEATLQHeamaaalrKKHADSMAELAEQIDNLQ 1214
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDK----------IKNKLLKLELLLS-NLKKKIQKN--------KSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1215 RVKQKLEKEKSELKMEIddlSSNAEVISKAKGNLEKMCRSLEDQVSELktkeEEQQRLINDLTAQrahLQTEAGEYSRLL 1294
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEI---SNTQTQLNQLKDEQNKIKKQLSEKQKEL----EQNNKKIKELEKQ---LNQLKSEISDLN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1295 DEKDA-LVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQ 1373
Cdd:TIGR04523 302 NQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1374 WRtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFD 1453
Cdd:TIGR04523 382 YK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1454 KVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIK 1533
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1534 KQVEQEKCEIQAALEEAEASLEHE--EGKILRIQLELNQVKSE---VDRKIAEKDEEIDQLKRN 1592
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEKE 597
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
868-1587 |
5.95e-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: 83.92 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 868 KSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLiKNKIQ-LEAKIKEVTERAEEEEEINAELTAKKRKL 946
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 947 EDECSELKKDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDK 1019
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1020 VNILTKAKTKLEQQVDDLEGSLEQEKKLR---MDLERAKRKLEGDLKLAQestmdieNDKQQLDEKLKKKEFEISNLISK 1096
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKSLEsqiSELKKQNNQLKDNIEKKQ-------QEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1097 IEDEQAveiQLQKKIKELQarieeleeeieaerasrsKAEKQRSDLSRELEEISERLEEAGgaTSAQVELNKKREAEFQK 1176
Cdd:TIGR04523 262 QNKIKK---QLSEKQKELE------------------QNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1177 LRRDLEEATLQheamaaalRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLE 1256
Cdd:TIGR04523 319 QEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1257 DQVSELKTKEEEQQRLINDLTAQRAHLQTeagEYSRLLDEKDALVSQLSRRKqastQQIEELKHQLEEETKAKNALAHAL 1336
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQ---EKELLEKEIERLKETIIKNN----SEIKDLTNQDSVKELIIKNLDNTR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1337 QSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCAS 1416
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK--------LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1417 LEKTKQRLQNEVEDLMLDVERSNaacaaLDKKQRNFDKVLSEWKQkyeeTQAELEASQKESrslstelfkvknayEESLD 1496
Cdd:TIGR04523 536 KESKISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIEELKQ----TQKSLKKKQEEK--------------QELID 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1497 QLETlrrENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQlelnQVKSEVD 1576
Cdd:TIGR04523 593 QKEK---EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR----NKWPEII 665
|
730
....*....|.
gi 1331883584 1577 RKIAEKDEEID 1587
Cdd:TIGR04523 666 KKIKESKTKID 676
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1146-1806 |
6.28e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.94 E-value: 6.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1146 LEEISERleeAGGATSAQVELNKKREAEFQKLRRDLE--EATLQHEAMAAaLRKKhadsMAELAEQIDNLQRVKQKLEKE 1223
Cdd:PRK02224 164 LEEYRER---ASDARLGVERVLSDQRGSLDQLKAQIEekEEKDLHERLNG-LESE----LAELDEEIERYEEQREQARET 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1224 KSELKMEIDDLSSNAEVISKAKGNLEKmcrsLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQ 1303
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1304 LSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE---- 1379
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEelee 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1380 --TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQN---EVEDLM---------LDVERSNAACAal 1445
Cdd:PRK02224 392 eiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveEAEALLeagkcpecgQPVEGSPHVET-- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1446 dkkqrnfdkvLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAyEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ 1525
Cdd:PRK02224 470 ----------IEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1526 IHELEKIKKQVEQEkceiqAALEEAEASLEHEEGKILRIQLelnqvkSEVDRKIAEKDEEIDQLKRnhtrvVETMQSTLd 1605
Cdd:PRK02224 539 AEELRERAAELEAE-----AEEKREAAAEAEEEAEEAREEV------AELNSKLAELKERIESLER-----IRTLLAAI- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1606 AEIRSRNDALRVKKKmegDLNEMEiqlnhanrlaaeslrnyrntqgilketqlhlddalqgqEDLKEQLAIVERRANLLQ 1685
Cdd:PRK02224 602 ADAEDEIERLREKRE---ALAELN--------------------------------------DERRERLAEKRERKRELE 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1686 AEIEELRATLEQTERSRkiAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLqteveeviqesrnaeekakkaitda 1765
Cdd:PRK02224 641 AEFDEARIEEAREDKER--AEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL------------------------- 693
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1331883584 1766 ammaEELKKEQDTsahlermkknLEQTVKDLQHRLDEAEQL 1806
Cdd:PRK02224 694 ----EELRERREA----------LENRVEALEALYDEAEEL 720
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
965-1515 |
8.60e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.55 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 965 AKVEKEKHATENKvknLTEEMAGLDEIIAKLSKEKKALQET----------HQQTLDDLQAEEDKVNILTKAKTKLEQQV 1034
Cdd:PRK02224 198 EKEEKDLHERLNG---LESELAELDEEIERYEEQREQARETrdeadevleeHEERREELETLEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1035 DDLEGSLEQEKKLRMDLERAKRKLEGDLKL--AQESTM-----DIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQL 1107
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLddADAEAVearreELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1108 QKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRRDLEEATLQ 1187
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA--------------PVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1188 HEamaaALRKKHADSMAELAEQIDNLQRVKQKLEKEK-SELKMEIDDlSSNAEVISKAKGNLEKmcrsLEDQVSELKTKE 1266
Cdd:PRK02224 421 RD----ELREREAELEATLRTARERVEEAEALLEAGKcPECGQPVEG-SPHVETIEEDRERVEE----LEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1267 EEQQRLINDLTAqrahLQTEAGEYSRLLDEKDALVSQLSRRKqastQQIEELKHQLEEETKAKNALAHALQSSRHDGDLL 1346
Cdd:PRK02224 492 EEVEERLERAED----LVEAEDRIERLEERREDLEELIAERR----ETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1347 REQYEEEQEGKAELQRALSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKcaslektK 1421
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLERIRTllaaiADAEDEIERLREKREALAELNDERRERLAEKRER-------K 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1422 QRLQNEVEDLMLDVERSNaacaaldkkqrnfdkvlsewKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETL 1501
Cdd:PRK02224 637 RELEAEFDEARIEEARED--------------------KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
570
....*....|....
gi 1331883584 1502 RRENKNLQQEISDL 1515
Cdd:PRK02224 697 RERREALENRVEAL 710
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1408-1937 |
3.86e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 81.76 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1408 EAVNAKCASLEKTKQRlQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELfkv 1487
Cdd:pfam01576 5 EEMQAKEEELQKVKER-QQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1488 KNAYEESLDQLETLRRENKNLQQEISDLTEQIA--EGGKQIHELEKIKKQVEQEKceiqaaLEEAEASLEHEEGKILRIQ 1565
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeEAARQKLQLEKVTTEAKIKK------LEEDILLLEDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1566 LELNQVKSEVDRKIAEKDEE---IDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAEs 1642
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAE- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1643 lrnyrnTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQ 1722
Cdd:pfam01576 234 ------LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1723 NTSLINT-------KKKLENDVSQLQTEVEEviqESRNAE----EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQ 1791
Cdd:pfam01576 308 LEDTLDTtaaqqelRSKREQEVTELKKALEE---ETRSHEaqlqEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1792 TVKDLQHRLDEAEQLALKGGKKQiQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLV 1871
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1872 DKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHE-------LEEAEERADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDErnslqeqLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
838-1330 |
5.85e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.83 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 838 KIKPLLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 918 LEAK---IKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVE---------------------KEKHA 973
Cdd:TIGR04523 199 LELLlsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 974 TENKVKNLTEEMAGLDEIIAKLSKEKKalQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLER 1053
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1054 AKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRS 1133
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1134 KAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQheamaaalrkkhadsMAELAEQIDNL 1213
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE---------------LKSKEKELKKL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1214 QRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQV---------SELKTKEEEQQRLINDLTAQRAHLQ 1284
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLK 581
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1331883584 1285 TEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLeEETKAKN 1330
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1080-1598 |
9.52e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1080 DEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGA 1159
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1160 TSAQVELNKKREAEFQKLrRDLEEATLQHEAMAAALRKKHAD--SMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSN 1237
Cdd:PRK03918 244 EKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1238 AEVI----------SKAKGNLEKMCRSLEDQVSELKTKEEEQQRlINDLTAQRAHLQTEAGEYSrlLDEKDALVSQLSRR 1307
Cdd:PRK03918 323 INGIeerikeleekEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLT--PEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1308 KQASTQQIEEL---KHQLEEETKAKNALAHALQSSR-------------HDGDLLREQYEEEQEGKAELQRA------LS 1365
Cdd:PRK03918 400 KEEIEEEISKItarIGELKKEIKELKKAIEELKKAKgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIeekerkLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1366 KANSEVAQWRTKYETDAIQRT--EELEEAKKKL----AQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSN 1439
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKElaEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1440 AACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNA---YEESLDQLETLRRENKNLQQEISDLT 1516
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAekeLEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1517 EQIAEGGKQIHELEKI-----KKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDrKIAEKDEEIDQLKR 1591
Cdd:PRK03918 640 KRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEK 718
|
....*..
gi 1331883584 1592 NHTRVVE 1598
Cdd:PRK03918 719 ALERVEE 725
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
864-1431 |
1.44e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 864 DELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLiknkiqleakikevteraeeeeeinaeltakk 943
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL-------------------------------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 944 rkledecSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKE---KKALQETHQQTLDDLQAEEDKV 1020
Cdd:PRK02224 254 -------ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1021 niltkaKTKLEQQVDDLEGSLEQEKKLRmdlERAKRkLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDe 1100
Cdd:PRK02224 327 ------RDRLEECRVAAQAHNEEAESLR---EDADD-LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1101 qaveiqLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGG--------------ATSAQVEL 1166
Cdd:PRK02224 396 ------LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1167 NKKREAEFQKLRRDLEEATLQHEAMAAALRKkhADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKG 1246
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1247 NLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEageysrlLDEKDALVSQLSRRKQAsTQQIEELKHQLEEET 1326
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-------IESLERIRTLLAAIADA-EDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1327 kAKNalahalqssrhdgDLLREQYEEEQEGKAELQRALSKANSEVAQWR----TKYETDAIQRTEELEEAKKKLAQRLQE 1402
Cdd:PRK02224 620 -ELN-------------DERRERLAEKRERKRELEAEFDEARIEEAREDkeraEEYLEQVEEKLDELREERDDLQAEIGA 685
|
570 580 590
....*....|....*....|....*....|....*
gi 1331883584 1403 AEEHVEAVNA---KCASLEKTKQRLQ---NEVEDL 1431
Cdd:PRK02224 686 VENELEELEElreRREALENRVEALEalyDEAEEL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1426 |
1.96e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 840 KPLLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQlqvqSEADSLADAEERCEQLIKNKIQLE 919
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 920 AKIKEvteraeeeeeinaeLTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEK 999
Cdd:PRK03918 259 EKIRE--------------LEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1000 KALQEthqqTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGS---LEQEKKLRMDLERAKRKLEG-DLKLAQESTMDIEND 1075
Cdd:PRK03918 324 NGIEE----RIKELEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1076 KQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEkqRSDLSRELEEISERLEE 1155
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE--LKRIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1156 AgGATSAQVELNKKREAEFQKLRRDLEeatlQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLs 1235
Cdd:PRK03918 478 L-RKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL- 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1236 snaEVISKAKGNLEKMCRSLEDQVSELKTK-EEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTqQ 1314
Cdd:PRK03918 552 ---EELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE-E 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1315 IEELKHQLEEETKAKNALAHALQssrhdgDLLREQYEEEQEGKAELQRALSKansEVAQWRTKYETdAIQRTEELEEAKK 1394
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELE------ELEKKYSEEEYEELREEYLELSR---ELAGLRAELEE-LEKRREEIKKTLE 697
|
570 580 590
....*....|....*....|....*....|..
gi 1331883584 1395 KLAQRLQEAEEHVEAVNakcaSLEKTKQRLQN 1426
Cdd:PRK03918 698 KLKEELEEREKAKKELE----KLEKALERVEE 725
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1207-1910 |
2.05e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.24 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1207 AEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQrahlqte 1286
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQ------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1287 ageysrllDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRhdgdlLREQYEEEQEGKAELQRALSK 1366
Cdd:TIGR00618 256 --------LKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA-----VTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1367 ANSEVAQWRtkyetdAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTK-------QRLQNEVEDLMLDVERSN 1439
Cdd:TIGR00618 323 RAKLLMKRA------AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1440 AACAALDKKQRNFDKVLSEwKQKYEETQAELEASQKESRsLSTELFKVKNAYEESLDQLETLR-RENKNLQQEISDLTEQ 1518
Cdd:TIGR00618 397 SLCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQE-LQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1519 IAEgGKQIHELEKIKKQVEQEKCEIQAALE-EAEASLEHEEGK-------------ILRIQLELNQVKSEVDRKIAEKDE 1584
Cdd:TIGR00618 475 LQT-KEQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1585 EIDQLKRNHTRVVETMQSTLDAEI---RSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLD 1661
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1662 DALQGQEDLKEQLAIVERRANLLQAEIEE-LRATLEQTERSRKIAEQELLDASERVQllhtqntSLINTKKKLENDVSQL 1740
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1741 QTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ---IQK 1817
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1818 LEARVRELEgEVENEQKRNAEAVKGLRKHERRVKELT-YQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANL 1896
Cdd:TIGR00618 787 IQFFNRLRE-EDTHLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
730
....*....|....
gi 1331883584 1897 SKFRKLQHELEEAE 1910
Cdd:TIGR00618 866 QEQAKIIQLSDKLN 879
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1072-1921 |
7.12e-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: 77.70 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1072 IENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEeieaeRASRSKAEKQRSDLSRELEEIS- 1150
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEEL-----KLQELKLKEQAKKALEYYQLKEk 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1151 ERLEEAGGATSAQVELNKKREAEFQKLRRDLEEAT--LQHEAMAAALRKKHADSMAELAEQIDNLQRVKQK-LEKEKSEL 1227
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIesSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEEL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1228 KMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRR 1307
Cdd:pfam02463 299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1308 KQASTQQIEELKHQLEEEtkaknaLAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTE 1387
Cdd:pfam02463 379 KKLESERLSSAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1388 ELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTkqrlQNEVEDLMLDVERSNAACAALDKKQRNF----DKVLSEWKQKY 1463
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQ----LELLLSRQKLEERSQKESKARSGLKVLLalikDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1464 EETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQihELEKIKKQVEQEKCEI 1543
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLP--LKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1544 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEG 1623
Cdd:pfam02463 607 QLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1624 DLNEMEIQLNHANRLAAESLRNyrntqgILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRK 1703
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQRE------KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1704 IAEQELLDASErvQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRnaEEKAKKAITDAAMMAEELKKEQDTSAHLE 1783
Cdd:pfam02463 761 EKEEEKSELSL--KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE--EELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1784 RMKKNLEQTVKDLQHRLDEAEQLALKGGKK-QIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRK 1862
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEeLLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1863 NVLRLQDLVDKLQAKVK-SYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVN 1921
Cdd:pfam02463 917 NEIEERIKEEAEILLKYeEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1387-1929 |
1.02e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.08 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1387 EELEEAKKKLAQRLQEAEE-HveavnakcaslEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNElH-----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1466 TQAELEASqkesRSLSTELFKVKNAyeeSLDQLETLRRENKNLQQEISDLTEQIAEG-GKQIHELEKIKK-QVEQEKCEI 1543
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEIRSILVDFEEAsGKKIYEHDSMSTmHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1544 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIaekdeeiDQLKRNHTRVVETMQSTLDAEIRSRNDAlrvkkkmeg 1623
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI-------ELLLQQHQDRIEQLISEHEVEITGLTEK--------- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1624 dlnemeiqlnhanrlaAESLRNYRNTqgilKETQLHLDdalqgQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRK 1703
Cdd:pfam15921 287 ----------------ASSARSQANS----IQSQLEII-----QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1704 IAEQELldaservqllhTQNTSLINTkkklenDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1783
Cdd:pfam15921 342 DKIEEL-----------EKQLVLANS------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1784 RMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKn 1863
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1864 vlRLQDLVDKLQAK---VKSYKR----------QAEEAEEQSNANLSKFR--------KLQHeLEEAEERADIAESQVNK 1922
Cdd:pfam15921 476 --MLRKVVEELTAKkmtLESSERtvsdltaslqEKERAIEATNAEITKLRsrvdlklqELQH-LKNEGDHLRNVQTECEA 552
|
....*..
gi 1331883584 1923 LRVKSRE 1929
Cdd:pfam15921 553 LKLQMAE 559
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1310-1888 |
1.09e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1310 ASTQQIEELKHQLEEEtkaknaLAHALQSSRHDGDLLREQYEEEQEGKAELQRaLSKANSEVAQWRtkyetdaiQRTEEL 1389
Cdd:PRK03918 186 KRTENIEELIKEKEKE------LEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEIEELE--------KELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1390 EEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLqNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAE 1469
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1470 L-EASQKESR-----SLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTeqiaegGKQIHELEKIKKQVEQEKCEI 1543
Cdd:PRK03918 330 IkELEEKEERleelkKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT------GLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1544 QAALEEAEASLEHEEGKILRIQLELNQVKSE------VDRKIAEKDEEidQLKRNHTRVVETMQSTLDAEIRSRNDALRV 1617
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1618 KKKMEGDLNEMEIQLnhANRLAAESLRNYRNTqgiLKETQLH-LDDALQGQEDLKEQLAIVERRANLLQAEIEELratlE 1696
Cdd:PRK03918 482 LRELEKVLKKESELI--KLKELAEQLKELEEK---LKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL----E 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1697 QTERSRKIAEQELLDASERvqllhtqntsLINTKKKLENDVSQLQTEVEEVIQESRNAEEK---AKKAITDAAMMAEELK 1773
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEE----------LAELLKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1774 KEQDTsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKEL 1853
Cdd:PRK03918 623 KLEEE---LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1331883584 1854 TYQTEEDRKNVLRLQDL------VDKLQAKVKSYKRQAEEA 1888
Cdd:PRK03918 700 KEELEEREKAKKELEKLekalerVEELREKVKKYKALLKER 740
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1228-1908 |
2.78e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.54 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1228 KMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLIND----LTAQRAHLQTEAGEYSRlldEKDALVSQ 1303
Cdd:pfam15921 56 KYEVELDSPRKIIAYPGKEHIERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQM---ERDAMADI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1304 LSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALskANSEVAQWRTKYETDAI 1383
Cdd:pfam15921 133 RRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1384 QRT-------------EELEEAKKKLAQRLQEAEEHVEAVNAKCAS-LEKTKQRLQNEVEDLMLDVErsnAACAALDKKQ 1449
Cdd:pfam15921 211 STMhfrslgsaiskilRELDTEISYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEHE---VEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1450 rnfdkvlSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNL-QQEISDLTEQIAEGGKQIHE 1528
Cdd:pfam15921 288 -------SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1529 LEKIKKQVEQEKCEIQAALEEAEASLEHEEGKIlriQLELNQVKSEVDRKIAEKDEeIDQLKR---NHTRVVETMQSTLD 1605
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLLADLHKREKEL---SLEKEQNKRLWDRDTGNSIT-IDHLRReldDRNMEVQRLEALLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1606 AeirsrndalrVKKKMEGDLNEMEIQLNHANrlaaESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERranllq 1685
Cdd:pfam15921 437 A----------MKSECQGQMERQMAAIQGKN----ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER------ 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1686 aEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENdvsqLQTEVEEV---IQESRNAEEKAKKAI 1762
Cdd:pfam15921 497 -TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRN----VQTECEALklqMAEKDKVIEILRQQI 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1763 TDaamMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLAlkggkkqiQKLEARVRELEGEVENEQKRNAEAVKG 1842
Cdd:pfam15921 572 EN---MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK--------DKKDAKIRELEARVSDLELEKVKLVNA 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1843 LRKHERRVKELTYQTE----EDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEE 1908
Cdd:pfam15921 641 GSERLRAVKDIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1387-1921 |
2.90e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1387 EELEEAKKKLaQRLQEAEEHVEAVNAKCASLEKTKQRLQ-NEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:COG4913 235 DDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1466 TQAELEASQKESRSLstelfkvKNAYEES-LDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQ 1544
Cdd:COG4913 314 LEARLDALREELDEL-------EAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1545 AALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRV---VETMQSTLDAEIRSRNDALRVKkkm 1621
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAELPFV--- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1622 eGDLneMEIQLNHAN-RLAAES-LRNYRNTqgILKETQlHLDDALqgqedlkeqlAIVERRAnllqaeieeLRATLeQTE 1699
Cdd:COG4913 464 -GEL--IEVRPEEERwRGAIERvLGGFALT--LLVPPE-HYAAAL----------RWVNRLH---------LRGRL-VYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1700 RSRKIAEQELLDASERVQLLHtqntslintkkKLENDVSQLQTEVEEVIQES------RNAEE--KAKKAITDAAMMaee 1771
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEElrRHPRAITRAGQV--- 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1772 lkkeqdtsahlermKKNLEQTVKDLQHRLDE--------AEQLALKggKKQIQKLEARVRELEGEVE---------NEQK 1834
Cdd:COG4913 584 --------------KGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLEaleaeldalQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1835 RNAEAVKGLRKHERRVKELTY---QTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEE 1911
Cdd:COG4913 648 EALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570
....*....|
gi 1331883584 1912 RADIAESQVN 1921
Cdd:COG4913 728 ELDELQDRLE 737
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
843-1518 |
4.01e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.21 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 843 LKSAETEKEmatmkedfqktkdelakseakRKELEEKMvtllkekNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKI 922
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 923 KEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKAL 1002
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1003 QETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegDLKLAQESTMDIEN--DKQQLD 1080
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKAISARYaeERDRAE 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1081 EKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLE----EA 1156
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEeledEL 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1157 GGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQidnlQRVKQKLEKEKSELKMEIDDLSS 1236
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE----RKQRAQAVAAKKKLELDLKELEA 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1237 NAEVISKAKGNLEKMCRSLEDQVSELktkeeeqQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLS-------RRKQ 1309
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDL-------QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQedlaaseRARR 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1310 ASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKY--ETDAIQRTE 1387
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSE 937
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1388 ----ELEEAKKKLAQRLQEAEEHVEA-VNAKCASLEKTKQRLQNEVEdlMLDVERSNAAcaaldKKQRNFDKVLSEWKQK 1462
Cdd:pfam01576 938 sarqQLERQNKELKAKLQEMEGTVKSkFKSSIAALEAKIAQLEEQLE--QESRERQAAN-----KLVRRTEKKLKEVLLQ 1010
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1463 YEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQ 1518
Cdd:pfam01576 1011 VEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
842-1539 |
4.81e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 842 LLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAK 921
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 922 IKEVTERAEEEEEINAeltaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDEIIAKLS--- 996
Cdd:TIGR00618 238 TQQSHAYLTQKREAQE----EQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQIEQQAQrih 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 997 ---KEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIE 1073
Cdd:TIGR00618 314 telQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1074 NDK--QQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISE 1151
Cdd:TIGR00618 394 KLQslCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1152 RLEEAGGATSAQVELNKKREA---EFQKLRRDLEEATLQHEAMAAALRKKHADS-------------------------- 1202
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLArllELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrgeqtyaqletseedvyhqlts 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1203 ----MAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTA 1278
Cdd:TIGR00618 554 erkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1279 QRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEetkaknALAHALQSSRHDGDLLREQYEEEQEGKA 1358
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ------LALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1359 ELQRALSKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRLQEAEEhvEAVNAKCASLEKTKQRLQNEVEDLMLDVERS 1438
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSS----LGSDLAAREDALNQSLKELMH--QARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1439 NAAcAALDKKQRNFDKVLSEWKQKYEETQAELEASQKEsRSLSTELFkvknayEESLDQLETLRRENKNLQQEISDLTEQ 1518
Cdd:TIGR00618 782 HLA-AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI-LNLQCETL------VQEEEQFLSRLEEKSATLGEITHQLLK 853
|
730 740
....*....|....*....|.
gi 1331883584 1519 IAEGGKQIHELEKIKKQVEQE 1539
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1144-1700 |
5.85e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1144 RELEEISERLEEAggatSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKE 1223
Cdd:COG4913 235 DDLERAHEALEDA----REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1224 KSELKMEIDDLssnaeviskakgnlEKMCRSLEDQVSELKTKEEEQqrlindLTAQRAHLQTEAGEYSRLLDEKDALVSQ 1303
Cdd:COG4913 311 LERLEARLDAL--------------REELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1304 LSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHD-GDLLREQYEEEQEGKAELqRALSKANSEVAQwrtkyetda 1382
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEI-ASLERRKSNIPA--------- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1383 iqrteELEEAKKKLAQRLQEAE-------EHVEaVNAKCAslektkqRLQNEVE--------DLMLDVERSNAACAALDK 1447
Cdd:COG4913 441 -----RLLALRDALAEALGLDEaelpfvgELIE-VRPEEE-------RWRGAIErvlggfalTLLVPPEHYAAALRWVNR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1448 ---KQR-NFDKVlsewkqkyEETQAELEASQKESRSLSTELFKVKNAYEESLDQL-------------ETLRRENK---- 1506
Cdd:COG4913 508 lhlRGRlVYERV--------RTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRaitr 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1507 ----------------------------------NLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEA 1552
Cdd:COG4913 580 agqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1553 SLEHEegkilriqlelnqvksEVDRKIAEKDEEIDQLKRNHTrVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQL 1632
Cdd:COG4913 660 EIDVA----------------SAEREIAELEAELERLDASSD-DLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1633 NHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRanlLQAEIEELRATLEQTER 1700
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN---LEERIDALRARLNRAEE 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
904-1537 |
6.09e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 904 AEERCEQLIKNKiqleakikevteraeeeeeiNAELTAKKRKLedecSELKKDIDDLELTLAKVEKEKhateNKVKNLTE 983
Cdd:PRK03918 187 RTENIEELIKEK--------------------EKELEEVLREI----NEISSELPELREELEKLEKEV----KELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 984 EMAGLDEIIAKLSKEKKALQEthqqtldDLQAEEDKVNILTKAKTKLEQQVDDLEgSLEQEKKLRMDLERAKrklegdlk 1063
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFY-------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1064 laqestmdiendkqqldEKLKKKEFEISNLISKIEDEQAVeiqLQKKIKELQARIEELEeeieaerasrsKAEKQRSDLS 1143
Cdd:PRK03918 303 -----------------EEYLDELREIEKRLSRLEEEING---IEERIKELEEKEERLE-----------ELKKKLKELE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1144 RELEEISERLEEAGGATSAQVELN--KKREA--EFQKLRRDLEEATLQHEamaaalrkkhadsmaELAEQIDNLQRVKQK 1219
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEELErlKKRLTglTPEKLEKELEELEKAKE---------------EIEEEISKITARIGE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1220 LEKEKSELKMEIDDLSS--------NAEVISKAKGNL-EKMCRSLEDQVSELKTKEEEQQRLINDLTaqraHLQTEAGEY 1290
Cdd:PRK03918 417 LKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLRKELR----ELEKVLKKE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1291 SRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEgKAELQRALSKANSE 1370
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK-LAELEKKLDELEEE 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1371 VAQWRTKYETDAIQRTEELEEakkklaqRLQEAE----EHVEAVNAkcaslEKTKQRLQNEVEDLMLDVERSNAACAALD 1446
Cdd:PRK03918 572 LAELLKELEELGFESVEELEE-------RLKELEpfynEYLELKDA-----EKELEREEKELKKLEEELDKAFEELAETE 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1447 KKQRNFDKVLSEWKQKYeetqaeleaSQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQI 1526
Cdd:PRK03918 640 KRLEELRKELEELEKKY---------SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
650
....*....|.
gi 1331883584 1527 HELEKIKKQVE 1537
Cdd:PRK03918 711 KELEKLEKALE 721
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1035-1629 |
6.80e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 73.99 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1035 DDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKEL 1114
Cdd:pfam05483 190 NNIEKMILAFEELRVQAENARLEMHFKLK---EDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1115 QARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEaggATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAA 1194
Cdd:pfam05483 267 RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR---SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1195 lRKKHADSMAELAEQIDNLQRV----KQKLEKEKSELK---MEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKT--- 1264
Cdd:pfam05483 344 -KAAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlld 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1265 KEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEEtKAKNalahaLQSSRHDGD 1344
Cdd:pfam05483 423 EKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE-KLKN-----IELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1345 LLREQYEEEQEGkAELQRALSKANSEVAQWRtKYETDAIQRTEELEEAKKKLAQRLQEAEEHV----EAVNAKCASLEKT 1420
Cdd:pfam05483 497 LLLENKELTQEA-SDMTLELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1421 KQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLsewkqkyEETQAELEASQKESRSLSTELfkvkNAYEESLDQLET 1500
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI-------EELHQENKALKKKGSAENKQL----NAYEIKVNKLEL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1501 LRRENKNLQQEISDLTEQIAEgGKQIHElEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIA 1580
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIE-DKKISE-EKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1581 EKDEEIDqLKRNHTRVVETMQSTLDAEIRS-RNDALRVKKKMEGDLNEME 1629
Cdd:pfam05483 722 ERDSELG-LYKNKEQEQSSAKAALEIELSNiKAELLSLKKQLEIEKEEKE 770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1292-1923 |
7.39e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1292 RLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDgdllREQYEEEQEGKAELQ------RALS 1365
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKReyegyeLLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1366 KANSEVAQWRTKYETDAIQRT-EELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQ-RLQNEVEDLMLDVERSNAACA 1443
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEElEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1444 ALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRE-------NKNLQQEISDLT 1516
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleevdkeFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1517 EQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILriqlELNQVKSEVDRKIAEKDEEIDQLKRnhtrv 1596
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN----ELEEEKEDKALEIKKQEWKLEQLAA----- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1597 vetMQSTLDAEIRSRNDALRvkkKMEGDLNEMEIQLNHANrlaaESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAI 1676
Cdd:TIGR02169 463 ---DLSKYEQELYDLKEEYD---RVEKELSKLQRELAEAE----AQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1677 VERR---------ANLLQA---EIEELRATLEQTERSRKIAEQELL------DASERVQLLHTQNT-----SLINTKKKL 1733
Cdd:TIGR02169 533 VGERyataievaaGNRLNNvvvEDDAVAKEAIELLKRRKAGRATFLplnkmrDERRDLSILSEDGVigfavDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1734 ENDVSQL--QTEVEEVIQESRN-----------------------AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1788
Cdd:TIGR02169 613 EPAFKYVfgDTLVVEDIEAARRlmgkyrmvtlegelfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1789 LEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQ 1868
Cdd:TIGR02169 693 LQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1869 DLVDKLQAKVKS-YKRQAEEAEEQSNANLSKFRKlqhELEEAEERADIAESQVNKL 1923
Cdd:TIGR02169 772 EDLHKLEEALNDlEARLSHSRIPEIQAELSKLEE---EVSRIEARLREIEQKLNRL 824
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
865-1662 |
1.03e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.93 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 865 ELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLadaeeRCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKR 944
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-----RARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 945 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQtlddLQAEEDKVNILT 1024
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ----LEGSSDRILELD 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1025 KAKTKLEQQVDDLEGSLEQEKKL---------RMDLERAKRKLEGDL------KLAQESTMDIENDKQQLDEKLKKKEF- 1088
Cdd:TIGR00606 478 QELRKAERELSKAEKNSLTETLKkevkslqneKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDKMDKDEQIRKIKSr 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1089 ---EISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVE 1165
Cdd:TIGR00606 558 hsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1166 lnkkrEAEFQKLRRDLEEATLQhEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKmeiddlssnaEVISKAK 1245
Cdd:TIGR00606 638 -----ESDLERLKEEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ----------EFISDLQ 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1246 GNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEE 1325
Cdd:TIGR00606 702 SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEE 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1326 TKAKNALAhalqssrhDGDLLREQYEEEQEGKAELQRALSKANSeVAQWRTKYETDaiQRTEELEEAKKKLAQRLQEAEE 1405
Cdd:TIGR00606 782 ESAKVCLT--------DVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVN--QEKQEKQHELDTVVSKIELNRK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1406 HVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELF 1485
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1486 KVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGgkqiheLEKIKKQVEQEKCEIQAALEEAEASLE---------- 1555
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG------KDDYLKQKETELNTVNAQLEECEKHQEkinedmrlmr 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1556 ------HEEGKILRIQLELNQVKS---EVDRKIAEKDEEIDQLKRNHTR-VVETMQSTLDAEIRSRNDALRVKKKMEGDL 1625
Cdd:TIGR00606 1005 qdidtqKIQERWLQDNLTLRKRENelkEVEEELKQHLKEMGQMQVLQMKqEHQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
810 820 830
....*....|....*....|....*....|....*..
gi 1331883584 1626 NEMEIQLNHANRLAAESlrNYRNTQGILKETQLHLDD 1662
Cdd:TIGR00606 1085 KHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKD 1119
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1040-1933 |
1.38e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.54 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1040 SLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEiSNLISKIEDEQAVEIQLQKKIKELqariE 1119
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHN----L 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1120 ELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREA-EFQKLRRDLEEATLQHEAMAAALRKK 1198
Cdd:TIGR00606 262 SKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1199 HAD-----SMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQ-------VSELKTKE 1266
Cdd:TIGR00606 342 KTEllveqGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1267 EEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLL 1346
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1347 REQYEeeQEGKAELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQEAE-EHVEAVNAKCA------SLEK 1419
Cdd:TIGR00606 502 EVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1420 TKQRLQNEVEDLMLDVERSNAACAALDKKQ---RNFDKVLSEWKQKYEETQAELEASQ-------------KESRSLSTE 1483
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQdeesdlerlkeeiEKSSKQRAM 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1484 LFKVKNAYEESLDQL-----------ETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKceiqaalEEAEA 1552
Cdd:TIGR00606 658 LAGATAVYSQFITQLtdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR-------DEMLG 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1553 SLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQL 1632
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1633 NHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEEL---RATLEQTERSRKIAEQEL 1709
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQL 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1710 LDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESrnaEEKAKKAITDAAMMAEELKK--------EQDTSAH 1781
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK---ETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDG 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1782 LERMKKNLEQTVKDLQHRLDEAEQlalkgGKKQIQKlEARVRELEGEVENEQKRNAEAVKGLRKHERRVKEL-----TYQ 1856
Cdd:TIGR00606 968 KDDYLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHL 1041
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1857 TEEDRKNVLRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1929
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
....
gi 1331883584 1930 VHTK 1933
Cdd:TIGR00606 1122 IYYK 1125
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
837-1269 |
2.01e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 837 FKIKPLLKSAETEKEMATMKEDFQKTKDELAKSEAKR---KELEEKMVTLLKEKNDLQLQVQSEADSLADAEE----RCE 909
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 910 QLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATEN-------K 977
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeytaE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 978 VKNLTEEMAGLDEIIAKLSKEKKALQE---------THQQTLDDLQAEEDKVNILTkaKTKLEQQVDDLEGSLEQEKKLR 1048
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1049 MDLERAKRKLegdlklaqESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEI-QLQKKIKELQARIEELEEEIEA 1127
Cdd:PRK03918 539 GEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELKDA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1128 ERASRSKaEKQRSDLSRELEEISERLEEaggaTSAQVELNKKREAEFQKLRRDLEEATLQHEAMaaALRKKHADSMAELA 1207
Cdd:PRK03918 611 EKELERE-EKELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELE 683
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1208 EQIDNLQRVKQKLEKEKSELKmEIDDLSSNAEVISKAKGNLEKmcrsLEDQVSELKTKEEEQ 1269
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEE----LREKVKKYKALLKER 740
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
847-1530 |
2.30e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.46 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 847 ETEKEMATMKEDFQKTKDELaksEAKRKELEEKMVTLLKEKNDLQLQVQSEAD----------SLADAEERCEQLIKNKI 916
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLLQQHQDRIEQLISEHEveitgltekaSSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 917 QLEAK------IKEVTERAEEEEEINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEmagL 988
Cdd:pfam15921 305 QEQARnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---L 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 989 DEIIAKLSKEKKALQETHQQT--------------------LDDLQAEEDKVNILTKA-----KTKLEQQVDDLEG---S 1040
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNkrlwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneS 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1041 LEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQ---QLDEKLKKKE--FEISNL-ISKIEDEQAVEIQLQKKIKEL 1114
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKEraIEATNAeITKLRSRVDLKLQELQHLKNE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1115 QARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAA 1194
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1195 LRKKHAD-SMAEL---------AEQIDNLQRVKQKLEKEKSELKM---EIDDLSSNAEVISKAKGN----LEKMCRSLED 1257
Cdd:pfam15921 620 IRELEARvSDLELekvklvnagSERLRAVKDIKQERDQLLNEVKTsrnELNSLSEDYEVLKRNFRNkseeMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1258 QVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEK----DALVSQLSRRKQASTQQIEElKHQLEEEtkaKNALA 1333
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqiDALQSKIQFLEEAMTNANKE-KHFLKEE---KNKLS 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1334 HAL-----QSSRHDGDL--LREQYEEEQEGKAELQRALSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQEAE-- 1404
Cdd:pfam15921 776 QELstvatEKNKMAGELevLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKElq 849
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1405 -------EHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAeLEASQKES 1477
Cdd:pfam15921 850 gpgytsnSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPT-VQLSKAED 928
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1478 RSLSTELFKVKNAYEESLDQLE----TLRRENKNLQQEISDLTEQIAEGGKQIHELE 1530
Cdd:pfam15921 929 KGRAPSLGALDDRVRDCIIESSlrsdICHSSSNSLQTEGSKSSETCSREPVLLHAGE 985
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
35-79 |
2.44e-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: 62.83 E-value: 2.44e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1331883584 35 DAKTSVFVAEPKESYVKSTIQSKEGGKITVKTEGGATLTVREDQV 79
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
943-1589 |
2.46e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.31 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 943 KRKLEDECSELKKDidDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQE--THQQTLDDLQAEEDKV 1020
Cdd:TIGR00618 195 KAELLTLRSQLLTL--CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEqlKKQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1021 N----ILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISK 1096
Cdd:TIGR00618 273 RaqeaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1097 IEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNK-----KRE 1171
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlahaKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1172 AEFQKLRRDLEEATLQHEAMAAALRKKHADSMAE-LAEQIDNLQRVKQKLEKEK-------------SELKMEIDDLSSN 1237
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQsLKEREQQLQTKEQIHLQETrkkavvlarllelQEEPCPLCGSCIH 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1238 AEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQA---STQQ 1314
Cdd:TIGR00618 513 PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1315 IEELKHQLEEETKAKNALAhalqssrhdgDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1394
Cdd:TIGR00618 593 TVRLQDLTEKLSEAEDMLA----------CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1395 KLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA-- 1472
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML----AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAre 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1473 -----SQKESRSLSTELFKVK-NAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAA 1546
Cdd:TIGR00618 739 dalnqSLKELMHQARTVLKARtEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1331883584 1547 LEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQL 1589
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL 861
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1668-1929 |
4.54e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1668 EDLKEQlAIVERRANLLQAEIEELRATLeqtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEV 1747
Cdd:COG1196 203 EPLERQ-AEKAERYRELKEELKELEAEL---------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1748 IQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELEG 1827
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE--------ELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1828 EVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELE 1907
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260
....*....|....*....|..
gi 1331883584 1908 EAEERADIAESQVNKLRVKSRE 1929
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEE 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1189-1598 |
5.46e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1189 EAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMcrsleDQVSELKTKEEE 1268
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----REELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1269 QQRLINDLTAQRAHLQTEAGEYSRLLDEKDALvSQLSRRKQASTQQIEELKHQLEEE-TKAKNALAHALQSSRHDGDLLR 1347
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEEL-RELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1348 EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQrtEELEEAK---------------------------------- 1393
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1394 -------KKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQkyEET 1466
Cdd:COG4717 284 gllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1467 QAELEASQKESRSLsteLFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKI--KKQVEQEKCEIQ 1544
Cdd:COG4717 362 ELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1545 AALEEAEASLEHEEGKILRIQLELNQVKSevDRKIAEKDEEIDQLKRNHTRVVE 1598
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAE 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
863-1519 |
1.26e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 863 KDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAK 942
Cdd:TIGR04523 88 NDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 943 KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNL---TEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQaeeDK 1019
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN---EK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1020 VNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKK-EFEISNLISKIE 1098
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1099 DEQAVEIQLQKKIKELQARIeeleeeieaerasrSKAEKQRSDLSRELEEISERLEEaggatsaQVELNKKREAEFQKLR 1178
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQI--------------SQLKKELTNSESENSEKQRELEE-------KQNEIEKLKKENQSYK 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1179 RDLEEATLQHEAMAAALRKKHADSmAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQ 1258
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLN-QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1259 VSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQS 1338
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1339 -----SRHDGDLLREQYEEEQEGK-------AELQRALSKANSEVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQEA 1403
Cdd:TIGR04523 543 ledelNKDDFELKKENLEKEIDEKnkeieelKQTQKSLKKKQEEKQELIDQKEKekkDLIKEIEEKEKKISSLEKELEKA 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1404 EEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKE---SRSL 1480
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKyitRMIR 702
|
650 660 670
....*....|....*....|....*....|....*....
gi 1331883584 1481 STELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQI 1519
Cdd:TIGR04523 703 IKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1773 |
2.07e-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: 69.69 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 850 KEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKnDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERA 929
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 930 EEEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETH--- 1006
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1007 --QQTLDDLQAEEDKVNILTKAKTKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLD 1080
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1081 EKLKKKEFEISNLISKIEDEQAV----EIQLQKKIKELQARIEELEEEIEAERASR------SKAEKQRSDLSRELEEIS 1150
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQELRkaerelSKAEKNSLTETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1151 ERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAA----LRKKHADSMAELAEQIDNLQRVKQKLEKEKSE 1226
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEqirkIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1227 LKMEIDDLS----------SNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRL------INDLTAQRAHLQTEAGEY 1290
Cdd:TIGR00606 586 INQTRDRLAklnkelasleQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLerlkeeIEKSSKQRAMLAGATAVY 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1291 SRLLDE---KDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKA 1367
Cdd:TIGR00606 666 SQFITQltdENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1368 NSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEaeehvEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALD- 1446
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-----EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDl 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1447 --------KKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKN---AYEESLDQLETLRRENKNLQQEISDL 1515
Cdd:TIGR00606 821 drtvqqvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1516 TEQIAEGGKQIHELEKIKKQVEQEKCEIqaaleeaeASLEHEEGKIlrIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTR 1595
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQEKEEL--------ISSKETSNKK--AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1596 VVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMeiqlnhanrlaaeslrnyrntqgilketQLHLDDALQGQEDLKEQLA 1675
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLM----------------------------RQDIDTQKIQERWLQDNLT 1022
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1676 IVERRANLlqAEIEELRATLEQTERSRKIAE--QELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEviQESRN 1753
Cdd:TIGR00606 1023 LRKRENEL--KEVEEELKQHLKEMGQMQVLQmkQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRD 1098
|
970 980
....*....|....*....|
gi 1331883584 1754 AEEKAKKAITDAAMMAEELK 1773
Cdd:TIGR00606 1099 AEEKYREMMIVMRTTELVNK 1118
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1102-1929 |
2.23e-11 |
|
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: 69.23 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1102 AVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDL 1181
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1182 EEATLQHeamaaalrkkhaDSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSE 1261
Cdd:pfam02463 223 EEYLLYL------------DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1262 LKTKEEEQQRlindltaQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRH 1341
Cdd:pfam02463 291 LAKEEEELKS-------ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1342 DGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTK 1421
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1422 QRLQNEVEDLMLDVERSNAACAALDKKQRNFDKvLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETL 1501
Cdd:pfam02463 444 GKLTEEKEELEKQELKLLKDELELKKSEDLLKE-TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1502 RRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEheegkILRIQLELNQVKSEVDRKIAE 1581
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLG-----ARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1582 KDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLD 1661
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1662 DALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQtersRKIAEQELLDASERVQLLHTQNTSLINTKKKLendvSQLQ 1741
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELK----KLKLEAEELLADRVQEAQDKINEELKLLKQKI----DEEE 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1742 TEVEEVIQESRNAEEKAKKAITDAAMMAEE------LKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQI 1815
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKEKELAEErektekLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1816 QKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKvksYKRQAEEAEEQSNAN 1895
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESK---EEKEKEEKKELEEES 906
|
810 820 830
....*....|....*....|....*....|....
gi 1331883584 1896 LSKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1929
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1492-1914 |
2.48e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1492 EESLDQLETL--RRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEheegkilriqlELN 1569
Cdd:PRK02224 186 RGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1570 QVKSEVDrKIAEKDEEIDQLKRNHTRVVETMQSTLDaEIRSRNDALRVKKKMEG----DLNEMEIQLNHANRLAAESLRN 1645
Cdd:PRK02224 255 TLEAEIE-DLRETIAETEREREELAEEVRDLRERLE-ELEEERDDLLAEAGLDDadaeAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1646 YRNTQGILKETqlhLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQ--- 1722
Cdd:PRK02224 333 CRVAAQAHNEE---AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDlgn 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1723 ----NTSLINTKKKLENDVSQLQT---EVEEVIQESRNAEEKAK-----KAITDAAMmAEELKKEQDTSAHLERMKKNLE 1790
Cdd:PRK02224 410 aedfLEELREERDELREREAELEAtlrTARERVEEAEALLEAGKcpecgQPVEGSPH-VETIEEDRERVEELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1791 QTVKDLQHRLDEAEQLAlkggkkqiqKLEARVRELEGEVENEQKRNAEavkglrKHERrvkeltyqTEEDRKNVLRLQDL 1870
Cdd:PRK02224 489 EEVEEVEERLERAEDLV---------EAEDRIERLEERREDLEELIAE------RRET--------IEEKRERAEELRER 545
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1331883584 1871 VDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1051-1591 |
2.72e-11 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 69.16 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1051 LERAKRKLEGDLKLAQESTMDIENdkqqLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERA 1130
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1131 S--------------RSKAEKQRSDLSRELEE---ISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAA 1193
Cdd:PRK01156 240 AlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1194 ALRKKHaDSMAELAE-QIDNLQRVKQKleKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRL 1272
Cdd:PRK01156 320 EINKYH-AIIKKLSVlQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1273 INDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEE 1352
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1353 EQEGKAE----LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ-------------RLQEAEEHVEAVNAKCA 1415
Cdd:PRK01156 477 KKSRLEEkireIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1416 SLEKTKQRLQNEvEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 1495
Cdd:PRK01156 557 SLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1496 DQLETLRRENKNLQQEISDLTEQIAEggkqihelekiKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKS-- 1573
Cdd:PRK01156 636 NEIQENKILIEKLRGKIDNYKKQIAE-----------IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESti 704
|
570 580
....*....|....*....|....*.
gi 1331883584 1574 --------EVDRKIAEKDEEIDQLKR 1591
Cdd:PRK01156 705 eilrtrinELSDRINDINETLESMKK 730
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1298-1937 |
2.93e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1298 DALVSQLSRRKQASTQQIEELKHQLEEETKAkNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQwrtK 1377
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKA-EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK---K 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1378 YETDAIQRTEELEEAKKKL--------AQRLQEAEEHVEAVNAKCASLEKTKQRLQN----EVEDLMLDVERSNAACAAL 1445
Cdd:PTZ00121 1106 TETGKAEEARKAEEAKKKAedarkaeeARKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1446 DKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTE--LFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGG 1523
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1524 KQIH---ELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETM 1600
Cdd:PTZ00121 1266 ARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1601 QSTLDAEIRSRNDALRVKKKMEGDLNEMEiqlnhANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAiVERR 1680
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKE-----EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA-AKKK 1419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1681 ANLLQAEIEELRatleQTERSRKIAEQEllDASERVQLLHTQNTSLINTKKKLENdvSQLQTEVEEVIQESRNAEEKAKK 1760
Cdd:PTZ00121 1420 ADEAKKKAEEKK----KADEAKKKAEEA--KKADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKK 1491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1761 A-----ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEaRVRELEGEVENEQKR 1835
Cdd:PTZ00121 1492 AeeakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAK 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1836 NAEAVKGLRkhERRVKELTYQTEEDRKNVLRLQDLVDKLQA----KVKSYKRQAEE---AEEQSNANLSKFRKLQHELEE 1908
Cdd:PTZ00121 1571 KAEEDKNMA--LRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670
....*....|....*....|....*....|
gi 1331883584 1909 AEE-RADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:PTZ00121 1649 AEElKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1175-1804 |
3.11e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1175 QKLRRDLEEAtlqHEAMAAALRK--------KHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIddlssNAEVISKAKG 1246
Cdd:COG4913 231 VEHFDDLERA---HEALEDAREQiellepirELAERYAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1247 NLEKmcrsLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEysRLLDEKDALVSQLSRRKQASTQ---QIEELKHQLE 1323
Cdd:COG4913 303 ELAR----LEAELERLEARLDALREELDELEAQIRGNGGDRLE--QLEREIERLERELEERERRRARleaLLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1324 EETKAKNALAHALQSSRHDGDLLREQYEEEQegkAELQRALSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQ 1398
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1399 RLQEAE-------EHVEaVNAKCAslektkqRLQNEVE--------DLMLDVERSNAACAALDK---KQR-NFDKVlsew 1459
Cdd:COG4913 452 ALGLDEaelpfvgELIE-VRPEEE-------RWRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV---- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1460 kqkyEETQAELEASQKESRSLSTELFKVKNAYEESLDQL-------------ETLRRENK-------------------- 1506
Cdd:COG4913 520 ----RTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRaitragqvkgngtrhekddr 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1507 ------------------NLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEgkilriqlel 1568
Cdd:COG4913 596 rrirsryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS---------- 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1569 nqvkseVDRKIAEKDEEIDQLKRNHtrvvetmqstldaeirsrndalrvkkkmeGDLNEMEIQLnhanrlaaeslrnyrn 1648
Cdd:COG4913 666 ------AEREIAELEAELERLDASS-----------------------------DDLAALEEQL---------------- 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1649 tqgilKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDasERVQLLHTQNtSLIN 1728
Cdd:COG4913 695 -----EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDA-VERE 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1729 TKKKLENDVSQLQTEVEEVIQESRNAEEKAKK--------------AITDAAMMAEELkKEQDTSAHLERMKKNLEQT-- 1792
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEYLALLDRL-EEDGLPEYEERFKELLNENsi 845
|
730
....*....|....
gi 1331883584 1793 --VKDLQHRLDEAE 1804
Cdd:COG4913 846 efVADLLSKLRRAI 859
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1447-1937 |
4.60e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1447 KKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAY---EESLDQLETLRRENKNLQQEISDLTEQIAEGG 1523
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1524 KQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEE--GKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETmq 1601
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL-- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1602 stldaeirsrndaLRVKKKMEGDLNEMEIQLNHANRLAA--ESLRNYRNTQGILKetqlhlddalqgQEDLKEQLAIVER 1679
Cdd:PRK03918 344 -------------KKKLKELEKRLEELEERHELYEEAKAkkEELERLKKRLTGLT------------PEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1680 RANLLQAEIEEL---RATLEQTERSRKIAEQELLDASERVQLLHTQNTSliNTKKKLENDVSQLQTEVEEVIQESRNAEE 1756
Cdd:PRK03918 399 AKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1757 KAKKAitdaammAEELKKEQDTSAHLERMKKNLEQtVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENeQKRN 1836
Cdd:PRK03918 477 KLRKE-------LRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1837 AEAVKGLRKHERRVKELTYQTEEDRKNVLR---------LQDLVDKLQAKVKSYKR--QAEEAEEQSNANLSKFRKLQHE 1905
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEE 627
|
490 500 510
....*....|....*....|....*....|..
gi 1331883584 1906 LEEAEERADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1490-1917 |
8.85e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1490 AYEESLDQLETLR-RENKNLQQEISDLTEQIAEGGKQ---IHELEKIKKQVEQEKCEIQAALEEAEASLEHEEgkILRIQ 1565
Cdd:COG4717 50 RLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLE--KLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1566 LELNQVKSEVDRKIAEKDEEIDQLKRnhtrvvetmqstldaEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRN 1645
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1646 YrntqgiLKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTS 1725
Cdd:COG4717 193 E------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1726 LINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNLEQTVKDLQHRLDEA 1803
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1804 EQLALKGGKKQIQKLEARVRELEGEVENEQKRN-----------AEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVD 1872
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEAgvedeeelraaLEQAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1331883584 1873 K--LQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAE 1917
Cdd:COG4717 427 EeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1094-1774 |
1.10e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1094 ISKIEDEQAVEIQLQKKIKELQARIeeleeeieaerasrskaEKQRSDLSRElEEISERLEEAGGATSAQVELNKKREAE 1173
Cdd:PRK03918 154 ILGLDDYENAYKNLGEVIKEIKRRI-----------------ERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1174 FQKLRRDLEEAtlqheamaaalrKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIddlssnaeviskakGNLEKMCR 1253
Cdd:PRK03918 216 LPELREELEKL------------EKEVKELEELKEEIEELEKELESLEGSKRKLEEKI--------------RELEERIE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1254 SLEDQVSELKTKEEEQQRlindltaqrahLQTEAGEYSRLLDEKDALVSQLSR---RKQASTQQIEELKHQLEEETKAKN 1330
Cdd:PRK03918 270 ELKKEIEELEEKVKELKE-----------LKEKAEEYIKLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEEKEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1331 ALahalqssrhdgdllreqyEEEQEGKAELQRALskanSEVAQWRTKYEtDAIQRTEELEEAKKKLaqrlqeAEEHVEAV 1410
Cdd:PRK03918 339 RL------------------EELKKKLKELEKRL----EELEERHELYE-EAKAKKEELERLKKRL------TGLTPEKL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1411 NAKCASLEKTKQRLQNEVEDLmldversNAACAALDKKQRNFDKVLSEWKQ---KYEETQAELEASQKES--RSLSTELF 1485
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKI-------TARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHRKEllEEYTAELK 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1486 KVKNAYEESLDQLETLRRENKNLQQEISDLTEQIA--EGGKQIHELEKIKKQVEQEKceiqaaLEEAEASLEHEEGKILR 1563
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNLEE------LEKKAEEYEKLKEKLIK 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1564 IQLELNQVKSEVDRKIAEKDEEIDQLKRNHTrvVETMQSTLDAEIRSRndALRVKKKMEGDLNEMEIQLNHANRLaaesl 1643
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDE--LEEELAELLKELEEL--GFESVEELEERLKELEPFYNEYLEL----- 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1644 rnyRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQN 1723
Cdd:PRK03918 608 ---KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAEL 682
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 1724 TSLINTKKKLENDVSQLQTEVEEvIQESRNAEEKAKKAITDAAMMAEELKK 1774
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEE-REKAKKELEKLEKALERVEELREKVKK 732
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1229-1702 |
1.11e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1229 MEIDDLSSNAEVISKAKGNLEKMC----RSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQL 1304
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNlkelKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1305 SRRKQAstQQIEELKHQLEEETKAKNALAHALQSSRHdgdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQ 1384
Cdd:COG4717 126 QLLPLY--QELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1385 RTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQ--NEVEDLMLDVERSNAACAALDKKQRNFDKVLS----- 1457
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1458 ----------EWKQKYEETQAELEASQKESRSLSTELfkvknAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIH 1527
Cdd:COG4717 280 flvlgllallFLLLAREKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1528 ELEKIKKQVEQEKC--EIQAALEEAEASLEHE---EGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRvvetmqS 1602
Cdd:COG4717 355 EAEELEEELQLEELeqEIAALLAEAGVEDEEElraALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE------E 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1603 TLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRnyrntqgilketqlhLDDALQGQEDLKEQLAIVERRAN 1682
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE---------------LAELLQELEELKAELRELAEEWA 493
|
490 500
....*....|....*....|
gi 1331883584 1683 LLQAEIEELRATLEQTERSR 1702
Cdd:COG4717 494 ALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1072-1540 |
1.43e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1072 IENDKQQLDEkLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEE--LEEEIEAERASRSKAEKQRSDLSRELEEI 1149
Cdd:COG4717 73 LKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1150 SERLEEaggaTSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKM 1229
Cdd:COG4717 152 EERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1230 EIDDLSSNAEVISKAKgnlekmcrsledqvselktKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDAL--------- 1300
Cdd:COG4717 228 ELEQLENELEAAALEE-------------------RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllal 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1301 -VSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1379
Cdd:COG4717 289 lFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1380 TDAIQrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcaaldkkqrnfdkvlsEW 1459
Cdd:COG4717 369 EQEIA--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE----------------EL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1460 KQKYEETQAELEASQKESRSLSTELFKVKNAYE--ESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVE 1537
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
...
gi 1331883584 1538 QEK 1540
Cdd:COG4717 511 EER 513
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1134-1817 |
1.93e-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: 66.40 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1134 KAEKQRSDLSRELEE---ISERLEEAGGATSAQVELN--KKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAE 1208
Cdd:pfam12128 215 KSRLNRQQVEHWIRDiqaIAGIMKIRPEFTKLQQEFNtlESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1209 QIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKG-----NLEKMCRSLEdQVSELKTKEEEQQRLINDLTAqrAHL 1283
Cdd:pfam12128 295 LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQE-QLPSWQSELENLEERLKALTG--KHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1284 QTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSsRHDGDLLreqyeEEQEGKAELQRA 1363
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELRE-QLEAGKL-----EFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1364 LSKAnsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLE----KTKQRLQNEVEDLMLDVERSN 1439
Cdd:pfam12128 446 LGEL---------KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQselrQARKRRDQASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1440 AACAALDKKQRNFD-------KVLSEWKQKYEETQAELEASQ------------KESRSLSTELFKVKNAYE-----ESL 1495
Cdd:pfam12128 517 ERQSALDELELQLFpqagtllHFLRKEAPDWEQSIGKVISPEllhrtdldpevwDGSVGGELNLYGVKLDLKridvpEWA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1496 DQLETLRRENKNLQQEISDLTEQIAEGGKQiheLEKIKKQVEqekcEIQAALEEAEASLEHEEGKILRIQLELNQVKSEV 1575
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQ---LVQANGELE----KASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1576 DRKIAEK-----------DEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVkkkMEGDLNEMEIQLNHAnrLAAESLR 1644
Cdd:pfam12128 670 NKALAERkdsanerlnslEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV---VEGALDAQLALLKAA--IAARRSG 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1645 NYRNTQGIlkETQLHLDDALQGqedlkeqlaIVERRANLLQAEIEELRATLEQTERSRKIAeqelldASERVQLLHT--- 1721
Cdd:pfam12128 745 AKAELKAL--ETWYKRDLASLG---------VDPDVIAKLKREIRTLERKIERIAVRRQEV------LRYFDWYQETwlq 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1722 QNTSLINTKKKLENDVSQLQTEVEEVIQES--RNAE-EKAKKAITDAAMMA-EELKKEQDTSAHLERMK--KNLEQTVKD 1795
Cdd:pfam12128 808 RRPRLATQLSNIERAISELQQQLARLIADTklRRAKlEMERKASEKQQVRLsENLRGLRCEMSKLATLKedANSEQAQGS 887
|
730 740
....*....|....*....|....
gi 1331883584 1796 LQHRLDEAEQLALK--GGKKQIQK 1817
Cdd:pfam12128 888 IGERLAQLEDLKLKrdYLSESVKK 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1099 |
3.40e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 842 LLKSAETEKEMATMKEDFQKT--------KDELAKSEAKRKELEEKMVTLLKEKNDL-----QLQVQSEADSLADAEERC 908
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSleqeienvKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEV 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 909 EQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 988
Cdd:TIGR02169 808 SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 989 DEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEG-------------SLEQEKKLRMDLERAK 1055
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelSLEDVQAELQRVEEEI 967
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1331883584 1056 RKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIED 1099
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1439 |
3.50e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 838 KIKPLLKSAETEKEMATMKEDFQKTKDElaksEAKRKELEEKMVTLLKEKNDlqlQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAE---EDKKKADELKKAAAAKKKADEAKKK 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 918 LEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAGLDEIIAKLSK 997
Cdd:PTZ00121 1427 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 998 EKKALQETHQQTLDDLQAEEDKvniltkaKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQEstMDIENDKQ 1077
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--LKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1078 QLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDlsrelEEISERleeag 1157
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKK----- 1634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1158 gatsaqVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADS--MAELAEQIDNLQRVKQKLEKEKSELKMEIDDLS 1235
Cdd:PTZ00121 1635 ------VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1236 SNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRlindltaqrahlqteAGEYSRLLDEKDALVSQLSRRKQASTQQI 1315
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK---------------KAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1316 EELKHQLEEETKAKNALAHALQSSRHDGDlLREQYEEEQEGkaelqralSKANSEVAQWRTKYETDAIQRTEELEEAKKK 1395
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVDKKIKD-IFDNFANIIEG--------GKEGNLVINDSKEMEDSAIKEVADSKNMQLE 1844
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1331883584 1396 LAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSN 1439
Cdd:PTZ00121 1845 EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD 1888
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1081-1756 |
5.41e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.74 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1081 EKLKKKEFEISNLISKIEDEQAVEIQLQKKIKelQARIEELEEEIEAERASRSKAEKQR---SDLSRELEEISERLEEAG 1157
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAEKIKKWK--VSIEAELKQKENKLQENRKIIEAQRkaiQELQFENEKVSLKLEEEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1158 GATSAQVELNKKREAEFQKLRRDLE---EATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEiddL 1234
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKETCArsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---L 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1235 SSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQ 1314
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1315 IEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEgkaELQRALSKANSEVAQWRTKyetdaiqrTEELEEAKK 1394
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQME---ELNKAKAAHSFVVTEFEAT--------TCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1395 KLAQRLQEAEEHVEAVN---AKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELE 1471
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITmelQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1472 ASQKESRSLSTELFKVKNAYEESLDQLETLRR---------------------ENKNLQQEISDLT-------EQIAEGG 1523
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTelekeklknieltahcdklllENKELTQEASDMTlelkkhqEDIINCK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1524 KQIHELEKIKKQVEQEKCEIQAALEEAEASL--EHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQ 1601
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1602 STLDAEIRSRNDALRVKKKMEG--------DLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQ 1673
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENkqlnayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1674 LAIVERRANL-LQAEIEELRATLEQTERS-RKIAEQE-----LLDASERVQ--LLHTQNTSLINTKKKLENDVSQLQTEV 1744
Cdd:pfam05483 687 AVKLQKEIDKrCQHKIAEMVALMEKHKHQyDKIIEERdselgLYKNKEQEQssAKAALEIELSNIKAELLSLKKQLEIEK 766
|
730
....*....|..
gi 1331883584 1745 EEVIQESRNAEE 1756
Cdd:pfam05483 767 EEKEKLKMEAKE 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1214-1891 |
5.74e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1214 QRVKQKLEKEKSELK---MEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQrahLQTEAGEY 1290
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD---LSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1291 SRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAhalqSSRHDGDLLREQYEEEQEGKAELQRALSKANSE 1370
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1371 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQR 1450
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1451 NFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD-----QLETLRRENKNLQQEISDLTEQIAEGGKQ 1525
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1526 IHELEKIKKQVEQEKCEIQAALEEAEASLEHE----EGKILRIQlELNQVKSEVDRKIaEKDEEIDQLKRNHTRVVETMQ 1601
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIK-NLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1602 STLDAEIRSRNDALRVKKKMEGDLNEMEIQLNhanrLAAESLRNYRntqgilketqlhlddalqgqEDLKEQLAIVERra 1681
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKE----LIIKNLDNTR--------------------ESLETQLKVLSR-- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1682 nllqaEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKa 1761
Cdd:TIGR04523 476 -----SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1762 itdaamMAEELKKEQdtsahLERMKKNLEQTVKDLQHrldeaeqlalkggkkQIQKLEARVRELEGEVENEQKRNAEAVK 1841
Cdd:TIGR04523 550 ------DDFELKKEN-----LEKEIDEKNKEIEELKQ---------------TQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1842 GLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQ 1891
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1378 |
7.17e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 844 KSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIK 923
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 924 EvteraeeeeeinaeltakkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQ 1003
Cdd:PRK02224 311 A---------------------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1004 ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDD----LEGSLEQEKKLRMDLERAKRK---LEGDLKLAQEstmDIENDK 1076
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREReaeLEATLRTARE---RVEEAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1077 QQLDE-----------------KLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQarieeleeeieaeraSRSKAEKQR 1139
Cdd:PRK02224 447 ALLEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE---------------DLVEAEDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1140 SDLSRELEEISERLEEAggatSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEqidnlqrvkqk 1219
Cdd:PRK02224 512 ERLEERREDLEELIAER----RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE----------- 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1220 LEKEKSELKMEIDDLSSNAEVISKAKgnlekmcrSLEDQVSELKTKEEEQQRLiNDLtaQRAHLQtEAGEYSRLLDEK-- 1297
Cdd:PRK02224 577 LNSKLAELKERIESLERIRTLLAAIA--------DAEDEIERLREKREALAEL-NDE--RRERLA-EKRERKRELEAEfd 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1298 DALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREqYEEEQEGKAELQRALSKANSEVAQWRTK 1377
Cdd:PRK02224 645 EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE-LRERREALENRVEALEALYDEAEELESM 723
|
.
gi 1331883584 1378 Y 1378
Cdd:PRK02224 724 Y 724
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1192-1920 |
8.10e-10 |
|
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: 64.20 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1192 AAALRKKHADSMAELAEQIDNLQRVKQKLEKEK---SELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDqVSELKTKEEE 1268
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSareSDLEQDYQAASDHLNLVQTALRQQEKIERYQED-LEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1269 QQRLINDLTAQRAHLQTEAGeysRLLDEKDALVSQLSRRKQA-STQQIEELKHQleeetKAKNALAHALQSSRHDgDLLR 1347
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLE---AAEEEVDSLKSQLADYQQAlDVQQTRAIQYQ-----QAVQALEKARALCGLP-DLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1348 EQYEEEQEG-KAELQRA----------LSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKKLAQ--RLQEAEEHVEA 1409
Cdd:COG3096 437 ENAEDYLAAfRAKEQQAteevleleqkLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQALAQRLQQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1410 VNAKCASLEKTKQRLQNevedlmldVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRslstelfkvkn 1489
Cdd:COG3096 517 LRAQLAELEQRLRQQQN--------AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAV----------- 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1490 ayeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHE-EGKILRIQLEl 1568
Cdd:COG3096 578 ------EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERErEATVERDELA- 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1569 nQVKSEVDRKIAE-------KDEEIDQLKrnhtrvvETMQSTLDAEIRSrndalrvkkkmegdlnemEIQLNHANRLAAE 1641
Cdd:COG3096 651 -ARKQALESQIERlsqpggaEDPRLLALA-------ERLGGVLLSEIYD------------------DVTLEDAPYFSAL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1642 --SLRN---YRNTQGILKetqlhlddALQGQEDLKEQLAIVERRANLLQA---EIEEL-RATLEQTE----RSRKIAEQE 1708
Cdd:COG3096 705 ygPARHaivVPDLSAVKE--------QLAGLEDCPEDLYLIEGDPDSFDDsvfDAEELeDAVVVKLSdrqwRYSRFPEVP 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1709 LLD--ASE-RVQLLHTQNTSLINTKKKLENDVSQLQTeveevIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 1785
Cdd:COG3096 777 LFGraAREkRLEELRAERDELAEQYAKASFDVQKLQR-----LHQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERE 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1786 KKNLEQTVKDLQHRLDeaeqlALKGGKKQIQKL------------EARVRELEGEVENEQkrnaEAVKGLRKHERRVKEL 1853
Cdd:COG3096 852 LAQHRAQEQQLRQQLD-----QLKEQLQLLNKLlpqanlladetlADRLEELREELDAAQ----EAQAFIQQHGKALAQL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1854 tyqteEDRKNVLR--------LQDLVDKLQAKVKSYKRQA---------------EEAEEQSNANLSKFRKLQHELEEAE 1910
Cdd:COG3096 923 -----EPLVAVLQsdpeqfeqLQADYLQAKEQQRRLKQQIfalsevvqrrphfsyEDAVGLLGENSDLNEKLRARLEQAE 997
|
810
....*....|
gi 1331883584 1911 ERADIAESQV 1920
Cdd:COG3096 998 EARREAREQL 1007
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
939-1536 |
1.20e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.77 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 939 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLS---KEKKALQETHQQTLDDLQA 1015
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1016 EEDKVNiltkaktkleqqvdDLEGSLEQEKKLRMDLERAKRklegdlklaqESTMDIENDKQQLDEKlkkkefeiSNLIS 1095
Cdd:PRK01156 268 ELEKNN--------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKNDIENK--------KQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1096 KIEDEQAVEIQLQKKIKELQARIEELEeeieaerasrsKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQ 1175
Cdd:PRK01156 316 NIDAEINKYHAIIKKLSVLQKDYNDYI-----------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1176 KLRR---DLEEATLQHEAMAAALRKKHAD---SMAELAEQIDNLQRVKQKLEKEKSELK--MEIDDLSSNAEVISKAKGN 1247
Cdd:PRK01156 385 NIERmsaFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSrnMEMLNGQSVCPVCGTTLGE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1248 --LEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTeageysrlldEKDALVSQLSRRKQASTQQIEELKHQLEEE 1325
Cdd:PRK01156 465 ekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK----------RKEYLESEEINKSINEYNKIESARADLEDI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1326 TKAKNALAHAlqssrHDG-DLLREQYEEEQEGKAELQR-ALSKANSEvaqwRTKYETDAIQ-RTEELEEAKKKLAQRLQE 1402
Cdd:PRK01156 535 KIKINELKDK-----HDKyEEIKNRYKSLKLEDLDSKRtSWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1403 AEEHVEAVNakcASLEKTKQRLQNEVEDL---MLDVERSNAACAALDKKQRNFDKVLSEwKQKYEETQAELEASQKESrs 1479
Cdd:PRK01156 606 IEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDI-- 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1480 lSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQV 1536
Cdd:PRK01156 680 -EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1234-1853 |
1.34e-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: 63.23 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1234 LSSNAEVISKAKGNL---EKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQA 1310
Cdd:pfam07111 61 LSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1311 STQQIEEL-KHQLEEETKAKNALAHALQSsrhdgdllREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEEL 1389
Cdd:pfam07111 141 ELEEIQRLhQEQLSSLTQAHEEALSSLTS--------KAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1390 EEAKKKLAQRLQE-------AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQK 1462
Cdd:pfam07111 213 LEAQVTLVESLRKyvgeqvpPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1463 YEETQAELEasqKESRSLstelfkVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIhelekikKQVEQEKCE 1542
Cdd:pfam07111 293 SDSLEPEFP---KKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQV-------TSQSQEQAI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1543 IQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKrnhtRVVETMQSTLDaeirsrndalrvkkKME 1622
Cdd:pfam07111 357 LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSSTQI--------------WLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1623 GDLNEME---IQLNHANRLAAESLRNYRNTQGILKE----TQLHLDD------ALQGQEDLKEQLAIVERRANLLQAEIe 1689
Cdd:pfam07111 419 TTMTRVEqavARIPSLSNRLSYAVRKVHTIKGLMARkvalAQLRQEScpppppAPPVDADLSLELEQLREERNRLDAEL- 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1690 ELRATLEQTERSRKIAEQElldaSERVQllhtqntsLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMA 1769
Cdd:pfam07111 498 QLSAHLIQQEVGRAREQGE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLR 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1770 EELKKEQDTSAH-----LERMKKNLEQTVKDLQHRLDEA--EQLALKGGKKQIQKLEARVRELEGEVE--NEQKRNAEAv 1840
Cdd:pfam07111 566 QELTQQQEIYGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHRATQEKERNQELRrlQDEARKEEG- 644
|
650
....*....|...
gi 1331883584 1841 kglRKHERRVKEL 1853
Cdd:pfam07111 645 ---QRLARRVQEL 654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
992-1427 |
1.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 992 IAKLSKEKKALQETHQQtlddLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEstmd 1071
Cdd:COG4717 73 LKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL---- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1072 iendKQQLdEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKEL-QARIEELEEEIEAERASRSKAEKQRSDLSRELEEIS 1150
Cdd:COG4717 145 ----PERL-EELEERLEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1151 ERLEEAGGATsAQVELNKKREAEFQKLRR--------------------------DLEEATLQHEAMAAALRKKHADSMA 1204
Cdd:COG4717 220 EELEELEEEL-EQLENELEAAALEERLKEarlllliaaallallglggsllslilTIAGVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1205 ELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELktKEEEQQRLINDLTAQRAHLQ 1284
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA--EELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1285 TEAGeysrlLDEKDALVSQL--SRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDL--LREQYEEEQEGKAEL 1360
Cdd:COG4717 377 AEAG-----VEDEEELRAALeqAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEEL 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1361 QRALSKANSEVAQWRTKyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNE 1427
Cdd:COG4717 452 REELAELEAELEQLEED------GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1106-1340 |
1.72e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1106 QLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRRDLEEAT 1185
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1186 LQheamAAALRKKHADSMAELAEQIDNLQRVKQKlekekSELKM-----EIDDLSSNAEVISKAKGNLEKMCRSLEDQVS 1260
Cdd:COG4942 90 KE----IAELRAELEAQKEELAELLRALYRLGRQ-----PPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1261 ELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSR 1340
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1274 |
1.96e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 838 KIKPLLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQ 917
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 918 LEAKIKEVTERAEEEEeinaeltakKRKLEdecsELKKDiddlELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSK 997
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEA---------KIKAE----ELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 998 EKKALQETHQQTLDDLQAEEDkvniltkaKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQ 1077
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEED--------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1078 QLDEKLKKKEFeisnliSKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEI---SERLE 1154
Cdd:PTZ00121 1738 EAEEDKKKAEE------AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFANII 1811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1155 EAGGATSAQVELNKKRE-------AEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSEL 1227
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEdsaikevADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1331883584 1228 KMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLIN 1274
Cdd:PTZ00121 1892 KIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
834-1507 |
1.99e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.14 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 834 KLFFKIKPLLKSAETEKEMATMKEDFQKTKDELAKSE--AKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAE------ 905
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 906 ERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 978
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 979 KNLTEEMAGLDEII------AKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLE 1052
Cdd:TIGR00606 615 ESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1053 RAKRKLEGDLKLAqestmdiENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASR 1132
Cdd:TIGR00606 695 EFISDLQSKLRLA-------PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1133 SKAEKQRSDLSRELEEISERLEEAGGATSAQVELnKKREAEFQKLRRDLEEATLqhEAMAAALRKKHADSMAEL---AEQ 1209
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdtvVSK 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1210 IDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEdqvselkTKEEEQQRLINDLTAQRAHLQTEAGE 1289
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV-------ELSTEVQSLIREIKDAKEQDSPLETF 917
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1290 YSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDgdlLREQYEEEQEGKA----ELQRALS 1365
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD---YLKQKETELNTVNaqleECEKHQE 994
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1366 KANSEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQEAEEhveavnAKCASLEKTKQRLQNEVEDLML 1433
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLIKR 1068
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1434 DVERSNAACAALDKKQRNFDKVLSEWK-QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKN 1507
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1668-1935 |
2.18e-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: 62.78 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1668 EDLKEQLAIVERRANLLQAEIEELRATLE--QTERSRKIAEQELLDASERVQLlhtqnTSLINTKKKLENDVSQLQTEVE 1745
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1746 EVIQEsrnaeekakkaITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQhRLDEAEQLALKGG----KKQIQKLEAR 1821
Cdd:TIGR02169 248 SLEEE-----------LEKLTEEISELEKR------LEEIEQLLEELNKKIK-DLGEEEQLRVKEKigelEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1822 VRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRK 1901
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270
....*....|....*....|....*....|....
gi 1331883584 1902 LQHELEEAEERADIAESQVNKLRVKSREVHTKVS 1935
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1506-1932 |
2.90e-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: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1506 KNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALE-EAEASLEHEEGKILRIQLELNQVK-SEVDRKIAEKD 1583
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1584 EEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKME---GDLNEMEIQLnHANRLAAESLRNYRNtqgilketqlhl 1660
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKLETLTNQNS------------ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1661 dDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQL 1740
Cdd:pfam10174 321 -DCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1741 QTEVEEVIQESRNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EQTVKDLQHRLDEAEQL--ALKG 1810
Cdd:pfam10174 400 QKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1811 GKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQakvksykrQAEEAEE 1890
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVR 551
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1331883584 1891 QSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1932
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
842-1309 |
3.00e-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: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 842 LLKSAETEKEMATMK-----EDFQKTKDELAKSEAKRKE-----LEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQL 911
Cdd:pfam10174 264 LLHTEDREEEIKQMEvykshSKFMKNKIDQLKQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 912 iknkiqlEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 991
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 992 IAKLSKEKKALQE------THQQTLDDLQAEEDKV-NILTKAKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKL 1064
Cdd:pfam10174 417 LAGLKERVKSLQTdssntdTALTTLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1065 AQESTMDIENDKQQLDEKLKKKEFEISNLiskiedeqavEIQLQKKIKELQARIEELEEEIEAERASRSKAEkqRSDLSR 1144
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSL----------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE--INDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1145 ELEEISERLEEAGGATSAQVE--LNKKREAEFQKLRRD-----LEEATLQH-----------EAMAAALRKKHADSMAEL 1206
Cdd:pfam10174 562 LLEQEVARYKEESGKAQAEVErlLGILREVENEKNDKDkkiaeLESLTLRQmkeqnkkvaniKHGQQEMKKKGAQLLEEA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1207 AEQIDNLQRVKQK---------LEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSE-LKTKEEEQQRLINDL 1276
Cdd:pfam10174 642 RRREDNLADNSQQlqleelmgaLEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEiLEMKQEALLAAISEK 721
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1331883584 1277 TAQRAHLQ-------TEAGEYSRLLDEKDALVSQLSRRKQ 1309
Cdd:pfam10174 722 DANIALLElssskkkKTQEEVMALKREKDRLVHQLKQQTQ 761
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
944-1567 |
3.01e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 944 RKLEDECSELKKDIDDLE-----LTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQEThqqtLDDLQAEED 1018
Cdd:COG4913 258 RELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE----LDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1019 KVNilTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKL-------EGDLKLAQESTMDIENDKQQLDEKLKKKEFEIS 1091
Cdd:COG4913 334 GNG--GDRLEQLEREIERLERELEERERRRARLEALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1092 NLISKIEDEQAveiQLQKKIKELqarieeleeeieaerasrskaEKQRSDLSRELEEISERLEEAGGATSAQV----EL- 1166
Cdd:COG4913 412 AALRDLRRELR---ELEAEIASL---------------------ERRKSNIPARLLALRDALAEALGLDEAELpfvgELi 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1167 -NKKREAEFQKlrrdleeatlqheAMAAALR---------KKHADSMAELAEQIDNLQRVK-QKLEKEKSELKMEIDDLS 1235
Cdd:COG4913 468 eVRPEEERWRG-------------AIERVLGgfaltllvpPEHYAAALRWVNRLHLRGRLVyERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1236 SNAEVI----SKAKGNLEKM---------CRSLED------------QVSELKTKEEEQQRlinDLTAQRAHLQTEAGey 1290
Cdd:COG4913 535 SLAGKLdfkpHPFRAWLEAElgrrfdyvcVDSPEElrrhpraitragQVKGNGTRHEKDDR---RRIRSRYVLGFDNR-- 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1291 sRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLlrEQYEEEQEGKAELQRALSKANSE 1370
Cdd:COG4913 610 -AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERLDASSDD 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1371 VaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAC-----AAL 1445
Cdd:COG4913 687 L---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALL 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1446 DKK--QRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNA------------------YEESLDQLET----- 1500
Cdd:COG4913 752 EERfaAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleslpeYLALLDRLEEdglpe 831
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1501 -----LRRENKNLQQEISDLTEQIAEggkqihELEKIKKQVEqekcEIQAALEEaeasLEHEEGKILRIQLE 1567
Cdd:COG4913 832 yeerfKELLNENSIEFVADLLSKLRR------AIREIKERID----PLNDSLKR----IPFGPGRYLRLEAR 889
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1509-1761 |
3.04e-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: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1509 QQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNqvksEVDRKIAEKDEEIDQ 1588
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1589 LKRNHTRVVETMQSTLDAEIRSrndalrvkkkmeGDLNEMEIQLNHANrlAAESLRNYRNTQGILKETQLHLddalqgqE 1668
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRL------------GRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQA-------E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1669 DLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVI 1748
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|...
gi 1331883584 1749 QESRNAEEKAKKA 1761
Cdd:COG4942 234 AEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
864-1325 |
4.02e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 864 DELAKSEAKRKELEEKmvtllkekndlQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKevterAEEEEEINAELTAKK 943
Cdd:COG4717 71 KELKELEEELKEAEEK-----------EEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 944 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEedkVNIL 1023
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR---LAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1024 TKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIendKQQLDEKLKKKEFEISNLISKIedEQAV 1103
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA---LLGLGGSLLSLILTIAGVLFLV--LGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1104 EIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELnKKREAEFQKLRRDLEE 1183
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1184 ATLQHEaMAAALRKKHADSMAELAEQIDNLQRvKQKLEKEKSELKMEIDDLSSNAEVISKA--KGNLEKMCRSLEDQVSE 1261
Cdd:COG4717 366 EELEQE-IAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1262 LKTKEEEQQRLINDLTAQRAHLQTEaGEYSRLLDEKDALVSQLSR------RKQASTQQIEELKHQLEEE 1325
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRElaeewaALKLALELLEEAREEYREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
949-1521 |
4.08e-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: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 949 ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKT 1028
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1029 KL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLiSKIEDEQAVE 1104
Cdd:pfam05483 328 QLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1105 IQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKreaEFQKLRRDLEEA 1184
Cdd:pfam05483 407 LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK---EVEDLKTELEKE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1185 TLQHeamaaalrkkhadsmAELAEQIDNLQRVKQKLEKEKSELKMEiddLSSNAEVISKAKGNLEKMCRSLEdqvselkT 1264
Cdd:pfam05483 484 KLKN---------------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKKQEERMLKQIE-------N 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1265 KEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGD 1344
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1345 LLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRL 1424
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1425 QNEVEDLMldversnaacAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRE 1504
Cdd:pfam05483 699 QHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEE 768
|
570
....*....|....*..
gi 1331883584 1505 NKNLQQEISDLTEQIAE 1521
Cdd:pfam05483 769 KEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1065-1281 |
4.29e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1065 AQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSR 1144
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1145 ELEEISERLEE-------AGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKhadsMAELAEQIDNLQRVK 1217
Cdd:COG4942 98 ELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1218 QKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRA 1281
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1007-1493 |
4.41e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1007 QQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESTMDIENDKQQLdEKLKKK 1086
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERL-EELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1087 EFEISNLISKIEDEQAVEIQLQKKIKEL-QARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAggatSAQVE 1165
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL----EEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1166 LNKKREAEFQKLRRDLEEATLqheAMAAALRKKHADSMAELAEQIDNLQRVkqklekekseLKMEIDDLSSNAEVISKAK 1245
Cdd:COG4717 231 QLENELEAAALEERLKEARLL---LLIAAALLALLGLGGSLLSLILTIAGV----------LFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1246 GNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSR-RKQASTQQIEELKHQLEE 1324
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1325 ETKAKN--ALAHALQssrhdgdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiqrteeleeakkkLAQRLQE 1402
Cdd:COG4717 378 EAGVEDeeELRAALE--------QAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-------------LEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1403 AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErsnaacaaldkkqrnfdkvLSEWKQKYEETQAELEASQKESRSLST 1482
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGE-------------------LAELLQELEELKAELRELAEEWAALKL 497
|
490
....*....|.
gi 1331883584 1483 ELFKVKNAYEE 1493
Cdd:COG4717 498 ALELLEEAREE 508
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1352-1912 |
4.48e-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: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1352 EEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK---------------------KLAQRLQEAEEHVEAV 1410
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieaqrkaiqelqfenekvslKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1411 NAK---CASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKES----RSLSTE 1483
Cdd:pfam05483 151 NATrhlCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDhekiQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1484 LFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIK----KQVEQEKCEIQAALEEAEASLEHEEG 1559
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQdenlKELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1560 KILRIQLELNQVKSEVDRKIAEKD---EEIDQLKRNHTRVV---ETMQSTLDAEIRSRNDALrvkKKMEGDLNEMEIQLN 1633
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEaqmEELNKAKAAHSFVVtefEATTCSLEELLRTEQQRL---EKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1634 HANRLAAESLRNYRNTQGILKEtqlhLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERsrkiaeqELLDAS 1713
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEE----LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK-------EIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1714 ERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTV 1793
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1794 KDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVkglrKHERRVKELTYQTEEDRKNVLRLQDLVDK 1873
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVL----KKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
570 580 590
....*....|....*....|....*....|....*....
gi 1331883584 1874 LQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEER 1912
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
858-1515 |
4.55e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.78 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 858 DFQKTKDELAKSEAK---RKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIknkIQLEAKIKEVTERAEEEEE 934
Cdd:pfam12128 235 GIMKIRPEFTKLQQEfntLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL---RTLDDQWKEKRDELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 935 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEMagldeiiaklSKEKKALQETHQQTLDDLQ 1014
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQ---LPSWQSELENL----------EERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1015 AEEDKVNiltkaktklEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlAQESTMDIENDKQQLDEKLKKKEFE--ISN 1092
Cdd:pfam12128 379 RRRSKIK---------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1093 LISKIEDEQAVEiqlqkkikELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEaggatsAQVELNKKrEA 1172
Cdd:pfam12128 449 LKLRLNQATATP--------ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ------ASEALRQA-SR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1173 EFQKLRRDLEEATLQHEAMA----AALRKKHADSMAELAEQID-----------------------------NLQRV--- 1216
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAgtllHFLRKEAPDWEQSIGKVISpellhrtdldpevwdgsvggelnlygvklDLKRIdvp 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1217 -----KQKLEKEKSELKMEIDDLSSNAEVISK----AKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAqrahlqtea 1287
Cdd:pfam12128 594 ewaasEEELRERLDKAEEALQSAREKQAAAEEqlvqANGELEKASREETFARTALKNARLDLRRLFDEKQS--------- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1288 geysrlldEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKA 1367
Cdd:pfam12128 665 --------EKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1368 NSEVAQWRTKYETDAIQrteelEEAKKKLAQRLQEaeehveavnakcaslEKTKQRLQNEVEDLMLDVERsnaaCAALDK 1447
Cdd:pfam12128 737 AIAARRSGAKAELKALE-----TWYKRDLASLGVD---------------PDVIAKLKREIRTLERKIER----IAVRRQ 792
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1448 KQRNFDKVLSE-WKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDL 1515
Cdd:pfam12128 793 EVLRYFDWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1359-1778 |
6.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1359 ELQRALSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQEAEEHVEAvnakcASLEKTKQRLQNEVEDLMLDVE 1436
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1437 RSNAACAALDKKQRNfdkvLSEWKQKYEETQAEL-EASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDL 1515
Cdd:COG4717 150 ELEERLEELRELEEE----LEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1516 TEQIAEGGKQiHELEKIKKQVEQEK---------CEIQAALEEAEASLEHEEGK------ILRIQLELNQVKSEVDRKIA 1580
Cdd:COG4717 226 EEELEQLENE-LEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1581 EKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRlAAESLRNYRNTQGILKETQLHL 1660
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1661 DDALQGQEDLKEQLAIVERRANLLQAEIEELR---------ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKK 1731
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLgeleelleaLDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1331883584 1732 KLEND--VSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDT 1778
Cdd:COG4717 464 QLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
983-1867 |
7.68e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 983 EEMAGLDEIIAKLSKEK---KALQETHQQTLDDLQAEEDKvniLTKAKTKLEQQVDDLEGSL----------EQEKKLRM 1049
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELAE---LNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1050 DLERAKRKLEGDL---KLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQarieeleeeie 1126
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1127 aerasrsKAEKQRSDLSRELEEISERLEEAggATSAQVELNKKREAEfQKLRrDLEEATLQHEAMAAALRKKHADSMAEL 1206
Cdd:PRK04863 425 -------RAKQLCGLPDLTADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRKIAGEVSRSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1207 AeqidnlQRVKQKLEKEKSELKMEIDDLSSnaeviskakgnlekmcrsLEDQVSELKTKEEEQQRLINDLT--AQRAHLQ 1284
Cdd:PRK04863 494 A------WDVARELLRRLREQRHLAEQLQQ------------------LRMRLSELEQRLRQQQRAERLLAefCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1285 -TEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALA------HALQSSRhdgDLLREQYEEEQEGK 1357
Cdd:PRK04863 550 lDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawLAAQDAL---ARLREQSGEEFEDS 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1358 ----------AELQRALSKANSEVAqwrtkyetdaiQRTEELEEAKKKLAQ-------RLQEAEEHVEAV---------- 1410
Cdd:PRK04863 627 qdvteymqqlLERERELTVERDELA-----------ARKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvs 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1411 ------------NAKCA----SLEKTKQRLQNEvEDLMLDVERSNAACAALDkkqrnfDKVLSEWKQKYEETQAELEASQ 1474
Cdd:PRK04863 696 ledapyfsalygPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFD------DSVFSVEELEKAVVVKIADRQW 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1475 KESRSLSTELFKvKNAYEESLDQletlrrenknLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCE-IQAALE-EAEA 1552
Cdd:PRK04863 769 RYSRFPEVPLFG-RAAREKRIEQ----------LRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEaDPEA 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1553 SLEheegkilriqlELNQVKSEVDRKIAEKDEEIDQLkrnhtrvvetmqstldaeiRSRNDALRVKKKMegdLNEMeiqL 1632
Cdd:PRK04863 838 ELR-----------QLNRRRVELERALADHESQEQQQ-------------------RSQLEQAKEGLSA---LNRL---L 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1633 NHANRLAAESLrnyrntQGILKETQLHLDDALQGQEDLKEQ---LAIVERRANLLQA---EIEELRATLEQTERSRKIAE 1706
Cdd:PRK04863 882 PRLNLLADETL------ADRVEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAK 955
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1707 QELLDASERVQLLHtqNTSLINTKKKLEND---VSQLQTEVEEVIQESRNAEEKAKKA---ITDAAMMAEELKKEQDTsa 1780
Cdd:PRK04863 956 QQAFALTEVVQRRA--HFSYEDAAEMLAKNsdlNEKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA-- 1031
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1781 hLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQK-----------LEARVRELEGEVENEQKRnaeavkgLRKHERR 1849
Cdd:PRK04863 1032 -KRQMLQELKQELQDLGVPADSGAEERARARRDELHArlsanrsrrnqLEKQLTFCEAEMDNLTKK-------LRKLERD 1103
|
970 980
....*....|....*....|.
gi 1331883584 1850 VKELTYQTEEDRKN---VLRL 1867
Cdd:PRK04863 1104 YHEMREQVVNAKAGwcaVLRL 1124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
850-1258 |
7.95e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 850 KEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDL--QLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTE 927
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 928 RAEEEEEINAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLS 996
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 997 KEKKALQE-----------THQQTLDDLQAEEDKV---------------NILTKAKTKLEQQVDDLEGSLEQEKKLRMD 1050
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1051 LERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEfeisnliskiedEQAVEIQLQKKIKELQARIEELEEEIEAERA 1130
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE------------ELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1131 SRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKR--EAEFQKLRRDLEEATLQHEAMAAALrkkhadsmAELAE 1208
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEELREEL--------AELEA 460
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1209 QIDNLQRVK--QKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQ 1258
Cdd:COG4717 461 ELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1461-1930 |
8.01e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.62 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1461 QKYEETQ-AELEASQKE--SRSLSTELFKVKNAY--EESLDQLETLRRENknlqQEISdlTEQIAEGGKQIHELE----- 1530
Cdd:PRK04778 24 RKRNYKRiDELEERKQEleNLPVNDELEKVKKLNltGQSEEKFEEWRQKW----DEIV--TNSLPDIEEQLFEAEelndk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1531 -KIKKqveqekceIQAALEEAEASLEHEEGKILRIQLELNQ-VKSEvdrkiAEKDEEIDQLKRNHtrvvETMQSTLDAEI 1608
Cdd:PRK04778 98 fRFRK--------AKHEINEIESLLDLIEEDIEQILEELQElLESE-----EKNREEVEQLKDLY----RELRKSLLANR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1609 RSRNDALrvkKKMEGDLNEMEIQLNHANRLAAESlrNYRNTQGILKETQLHLDdalQGQEDLKEQLAIVERRANLLQAEI 1688
Cdd:PRK04778 161 FSFGPAL---DELEKQLENLEEEFSQFVELTESG--DYVEAREILDQLEEELA---ALEQIMEEIPELLKELQTELPDQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1689 EELRATLEQ-TERSRKIAEQELLdasERVQLLHTQNTSLINTKKKLE-NDVSQLQTEVEEVIQ---ESRNAEEKAKKait 1763
Cdd:PRK04778 233 QELKAGYRElVEEGYHLDHLDIE---KEIQDLKEQIDENLALLEELDlDEAEEKNEEIQERIDqlyDILEREVKARK--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1764 daammaeELKKEQDT-SAHLERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNA 1837
Cdd:PRK04778 307 -------YVEKNSDTlPDFLEHAKEQNKELKEEIDRvkqsyTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYS 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1838 EAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAE---EQSN------ANLSKFRKLQHELEE 1908
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKrylEKSNlpglpeDYLEMFFEVSDEIEA 459
|
490 500 510
....*....|....*....|....*....|....*.
gi 1331883584 1909 AEER--------------ADIAESQVNKLRVKSREV 1930
Cdd:PRK04778 460 LAEEleekpinmeavnrlLEEATEDVETLEEETEEL 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1663-1894 |
9.99e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1663 ALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLENDVSQLQT 1742
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-------LAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1743 EVEEVIQESRNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1816
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1817 KLEARVRELEGEVENEQKRNAEAVKglrKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNA 1894
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1156-1416 |
1.10e-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: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1156 AGGATSAQVELNKKREAEFQKLRRDLEEATlQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIddls 1235
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1236 snaeviskakgnlekmcRSLEDQVSELKTKEEEQQRLINDLTAQrAHLQTEAGEYSRLLDEKDALvsQLSRRKQASTQQI 1315
Cdd:COG4942 86 -----------------AELEKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1316 EELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKK 1395
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEE 224
|
250 260
....*....|....*....|.
gi 1331883584 1396 LAQRLQEAEEHVEAVNAKCAS 1416
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPA 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1347-1911 |
1.14e-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: 60.37 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1347 REQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQEAEEHVEAVNAKCASLEKTKQRLQN 1426
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1427 EVEDLMLDVERSNAACAALdkKQRNFDKVLSEWKQKYEETQAELeasQKESRSLSTELFKVKNAYEESLDQLETLRRENK 1506
Cdd:TIGR00618 275 QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTEL---QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1507 NLQQE--ISDLTEQ----IAEGGKQIHELEKIKKQVEQEKCEIQA--ALEEAEASLEHEEGKILRIQLELN--QVKSEVD 1576
Cdd:TIGR00618 350 LHSQEihIRDAHEVatsiREISCQQHTLTQHIHTLQQQKTTLTQKlqSLCKELDILQREQATIDTRTSAFRdlQGQLAHA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1577 RKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKET 1656
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1657 QLHLDDALQG---QEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKL 1733
Cdd:TIGR00618 510 CIHPNPARQDidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1734 ENDVSQLQTEVEEviqesrNAEEKAKKAitdAAMMAEELKKEQdtSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKK 1813
Cdd:TIGR00618 590 QNITVRLQDLTEK------LSEAEDMLA---CEQHALLRKLQP--EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1814 QIQKLEARVRELEGEVENEQKRNaeavkgLRKHERRVKELTYqteeDRKNVLRLQDLVDKLQAKVKSYKRQAEEaeeQSN 1893
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLA------LQKMQSEKEQLTY----WKEMLAQCQTLLRELETHIEEYDREFNE---IEN 725
|
570
....*....|....*...
gi 1331883584 1894 ANLSKFRKLQHELEEAEE 1911
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQ 743
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1461-1681 |
1.40e-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: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1461 QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEK 1540
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1541 CEIQAALEEAEASLeHEEGKILRIQLELNQVKSEvdrKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKK 1620
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 1621 MEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRA 1681
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1388-1830 |
1.91e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 59.32 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1388 ELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSE--------- 1458
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEEnfrletard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1459 -WKQKYEE----------TQAELEASQKESRSLSTELFKVKNA-------------YEESLDQLETLRRENKNLQQEISD 1514
Cdd:pfam05622 84 dYRIKCEElekevlelqhRNEELTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1515 LTEQIAEGGKQIHELEKIKKQVEQEKCEIQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEVDRKIAEKD---E 1584
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1585 EIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAaeSLRNYRNTQGILKETQLHLDDAL 1664
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKML--RLGQEGSYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1665 QGQEDLKEQLAIVERRANLLQAEIEELRATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLENDVSQLQTEV 1744
Cdd:pfam05622 318 RRKNELETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1745 EEVIQESRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLEQ---TVKDLQHRLDEAEQLALKGGKKQIQ 1816
Cdd:pfam05622 377 SELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLL 456
|
490
....*....|....
gi 1331883584 1817 KLEARVRELEGEVE 1830
Cdd:pfam05622 457 EKDKKIEHLERDFE 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
844-1212 |
2.16e-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: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 844 KSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTL--LKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAk 921
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 922 ikevteraeeeeeinaeltakkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEIIAKLSKEKKA 1001
Cdd:COG4913 690 ------------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---LDELQDRLEAAEDL 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1002 LQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQ-EKKLRMDLERAKRKLEGDLKLAQESTMDIEndkqqld 1080
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP------- 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1081 eklkkkefEISNLISKIEDEQAVEiqLQKKIKELQArieeleeeieaeraSRSKAEKQR--SDLSRELEEISERLEEA-- 1156
Cdd:COG4913 816 --------EYLALLDRLEEDGLPE--YEERFKELLN--------------ENSIEFVADllSKLRRAIREIKERIDPLnd 871
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1157 -------GGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDN 1212
Cdd:COG4913 872 slkripfGPGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 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 1331883584 1391 EAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAEL 1470
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1471 EASQKESRSLSTELFKVKNAYEESL----DQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQ-- 1544
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEal 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1545 -AALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVK 1618
Cdd:COG4942 180 lAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1273-1719 |
2.51e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1273 INDLTAQRAHLQTEAGEYSRLLDEKDalvsQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLR----- 1347
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1348 EQYEEEQEGKAELQRALSKANSEVAQWRTkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNE 1427
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1428 VEDLMLDVERSNAACAALDKKQRnfdkvLSEWKQKYEE--TQAELEASQKESRSLSTELFKVKNAYEESL-DQLETLRRE 1504
Cdd:COG4717 222 LEELEEELEQLENELEAAALEER-----LKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1505 NKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEheegkilriqlELNQVKSEVDRkiAEKDE 1584
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-----------ELQELLREAEE--LEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1585 EIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRnyrntqgilketQLHLDDAL 1664
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE------------ALDEEELE 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1665 QGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAE--QELLDASERVQLL 1719
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1316-1711 |
2.82e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1316 EELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEgkaELQRALSKANSEVAQwrtkYETDAIQRTEELEEAKKK 1395
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDRE---QWERQRRELESRVAE----LKEELRQSREKHEELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1396 LAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE---TQAELEA 1472
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1473 SQKESRSLSTELFKVKNAYEESLDQLETlrrenknLQQEISDLTEQIAEGGKQIHELEKIKKqveqekcEIQAALEEAEA 1552
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLE-------ELRSLQERLNA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1553 SLEHEEGkilrIQLELNQVKSEVDRKIAEkdeeidqLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQL 1632
Cdd:pfam07888 249 SERKVEG----LGEELSSMAAQRDRTQAE-------LHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1633 NHANRLAAESLRnyrntqgilkeTQLHLDDALQGQEDLKEQLAIvERRANLLQA-----EIEELRATLE--QTERSRKIA 1705
Cdd:pfam07888 318 DRIEKLSAELQR-----------LEERLQEERMEREKLEVELGR-EKDCNRVQLsesrrELQELKASLRvaQKEKEQLQA 385
|
....*..
gi 1331883584 1706 E-QELLD 1711
Cdd:pfam07888 386 EkQELLE 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1134 |
3.27e-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: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 900 SLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK 979
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 980 NLTEEMAGLDEIIAKLskeKKALQETHQQTL-------DDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLE 1052
Cdd:COG4942 94 ELRAELEAQKEELAEL---LRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1053 RAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASR 1132
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
..
gi 1331883584 1133 SK 1134
Cdd:COG4942 251 LK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1667-1900 |
3.67e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1667 QEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEV 1744
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1745 EEvIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNLEQTVKDLQHRLDEAEQLALKGGKKQ 1814
Cdd:COG3206 243 AA-LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1815 IQKLEARVRELEGEVENEQKRnaeaVKGLRKHERRVKELTYQTEEDRKNvlrLQDLVDKLQakvksykrqaeEAEEQSNA 1894
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE-----------EARLAEAL 383
|
....*.
gi 1331883584 1895 NLSKFR 1900
Cdd:COG3206 384 TVGNVR 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1456-1912 |
3.72e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1456 LSEWKQKYEETQAELEASQKESRSLSTELfkvknAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQ 1535
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1536 VEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDAL 1615
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1616 RVkkkmegDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATL 1695
Cdd:COG4717 252 LL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1696 EQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEndVSQLQTEVEEVIQESRNAEEKakkaitDAAMMAEELKKE 1775
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDEE------ELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1776 QDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERrvkelty 1855
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELEEELEELREELAELEAELEQLEE------- 467
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1856 qteedrknvlrlQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEER 1912
Cdd:COG4717 468 ------------DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1390-1591 |
5.75e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1390 EEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcaaLDKKQRNFDKVLSEWKQKYEETQAE 1469
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1470 LEASQKESRSLS--TELFKVKNaYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAAL 1547
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSES-FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1331883584 1548 EEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKR 1591
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1445-1935 |
7.61e-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: 57.72 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1445 LDKKQRNFDKVLSEWKQKYEETQAELEASQKESRS-------LSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTE 1517
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNdkeqknkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1518 QIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQ-------------LELNQVKSEVDRKIAEKDE 1584
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiqknkslesqiSELKKQNNQLKDNIEKKQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1585 EIDQ----LKRNHTRVVETMQS------TLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNY-----RNT 1649
Cdd:TIGR04523 240 EINEktteISNTQTQLNQLKDEqnkikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1650 QGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1729
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1730 KKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD-------- 1801
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsink 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1802 -----EAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQ- 1875
Cdd:TIGR04523 480 ikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENl 559
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1876 AKVKSYKRQAEEAEEQSNANLSKfrklqhELEEAEERADIAESQVNKLRVKSREVHTKVS 1935
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
846-1303 |
7.70e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 846 AETEKEMATMKEDFQKTK--------------DELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQL 911
Cdd:PRK02224 268 AETEREREELAEEVRDLRerleeleeerddllAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 912 IKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 991
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 992 IAKLSKEKKALQET------------------------HQQTLDDlqaEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKL 1047
Cdd:PRK02224 428 EAELEATLRTARERveeaealleagkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1048 -----RMDLERAKRKLEGDLKLAQESTmdIENDKQQLDEKLKKKEfeisNLISKIEDEQAVEIQLQKKIKELQARIEELE 1122
Cdd:PRK02224 505 veaedRIERLEERREDLEELIAERRET--IEEKRERAEELRERAA----ELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1123 EEIEAERASRSKAEKQRSDLSrELEEISERLEEAGGATSAQVELNKKREAEFQKLR---RDLEEATLQHEAMAAALRKKH 1199
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRerkRELEAEFDEARIEEAREDKER 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1200 ADS-MAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSnaeviskakgnLEKMCRSLEDQVSELKTKEEEQQRLINDLTA 1278
Cdd:PRK02224 658 AEEyLEQVEEKLDELREERDDLQAEIGAVENELEELEE-----------LRERREALENRVEALEALYDEAEELESMYGD 726
|
490 500
....*....|....*....|....*.
gi 1331883584 1279 QRAHL-QTEAGEYSRLLDEKDALVSQ 1303
Cdd:PRK02224 727 LRAELrQRNVETLERMLNETFDLVYQ 752
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
849-1838 |
8.44e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.75 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 849 EKEMATMKEDFQKTKDELAKSEAKRKELEEKMvtllkekNDlqlqvQSEADSLADAEERceqliKNKIQLEAKIKevter 928
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEIKNHY-------ND-----QINIDNIKDEDAK-----QNYDKSKEYIK----- 821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 929 aeeeeeinaELTAKKRKLEDECSELKKDIDDLeltLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEkkalqethqq 1008
Cdd:TIGR01612 822 ---------TISIKEDEIFKIINEMKFMKDDF---LNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAE---------- 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1009 tlddlqAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLerakRKLEGDLKLAQESTMDIE---NDKQQLDEKLKK 1085
Cdd:TIGR01612 880 ------ISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTL----KKVDEYIKICENTKESIEkfhNKQNILKEILNK 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1086 --KEFEISNLISKIEDEQaVEIQLQKKIKELQarieeleeeIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQ 1163
Cdd:TIGR01612 950 niDTIKESNLIEKSYKDK-FDNTLIDKINELD---------KAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYH 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1164 velnkkREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNL---------QRVKQKLE-------KEKSEL 1227
Cdd:TIGR01612 1020 ------QFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigkniellnKEILEEAEinitnfnEIKEKL 1093
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1228 KM-EIDDLSSNAEV-----ISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQ-----TEAGEYSRLLDE 1296
Cdd:TIGR01612 1094 KHyNFDDFGKEENIkyadeINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEdvadkAISNDDPEEIEK 1173
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1297 K-DALVSQLSRRKQAsTQQIEELKHQLEEETKAKNALAHA----LQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEV 1371
Cdd:TIGR01612 1174 KiENIVTKIDKKKNI-YDEIKKLLNEIAEIEKDKTSLEEVkginLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDL 1252
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1372 aqwrtkyetDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldvERSnaacaaLDKKQRN 1451
Cdd:TIGR01612 1253 ---------DEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR---EKS------LKIIEDF 1314
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1452 FDKvlSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYeesldqlETLRREN-KNLQQEISDLTEQIAEGGKQIH-EL 1529
Cdd:TIGR01612 1315 SEE--SDINDIKKELQKNLLDAQKHNSDINLYLNEIANIY-------NILKLNKiKKIIDEVKEYTKEIEENNKNIKdEL 1385
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1530 EKIKKQVEQEKCEIqaALEEAEASLEHE------EGKILRIQLELNQVKSEVdrkiAEKDEEIDQLKRNHTRVVETMQST 1603
Cdd:TIGR01612 1386 DKSEKLIKKIKDDI--NLEECKSKIESTlddkdiDECIKKIKELKNHILSEE----SNIDTYFKNADENNENVLLLFKNI 1459
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1604 LDAEIRSRNdALRVKKK-----MEGDLNEMEIQLNHANRLAAESLRNYRNTQG---ILKETQLHLDDALQ--GQEDLKEQ 1673
Cdd:TIGR01612 1460 EMADNKSQH-ILKIKKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFEQYKKDVTELLNkySALAIKNK 1538
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1674 LAIVERRANLLQAEIEELRA--TLEQTERSRKIAE--QELLDASERVQLLHTQNTSLINTKKKLEN------DVSQLQTE 1743
Cdd:TIGR01612 1539 FAKTKKDSEIIIKEIKDAHKkfILEAEKSEQKIKEikKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKK 1618
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1744 VEEVIQESRNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeqlalkggKKQIQKLEARVR 1823
Cdd:TIGR01612 1619 INDCLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIE 1684
|
1050
....*....|....*
gi 1331883584 1824 ELEGEVeNEQKRNAE 1838
Cdd:TIGR01612 1685 KIEIDV-DQHKKNYE 1698
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1484-1930 |
9.45e-08 |
|
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: 57.17 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1484 LFKVKNAYEEsLDQLETLRRE--NKNLQQEISDLtEQIAEGGKQIHELEKIKKQ----VEQEKCEIQAALEEAEASLEhe 1557
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1558 EGKILRIQLELNQVKS---EVDRKIAEKDEEIDQL----KRNHTRV--VETMQSTLDAEIRSRNDAL-RVKKKMEGDLNE 1627
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELleseEKNREEVeeLKDKYRELRKTLLANRFSYgPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1628 MEIQLNHANRLAAESlrNYRNTQGILKETQLHLDDAlqgQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQ 1707
Cdd:pfam06160 158 IEEEFSQFEELTESG--DYLEAREVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1708 elLDASERVQLLHTQNTSLINTKKKLE-NDVSQLQTEVEEVIQ---ESRNAEEKAKKaitdaammaeELKKEQDT-SAHL 1782
Cdd:pfam06160 233 --LNVDKEIQQLEEQLEENLALLENLElDEAEEALEEIEERIDqlyDLLEKEVDAKK----------YVEKNLPEiEDYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1783 ERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRN-------AEAVKGLRKHERRV 1850
Cdd:pfam06160 301 EHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYselqeelEEILEQLEEIEEEQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1851 KELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAE----------------EAEEQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:pfam06160 381 EEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADELNEVPLNMDEVNRLLD 460
|
490
....*....|....*.
gi 1331883584 1915 IAESQVNKLRVKSREV 1930
Cdd:pfam06160 461 EAQDDVDTLYEKTEEL 476
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
654-678 |
1.37e-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: 1.37e-07
10 20
....*....|....*....|....*
gi 1331883584 654 FRENLNKLMTNLRSTHPHFVRCIIP 678
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1034-1589 |
1.65e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1034 VDDLEGSLeqeKKLRMDLE--RAKRKLEGDLK-LAQEST-------MDIENDKQQLDEKLKKKEFEISNLISKIEDEQAV 1103
Cdd:PRK04863 232 FQDMEAAL---RENRMTLEaiRVTQSDRDLFKhLITESTnyvaadyMRHANERRVHLEEALELRRELYTSRRQLAAEQYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1104 EIQLQKKIKELqarieeleeeieaerasrskaEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREaefqklrrDLEE 1183
Cdd:PRK04863 309 LVEMARELAEL---------------------NEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA--------DLEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1184 ATLQHEAMAAALrkkhadsmAELAEQIDNLQRVKQKLEKEKSELKMEIDDLssnaeviskakgnlekmcrsledqvselk 1263
Cdd:PRK04863 360 LEERLEEQNEVV--------EEADEQQEENEARAEAAEEEVDELKSQLADY----------------------------- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1264 tkeeeQQRLIndltaqraHLQTEAGEYS---RLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSr 1340
Cdd:PRK04863 403 -----QQALD--------VQQTRAIQYQqavQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1341 hdgDLLREQYEEeqegKAELQRALSKANSEVAQWRTkyetdAIQRTEELEEAKKkLAQRLQEAEEHveavnakcasLEKT 1420
Cdd:PRK04863 469 ---QAAHSQFEQ----AYQLVRKIAGEVSRSEAWDV-----ARELLRRLREQRH-LAEQLQQLRMR----------LSEL 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1421 KQRLQNevedlmldversnaacaaldkkQRNFDKVLSEWKQKY---EETQAELEASQKEsrsLSTELFKVKNAYEESLDQ 1497
Cdd:PRK04863 526 EQRLRQ----------------------QQRAERLLAEFCKRLgknLDDEDELEQLQEE---LEARLESLSESVSEARER 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1498 LETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEgkilriqlELNQVKSEVDR 1577
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERER--------ELTVERDELAA 652
|
570
....*....|..
gi 1331883584 1578 KIAEKDEEIDQL 1589
Cdd:PRK04863 653 RKQALDEEIERL 664
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1253-1473 |
1.70e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1253 RSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNAL 1332
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1333 AHALQssrhdgDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQ 1401
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1402 EAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEAS 1473
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
939-1163 |
1.78e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 939 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQ--AE 1016
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1017 EDKVNILTKAktkleQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISK 1096
Cdd:COG4942 119 QPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1097 IEDEQAVEIQLQKKIKELQARIEeleeeieaerasrsKAEKQRSDLSRELEEISERLEEAGGATSAQ 1163
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELA--------------ELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1088-1931 |
1.95e-07 |
|
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: 56.59 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1088 FEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAekqrsdLSRELEEISERleeaggatsaqvELN 1167
Cdd:TIGR00606 179 FSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQI------TSKEAQLESSR------------EIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1168 KKREAEFQKLRRDLEEAtlqheamaaalrKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDD-LSSNAEVISKAKG 1246
Cdd:TIGR00606 241 KSYENELDPLKNRLKEI------------EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYH 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1247 NLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLD--EKDALVSQLSRRKQASTQQIEELKHQLEE 1324
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSLATRLELDGFERGPFS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1325 ETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQrLQEAE 1404
Cdd:TIGR00606 389 ERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKE-LQQLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1405 EHVEAVNAKCASLEKTKQRL-----QNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEwKQKYEETQAELEASQKESRS 1479
Cdd:TIGR00606 468 GSSDRILELDQELRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ-LNHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1480 LSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEG 1559
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1560 KILRI-QLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRL 1638
Cdd:TIGR00606 627 KLFDVcGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1639 AAESLRNyrnTQGILKETQLHLDdalqgqedlkEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQL 1718
Cdd:TIGR00606 707 APDKLKS---TESELKKKEKRRD----------EMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1719 LHTQNTSLiNTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAitdaammaeelkkeqdTSAHLERMKKNLEQTVKDLQH 1798
Cdd:TIGR00606 774 LGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL----------------QGSDLDRTVQQVNQEKQEKQH 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1799 RLDEAEQlalkggkkqiqklearvrelegEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKV 1878
Cdd:TIGR00606 837 ELDTVVS----------------------KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1879 KSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERAD-------IAESQVNKLRVKSREVH 1931
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISsketsnkKAQDKVNDIKEKVKNIH 954
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1562-1912 |
2.29e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1562 LRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETmQSTLDAEIRSRND-------ALRVKKKME---GDLNEMEIQ 1631
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEA-ESDLEQDYQAASDhlnlvqtALRQQEKIEryqADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1632 LNHANRLAAESlrnyrntQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQaeieelratleqterSRKIAEQELLD 1711
Cdd:PRK04863 364 LEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ---------------TRAIQYQQAVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1712 ASERVQLLhTQNTSLinTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKNLEQ 1791
Cdd:PRK04863 422 ALERAKQL-CGLPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR--SEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1792 TVKDLQHRLDEAEQLAlkggkKQIQKLEARVRELEGEVENEQkrnaEAVKGLRKHERRVkELTYQTEEDrknvlrLQDLV 1871
Cdd:PRK04863 497 VARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRL-GKNLDDEDE------LEQLQ 560
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1331883584 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 |
2.47e-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: 55.67 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1660 LDDALQGQEDLKEQLAIVERrANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhTQNTSLINTKKKLENDVSQ 1739
Cdd:pfam07888 9 LEEESHGEEGGTDMLLVVPR-AELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1740 LQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqLALKGGKKQIQKLE 1819
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1820 ARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKsykrQAEEAEEQSNANLSKF 1899
Cdd:pfam07888 164 AQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT----TAHRKEAENEALLEEL 239
|
250
....*....|....
gi 1331883584 1900 RKLQHELEEAEERA 1913
Cdd:pfam07888 240 RSLQERLNASERKV 253
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
945-1612 |
2.83e-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: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 945 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLteemagLDEIIAKLSKEKKALQETHQQtlDDLQAEEDKV-NIL 1023
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENY------IDEIKAQINDLEDVADKAISN--DDPEEIEKKIeNIV 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1024 TK--AKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKlegDLKLAQE-STMDIEndkqQLDEKLKKKEFEISNLISKIEDE 1100
Cdd:TIGR01612 1180 TKidKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGI---NLSYGKNlGKLFLE----KIDEEKKKSEHMIKAMEAYIEDL 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1101 QAVEIQLQKKIKELqARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEaggatSAQVELNKKREAEFQKLRRD 1180
Cdd:TIGR01612 1253 DEIKEKSPEIENEM-GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1181 LEEATLQHEamaaalrkKHADSMAELAEQIDNLQRVKQ--KLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQ 1258
Cdd:TIGR01612 1327 LQKNLLDAQ--------KHNSDINLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDD 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1259 VS--ELKTKEEEQ------QRLINDLTAQRAHLQTEAGE---YSRLLDEKDALVSQLSRRKQASTQqieelKHQLEEETK 1327
Cdd:TIGR01612 1399 INleECKSKIESTlddkdiDECIKKIKELKNHILSEESNidtYFKNADENNENVLLLFKNIEMADN-----KSQHILKIK 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1328 AKNAlahalqSSRHDGDLlreqyeeeqegkAELQRALSKANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQEAEEHV 1407
Cdd:TIGR01612 1474 KDNA------TNDHDFNI------------NELKEHIDKSK--------GCKDEADKNAKAIEKNKELFEQYKKDVTELL 1527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1408 E-----AVNAKCASLEKTKQRLQNEVEDL----MLDVERSNAACAALDKKQRNFDKVLSewkqKYEETQAELEASQKESR 1478
Cdd:TIGR01612 1528 NkysalAIKNKFAKTKKDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIEDDAA----KNDKSNKAAIDIQLSLE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1479 SLSTELFKVKNAYEESLDQLetlrRENKNLQQEISDLT-----EQIAEGGKQIHELEKIKKQVEQEKCEIqaalEEAEAS 1553
Cdd:TIGR01612 1604 NFENKFLKISDIKKKINDCL----KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNI----EDKKKE 1675
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1554 LEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVET-MQSTLDAEIRSRN 1612
Cdd:TIGR01612 1676 LDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKElIEPTIENLISSFN 1735
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1165-1908 |
3.13e-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: 55.83 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1165 ELNKKREAEFQKLRrDLEEATLQ-HEAMAAALRKKHADSMAELAEQI-----DNLQRVKQKLEKEKSELKMEIDDLSSNA 1238
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIKKHIhgeinKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1239 EVISKAKGNLEKMCRSLEDQVSELKTKEEEqqrlindltAQRAHLQTEagEYSRLLDEKDALVSQLsrrkqastqqIEEL 1318
Cdd:TIGR01612 779 DELNKYKSKISEIKNHYNDQINIDNIKDED---------AKQNYDKSK--EYIKTISIKEDEIFKI----------INEM 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1319 KHQLEEETKAKNALAHALQSSrhdgdllREQYEEEQEGKAELqraLSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLA 1397
Cdd:TIGR01612 838 KFMKDDFLNKVDKFINFENNC-------KEKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1398 QR------LQEAEEHVEAVNAKCASLEK--TKQRLQNEVEDLMLDVERSNaacAALDKKQRN-FDKVLSEWKQKYEETQA 1468
Cdd:TIGR01612 908 EEyqnintLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTIKES---NLIEKSYKDkFDNTLIDKINELDKAFK 984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1469 ELEASQKESRslSTELFKVKNAYEESL---------DQLETLRRENKNLQQEISDLTEQIAEGGKQIH--------ELEK 1531
Cdd:TIGR01612 985 DASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIEK 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1532 -IKKQVEQEKCEIqaaLEEAEASLEHEEGkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrvVETMQSTLDAEIrs 1610
Cdd:TIGR01612 1063 eIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKIDHHI-- 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1611 rNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNyRNTQGILKETQlhlddalqgqedlkEQLAIVERRANLLQaEIEE 1690
Cdd:TIGR01612 1132 -KALEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIE--------------NIVTKIDKKKNIYD-EIKK 1194
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1691 LRATLEQTERsrkiaEQELLDASERVQLLHTQNTSLI------NTKKKLENDVSQLQTEVEEV--IQESRNAEEKAKKAI 1762
Cdd:TIGR01612 1195 LLNEIAEIEK-----DKTSLEEVKGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGIE 1269
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1763 TDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKG 1842
Cdd:TIGR01612 1270 MDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLY 1344
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1843 LRKherrvkeltyqtEEDRKNVLRLQDlVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEE 1908
Cdd:TIGR01612 1345 LNE------------IANIYNILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1161-1745 |
3.88e-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: 55.13 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1161 SAQVELNKKREAefqkLRRDLEEATLQHEAMAA---ALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSN 1237
Cdd:pfam05557 27 RARIELEKKASA----LKRQLDRESDRNQELQKrirLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1238 AEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLindltaqrahlqteageySRLLDEKDALVSQLSRRKQASTQQIEE 1317
Cdd:pfam05557 103 REVISCLKNELSELRRQIQRAELELQSTNSELEEL------------------QERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1318 LKhqlEEETKAKNaLAHALQSSRHDGDLLREQyEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRtEELEEAKKKLa 1397
Cdd:pfam05557 165 LA---EAEQRIKE-LEFEIQSQEQDSEIVKNS-KSELARIPELEKELERLREHNKHLNENIENKLLLK-EEVEDLKRKL- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1398 qrlqeaeEHVEAVNAKCASLEKTKQRLQNEvedlmldversnaacaaldkkqrnfdkvLSEWKQKYEETQAELEASQKES 1477
Cdd:pfam05557 238 -------EREEKYREEAATLELEKEKLEQE----------------------------LQSWVKLAQDTGLNLRSPEDLS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1478 RslstelfkvknayeesldQLETLRRENKNLQQEISDLTEqiaeggkQIHELEKIKKQVEQEKCEIQAALEEAEASLEHE 1557
Cdd:pfam05557 283 R------------------RIEQLQQREIVLKEENSSLTS-------SARQLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1558 EGKILRIQlelnqvksevdRKIAEKDEEIDQLKRNhtrvVETMQSTLDAEIRSRNDALRVK------KKMEGDLNEMEIQ 1631
Cdd:pfam05557 338 KALVRRLQ-----------RRVLLLTKERDGYRAI----LESYDKELTMSNYSPQLLERIEeaedmtQKMQAHNEEMEAQ 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1632 LNHANRlaaeslrnyrnTQGILKETQLHLD---DALQGQEDLKEQLAIVERRANLLQaEIEELRATLEQTERSRKIAEQE 1708
Cdd:pfam05557 403 LSVAEE-----------ELGGYKQQAQTLErelQALRQQESLADPSYSKEEVDSLRR-KLETLELERQRLREQKNELEME 470
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1331883584 1709 LLDAS-------ERVQLLHTQNTSLINTKKKLENDVSQLQTEVE 1745
Cdd:pfam05557 471 LERRClqgdydpKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIE 514
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1080-1331 |
5.79e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1080 DEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIeeleeeieaerasrSKAEKQRSDLSRELEEISERLEEAgga 1159
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY--------------NELQAELEALQAEIDKLQAEIAEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1160 tsaQVELNKKREaEFQKLRRDLEEATLQHEAMAAALrkkHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAE 1239
Cdd:COG3883 78 ---EAEIEERRE-ELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1240 VISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELK 1319
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|..
gi 1331883584 1320 HQLEEETKAKNA 1331
Cdd:COG3883 231 AAAAAAAAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
972-1202 |
6.43e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 972 HATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSL----EQEKKL 1047
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1048 RMDLERAKRKLEGDLKLAQEStmdieNDKQQLDEKLKKKEFE----ISNLISKIEDEQAVEI-QLQKKIKELQARIEELE 1122
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrRLQYLKYLAPARREQAeELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1123 EEIEAERASRSKAEKQRSDLSRELEEISERLEEAggatSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADS 1202
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1453-1620 |
6.53e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1453 DKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGG--------- 1523
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1524 KQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNhtrvVETMQST 1603
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAK 171
|
170
....*....|....*..
gi 1331883584 1604 LDAEIRSRNDALRVKKK 1620
Cdd:COG1579 172 IPPELLALYERIRKRKN 188
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1387-1852 |
7.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1387 EELEEAKKKLAQRLQEAEEHVEAVNAKcASLEKTKQRLQNEVEDLMLDVERSNAACAALD--KKQRNFDKVLSEWKQKYE 1464
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1465 EtqaeLEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKN-LQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEI 1543
Cdd:COG4717 150 E----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLaTEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1544 QAALEEAEASLEHEEgkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEG 1623
Cdd:COG4717 226 EEELEQLENELEAAA---LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1624 DLNEmeiqlnhANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRK 1703
Cdd:COG4717 303 EAEE-------LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1704 IAEQELLDASERVQLLHtqntsLINTKKKLENDVSQLQTEVEEviqesRNAEEKAKKAITDAAMMAEELkkeQDTSAHLE 1783
Cdd:COG4717 376 LAEAGVEDEEELRAALE-----QAEEYQELKEELEELEEQLEE-----LLGELEELLEALDEEELEEEL---EELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1784 RMKKNLEQtvkdLQHRLDEAE-QLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKG---LRKHERRVKE 1852
Cdd:COG4717 443 ELEEELEE----LREELAELEaELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAlelLEEAREEYRE 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1102 |
7.33e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 7.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 864 DELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKevteraeeeeeinaELTAKK 943
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA--------------ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 944 RKLEDECSELKKDIDDLELTLAKVEKE--KHATENKVKNLT-----EEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAe 1016
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1017 edkvniltkAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlKLAQESTMDIENDKQQLDEkLKKKEFEISNLISK 1096
Cdd:COG4942 165 ---------LRAELEAERAELEALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAE-LQQEAEELEALIAR 231
|
....*.
gi 1331883584 1097 IEDEQA 1102
Cdd:COG4942 232 LEAEAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1453-1642 |
8.88e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1453 DKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ------- 1525
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1526 -----------------------IHELEKIKKQVEQEKCEI------QAALEEAEASLEHEEGKILRIQLELNQVKSEVD 1576
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1577 RKIAEKDEEIDQLKRNHTRVVETMQStLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAES 1642
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1244-1887 |
8.99e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.42 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1244 AKGNLEKmcrsLEDQVSELKTKEEEQQRLIND------------LTAQRAHLQteageYSRLLDEKDALVSQLSRRKQAS 1311
Cdd:PRK10246 196 ARTELEK----LQAQASGVALLTPEQVQSLTAslqvltdeekqlLTAQQQQQQ-----SLNWLTRLDELQQEASRRQQAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1312 TQQIEELkhqleeeTKAKNALAhALQSSrHDGDLLREQYEEEQEGKAELQRALSKANS------EVAQWRTKYETDAIQR 1385
Cdd:PRK10246 267 QQALAAE-------EKAQPQLA-ALSLA-QPARQLRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1386 TEELEEAKKKLAQRLQEAE------EHVEAVNAKCASLEKTKQRLQNEVEDLMLDVE-RSNAACAALDkkqrnfdkvLSE 1458
Cdd:PRK10246 338 SAELQAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQkLNALPAITLT---------LTA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1459 wkqkyEETQAELeASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ------------- 1525
Cdd:PRK10246 409 -----DEVAAAL-AQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRykektqqladvkt 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1526 IHELEKIKKQVEQEKCEIQAALE------------EAEASLEHEEGKILRIQL--ELNQVKSEVDRKIAEKDEEIDQLKR 1591
Cdd:PRK10246 483 ICEQEARIKDLEAQRAQLQAGQPcplcgstshpavEAYQALEPGVNQSRLDALekEVKKLGEEGAALRGQLDALTKQLQR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1592 NHTRVVETMQ--STLDAEIRSRNDALRVKKKMEGDLN-------EMEIQLNHAN-RLA-----AESLRNYRNTQGILKET 1656
Cdd:PRK10246 563 DESEAQSLRQeeQALTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLLSqRHElqgqiAAHNQQIIQYQQQIEQR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1657 QLHLDDALQG-----QEDLKEQLAIVER------------RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLL 1719
Cdd:PRK10246 643 QQQLLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQV 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1720 HTQNTSLintkkklendVSQLQTEVEEVIQESRNAEE---------KAKKAITDAAMMAEELKKEqdTSAHLERMKKNLE 1790
Cdd:PRK10246 723 HEQCLSL----------HSQLQTLQQQDVLEAQRLQKaqaqfdtalQASVFDDQQAFLAALLDEE--TLTQLEQLKQNLE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1791 QtvkdlqhRLDEAEQLALKGGKKQIQKLEARVRELEG--EVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQ 1868
Cdd:PRK10246 791 N-------QRQQAQTLVTQTAQALAQHQQHRPDGLDLtvTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQ 863
|
730
....*....|....*....
gi 1331883584 1869 DLVdklqAKVKSYKRQAEE 1887
Cdd:PRK10246 864 ALM----QQIAQATQQVED 878
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1133-1333 |
9.69e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1133 SKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEAtlqhEAMAAALRKKHADSMAELAEQIDN 1212
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGERARALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1213 LQRVKQKLEKEkselkmEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSR 1292
Cdd:COG3883 102 VSYLDVLLGSE------SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1331883584 1293 LLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALA 1333
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
857-1148 |
1.24e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 857 EDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLqlqVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEIN 936
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL---TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 937 AELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQT 1009
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDkseenarSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1010 LDDLQAEEDKVNI----LTKAKTKLEQQVDDLEGSLE----QEKKLRMDLERAKRKLEGDLKLAQESTMD---------- 1071
Cdd:pfam05483 628 NKQLNAYEIKVNKleleLASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemva 707
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1072 -IENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEE 1148
Cdd:pfam05483 708 lMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1132-1371 |
1.34e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1132 RSKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRR-----DLEEATLQHEAMAAALRKKHADSMAEL 1206
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA--------------EAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1207 AEQIDNLQRVKQKLEKEKSELKMEIDDlssnaEVISKAKGNLEKmcrsLEDQVSELKTKEEEQQRLINDLTAQRAHLQTE 1286
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAE----LEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1287 -AGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAhALQSSRhdgDLLREQYEE--EQEGKAELQRA 1363
Cdd:COG3206 307 lQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR-RLEREV---EVARELYESllQRLEEARLAEA 382
|
....*...
gi 1331883584 1364 LSKANSEV 1371
Cdd:COG3206 383 LTVGNVRV 390
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1498-1909 |
1.65e-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: 53.30 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1498 LETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR 1577
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1578 KIAEKDEEIDQLKRNHTRV----VETMQSTLDAEIRSRNDALRVKKKMEGDL-NEMEIQLNHANRLAAESLRNYRNTQGI 1652
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFldadIETAAADQEQLPSWQSELENLEERLKALTgKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1653 lketqlhlDDALQGQEDLKEQLAIVERraNLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1732
Cdd:pfam12128 396 --------KDKLAKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1733 LENDVSQLQTEVEEviQESRNAE-EKAKKAITDAAMMAEE-LKKEQDTSAHLERMKKNLEQtvkdLQHRLDEAEQLALK- 1809
Cdd:pfam12128 466 LENFDERIERAREE--QEAANAEvERLQSELRQARKRRDQaSEALRQASRRLEERQSALDE----LELQLFPQAGTLLHf 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1810 ------GGKKQIQKLEARVR----ELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDrknvlRLQDLVDKLQAKVK 1879
Cdd:pfam12128 540 lrkeapDWEQSIGKVISPELlhrtDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE-----ELRERLDKAEEALQ 614
|
410 420 430
....*....|....*....|....*....|
gi 1331883584 1880 SYKRQAEEAEEQSNANLSKFRKLQHELEEA 1909
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFA 644
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1464-1756 |
1.99e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1464 EETQAELEASQKeSRSLSTELFKVKNAYEESLDQLETLRR---ENKNLQQEISDLTEQIAEGGKqihELEKIKKQVEQEK 1540
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLDKIDRqkeETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1541 CEIQAA--LEEAEASLEHEEGKILRIQLELNQVKSevdrkiaekdeeidQLKRNHTRvVETMQSTLDA------EIRSRN 1612
Cdd:PRK11281 115 RETLSTlsLRQLESRLAQTLDQLQNAQNDLAEYNS--------------QLVSLQTQ-PERAQAALYAnsqrlqQIRNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1613 DALRVKKKmegDLNEMEIQLNHAnRLAAESLRNYRNTQGILKETQLHldDALQGQEDLK-EQLAIVERRANLLQAEIEEL 1691
Cdd:PRK11281 180 KGGKVGGK---ALRPSQRVLLQA-EQALLNAQNDLQRKSLEGNTQLQ--DLLQKQRDYLtARIQRLEHQLQLLQEAINSK 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1692 RatLEQTErsRKIAEQELLDASERVQ---LLHTQ---NTS----LINTKKKLeNDVSQ--LQTE--VEEVIQESRNAEE 1756
Cdd:PRK11281 254 R--LTLSE--KTVQEAQSQDEAARIQanpLVAQEleiNLQlsqrLLKATEKL-NTLTQqnLRVKnwLDRLTQSERNIKE 327
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1663-1920 |
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 1331883584 1663 ALQGQEDLKEQLaivERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQT 1742
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1743 EVEEVIQESRNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1816
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1817 KLEARVRELEGEVENEQKRNAEAVKglrkherrvkeltyqteedrknvlRLQDLVDKLQAKVKSYKRQAEEAEEQSnanl 1896
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA------------------------ERQKLLARLEKELAELAAELAELQQEA---- 222
|
250 260
....*....|....*....|....
gi 1331883584 1897 skfRKLQHELEEAEERADIAESQV 1920
Cdd:COG4942 223 ---EELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
996-1248 |
3.07e-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: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 996 SKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQekklrmdLERAKRKLEGDLKLAQESTMDIEND 1075
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1076 KQQLDEKLKKKEFEISNLISKIED-EQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLsRELEEISERLE 1154
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1155 EaggatsaQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKhadsMAELAEQIDNLQRVKQKLEKEKSELKMEIDDL 1234
Cdd:COG4942 171 A-------ERAELEALLAELEEERAALEALKAERQKLLARLEKE----LAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|....*.
gi 1331883584 1235 S--SNAEVISKAKGNL 1248
Cdd:COG4942 240 AerTPAAGFAALKGKL 255
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1312-1798 |
3.07e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1312 TQQIEEL-KHQLEEETK--AKNALAHALQSSRHDGDLL--REQYEEEQEGKAELQRALSKANSEVaqwrtkyetdaiqrt 1386
Cdd:COG3096 251 TQSDRDLfKHLITEATNyvAADYMRHANERRELSERALelRRELFGARRQLAEEQYRLVEMAREL--------------- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1387 EELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERSNAacaaldkkqrnfdkVLSEWKQKYEET 1466
Cdd:COG3096 316 EELSARESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQEDLEELTERLEEQEE--------------VVEEAAEQLAEA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1467 QAELEASQKESRSLSTELFKvknaYEESLDQLETlrrenKNLQQeisdlteqiaeggkqihelekikKQVEQEKCEIQAA 1546
Cdd:COG3096 381 EARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAIQY-----------------------QQAVQALEKARAL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1547 LEEAEASLEHEEGKILRIQLELNQVKSEVdRKIAEKDEEIDQLKRNHTRVVETMQStLDAEIrSRNDALRVKKKMEGDLN 1626
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELVCK-IAGEV-ERSQAWQTARELLRRYR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1627 EMEIQLNHANRLAAE------SLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAiverranLLQAEIEELRATLEQTER 1700
Cdd:COG3096 506 SQQALAQRLQQLRAQlaeleqRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQAAEAVE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1701 SRKIAEQELLDASERVQLLHTQNTSLINTKKKLEndvsQLQTEVEEVIQESRnaeekakkAITDAamMAEELKKEQDTSA 1780
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARAPAWLAAQDALE----RLREQSGEALADSQ--------EVTAA--MQQLLEREREATV 644
|
490 500
....*....|....*....|.
gi 1331883584 1781 ---HLERMKKNLEQTVKDLQH 1798
Cdd:COG3096 645 erdELAARKQALESQIERLSQ 665
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1192-1553 |
3.25e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1192 AAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQR 1271
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1272 LINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKH-------QLEEETKAKNALAHALQSSRHDGD 1344
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErakkagaQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1345 LLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQEAEEHVEAVNAKCASLEKTK 1421
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1422 QRLQNEVEDLMLDVERSNAACAALDKKQRNFDkvlSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEE-------- 1493
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerekl 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1494 ----------SLDQLETLRRENKNL-------QQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEAS 1553
Cdd:pfam07888 345 evelgrekdcNRVQLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPD 421
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1201-1521 |
4.08e-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: 51.78 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1201 DSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAeviskakgnlekmcRSLEDQVSELKTKEEE-QQRLINDLTAQ 1279
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLE--------------RSLKSELGQLRQENDLlQTKLHNAVSAK 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1280 RAHLQTEAGEYSRLLDEKDAlvsqlsrRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLReqyeeeqegkae 1359
Cdd:pfam09726 461 QKDKQTVQQLEKRLKAEQEA-------RASAEKQLAEEKKRKKEEEATAARAVALAAASRGECTESLK------------ 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1360 lqralskansevaqwrtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRlQNEVEDLMldversn 1439
Cdd:pfam09726 522 ------------------------QRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKES-EKDTEVLM------- 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1440 AACAALDKKQRNFDKVLSewkqkyEETQAELeasqkesrslstELFkvkNAYEESLDQLETLRRENKNLQQEISDLTEQI 1519
Cdd:pfam09726 570 SALSAMQDKNQHLENSLS------AETRIKL------------DLF---SALGDAKRQLEIAQGQIYQKDQEIKDLKQKI 628
|
..
gi 1331883584 1520 AE 1521
Cdd:pfam09726 629 AE 630
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1602-1929 |
4.85e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1602 STLDAEIRSRNDALRVKKKMEGDLNEMEiqlnhaNRLAAESLRNYR--NTQGILKETQ---LHLDDA-LQGQEDLKEQLA 1675
Cdd:PLN02939 90 STSSDDDHNRASMQRDEAIAAIDNEQQT------NSKDGEQLSDFQleDLVGMIQNAEkniLLLNQArLQALEDLEKILT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1676 ivERRAnlLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQEsrNAE 1755
Cdd:PLN02939 164 --EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE--NML 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1756 EKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENE 1832
Cdd:PLN02939 238 LKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1833 QKRNAEAVKGLRKH---ERRVKELTYQTEEdrKNVLRLQ-DLVDKLQAKVKSykrqAEEAEEQSNANLSKFRKLQHELee 1908
Cdd:PLN02939 313 TNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKL----LEERLQASDHEIHSYIQLYQES-- 384
|
330 340
....*....|....*....|.
gi 1331883584 1909 AEERADIAESQVNKLRVKSRE 1929
Cdd:PLN02939 385 IKEFQDTLSKLKEESKKRSLE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1653-1861 |
4.94e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1653 LKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1732
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1733 LENDVSQLqteveEVIQESRNAEE-----KAKKAITDA-AMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQl 1806
Cdd:COG3883 98 SGGSVSYL-----DVLLGSESFSDfldrlSALSKIADAdADLLEELKADKAE---LEAKKAELEAKLAELEALKAELEA- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1807 ALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDR 1861
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1330-1890 |
4.98e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1330 NALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE--TDAIQRTEELEEAKKKLAQRLQEAEEHV 1407
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1408 EAVNAKCASLEKTKQRLqNEVEDLMLDVERSNAACAALDKKQ-RNFDKVLSEWK---QKYEETQAELEASQKESrslste 1483
Cdd:PRK01156 266 SMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIKKLSVLQKDY------ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1484 lfkvknayeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILR 1563
Cdd:PRK01156 339 ------------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1564 IQLELNQVKSEVDR---KIAEKDEEIDQLKRNHTRVVETMQ------------STLDAEI--RSRNDALRVKKKMEGDLN 1626
Cdd:PRK01156 407 IKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgTTLGEEKsnHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1627 EMEIQLNHAN-----------RLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQlaivERRANLLQAEIEELRatl 1695
Cdd:PRK01156 487 EIEIEVKDIDekivdlkkrkeYLESEEINKSINEYNKIESARADLEDIKIKINELKDK----HDKYEEIKNRYKSLK--- 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1696 eqtersrkiaeqelldaserVQLLHTQNTSLINTKKKLEN-DVSQLQTEVEEViqesrnaeekaKKAITDAAMMAEELKK 1774
Cdd:PRK01156 560 --------------------LEDLDSKRTSWLNALAVISLiDIETNRSRSNEI-----------KKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1775 E-QDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELE---GEVENEQKRNAEAVKGLRKHERRV 1850
Cdd:PRK01156 609 GfPDDKSYIDKSIREIENEANNLNNKYNEIQEN-----KILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNL 683
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1331883584 1851 KELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEE 1890
Cdd:PRK01156 684 KKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
980-1244 |
6.19e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 980 NLTEEMAGLDEIIAKLSKEKKALQ---ETHQQTLDDLQAEEDKVNILTKAKTkLEQQVDDLEGSLEQEKKLRMDLERAKR 1056
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRkelEEAEAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1057 KLEGDLKLAQESTMDIENDK--QQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERAS-RS 1133
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAeLE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1134 KAEKQRSDLSRELEEISERLEEAGgatsaqvelnkKREAEFQKLRRDLEEATLQHEAMaaalrkkhadsmaelaeqidnL 1213
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELP-----------ELEAELRRLEREVEVARELYESL---------------------L 371
|
250 260 270
....*....|....*....|....*....|.
gi 1331883584 1214 QRVKqklekeksELKMEIDDLSSNAEVISKA 1244
Cdd:COG3206 372 QRLE--------EARLAEALTVGNVRVIDPA 394
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1646-1935 |
6.91e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1646 YRNTQGILKETQL---HLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLD---ASERVQLL 1719
Cdd:PRK03918 164 YKNLGEVIKEIKRrieRLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1720 HTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNLEQtvkdlqhr 1799
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD-------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1800 ldeaeqlalkgGKKQIQKLEARVRELEGEVEneqkrnaEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQaKVK 1879
Cdd:PRK03918 308 -----------ELREIEKRLSRLEEEINGIE-------ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAK 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1880 SYKRQAEEAEEQSnANLSKfRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVS 1935
Cdd:PRK03918 369 AKKEELERLKKRL-TGLTP-EKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1027-1552 |
7.11e-06 |
|
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: 50.89 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1027 KTKLEQQVDDLEGSLEQEKKLRMDLERA----KRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQA 1102
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKasalKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1103 VEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSR---ELEEISERLEEaggatsaqvelNKKREAEFQKLRR 1179
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQStnsELEELQERLDL-----------LKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1180 DLEEAtlQHEAMAAALRKKhaDSMAELAEQIDNLQRVKQ---------KLEKEKSELKMEIDDLSSNAEVISkakgnlek 1250
Cdd:pfam05557 157 NLEKQ--QSSLAEAEQRIK--ELEFEIQSQEQDSEIVKNskselaripELEKELERLREHNKHLNENIENKL-------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1251 mcrSLEDQVSELKTK---EEEQQRLINDLTAQRAHLQTEAGEYSRL-------LDEKDAL---VSQLSRRKQASTQQIEE 1317
Cdd:pfam05557 225 ---LLKEEVEDLKRKlerEEKYREEAATLELEKEKLEQELQSWVKLaqdtglnLRSPEDLsrrIEQLQQREIVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1318 LKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEelEEAKKKLA 1397
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--SNYSPQLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1398 QRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFD-----KVLSEWKQKYEETQAELEA 1472
Cdd:pfam05557 380 ERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADpsyskEEVDSLRRKLETLELERQR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1473 SQKESRSLSTEL-------------FKV--------KNAYEESLDQLETLRRENKNLQQEISDLTeqiAEGGKQIHELEK 1531
Cdd:pfam05557 460 LREQKNELEMELerrclqgdydpkkTKVlhlsmnpaAEAYQQRKNQLEKLQAEIERLKRLLKKLE---DDLEQVLRLPET 536
|
570 580
....*....|....*....|.
gi 1331883584 1532 IKKQVEQEKCEIQAALEEAEA 1552
Cdd:pfam05557 537 TSTMNFKEVLDLRKELESAEL 557
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1348-1558 |
7.30e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1348 EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNE 1427
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1428 VEDLM----LDVE------RSNAACAALDKKQRNFDKVLSEWKQKYEEtqaelEASQKESRSLSTeLFKVKNAYEESLDQ 1497
Cdd:PRK05771 123 IERLEpwgnFDLDlslllgFKYVSVFVGTVPEDKLEELKLESDVENVE-----YISTDKGYVYVV-VVVLKELSDEVEEE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1498 LETLRRENKNL------QQEISDLTEQIAEGGKQIHEL-EKIKKQVEQEKCEIQAALEEAEASLEHEE 1558
Cdd:PRK05771 197 LKKLGFERLELeeegtpSELIREIKEELEEIEKERESLlEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1671-1934 |
9.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1671 KEQLAIVE--RRANLLQAEIEELRATLEQ-------TERsRKIAEQELLDASE---RVQLLHTQntslinTKKKLENdvS 1738
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--L 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1739 QLQTEVEEVIQESRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKL 1818
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1819 EARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSK 1898
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
250 260 270
....*....|....*....|....*....|....*.
gi 1331883584 1899 FRKLQHELEEAEERADIAESQVNKLRVKSREVHTKV 1934
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1389-1599 |
9.16e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1389 LEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAAcaaldkkqrnfdkvLSEWKQKYEETQA 1468
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA--------------LNKLNTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1469 ELEASQKESRSLS--TELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEqekcEIQAA 1546
Cdd:PHA02562 270 KIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNK 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1547 LEEAEASLEHEEGKILRIQLELNQVKSEVdrkiAEKDEEIDQLKRNHTRVVET 1599
Cdd:PHA02562 346 ISTNKQSLITLVDKAKKVKAAIEELQAEF----VDNAEELAKLQDELDKIVKT 394
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1351-1543 |
9.22e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1351 EEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqeaeehVEAVNAKCASLEKTKQRLQNEVED 1430
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1431 lmldversnaacaaLDKKQRNFDKVLSEWKQKYEETQAELEasqkESRSLSTElfkvkNAYEESLDQLEtlrrenknlqq 1510
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELE----RISGLTAE-----EAKEILLEKVE----------- 164
|
170 180 190
....*....|....*....|....*....|...
gi 1331883584 1511 eiSDLTEQIAEGGKQIHelEKIKKQVEQEKCEI 1543
Cdd:PRK12704 165 --EEARHEAAVLIKEIE--EEAKEEADKKAKEI 193
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1730-1893 |
1.07e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1730 KKKLENDVSQLQTEVEEVIQESRN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMK-KNLEQTVKDLQHRLDEAEQLA 1807
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1808 lkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQAKVKSYKRQAE- 1886
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL-LEKVEEEARHEAAVLIKEIEe 180
|
....*..
gi 1331883584 1887 EAEEQSN 1893
Cdd:PRK12704 181 EAKEEAD 187
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
850-1636 |
1.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 850 KEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQliKNKIQ--------LEAK 921
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIEryqadleeLEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 922 IKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNL--TEEMAGLDEIIAklskek 999
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALerAKQLCGLPDLTA------ 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1000 KALQETHQQtlddLQAEEDKvniLTKAKTKLEQQVDDLEGSLEQ-EKKLR--------MDLERAKRKlegdlklAQESTM 1070
Cdd:PRK04863 438 DNAEDWLEE----FQAKEQE---ATEELLSLEQKLSVAQAAHSQfEQAYQlvrkiageVSRSEAWDV-------ARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1071 DIENDKQQlDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEeieaerasrskAEKQRSDLSRELEEIS 1150
Cdd:PRK04863 504 RLREQRHL-AEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE-----------LEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1151 ERLEEAGGATSAQVELNKKREAEFQKLRRdLEEATLQHEAMAAALRKKHADS----------MAELAEQIDNLQRVKQKL 1220
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA-RAPAWLAAQDALARLREQSGEEfedsqdvteyMQQLLERERELTVERDEL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1221 EKEKSELKMEIDDLSsnaeviSKAKGNLEKMCRSLED----QVSELK---TKEE-----------EQQRLINDLTAQRAH 1282
Cdd:PRK04863 651 AARKQALDEEIERLS------QPGGSEDPRLNALAERfggvLLSEIYddvSLEDapyfsalygpaRHAIVVPDLSDAAEQ 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1283 LQTE----------AGEYSRLLDE-------KDALVSQLSRR--------------KQASTQQIEELKHQLEEETkakna 1331
Cdd:PRK04863 725 LAGLedcpedlyliEGDPDSFDDSvfsveelEKAVVVKIADRqwrysrfpevplfgRAAREKRIEQLRAEREELA----- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1332 lahalqssrhdgdllrEQYEEEQEGKAELQRALSKANSEVA-------QWRTKYETDAIQRT--------EELEEAKKKL 1396
Cdd:PRK04863 800 ----------------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRrveleralADHESQEQQQ 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1397 AQRLQEAEEHVEAVNaKCASLEKTKQR--LQNEVEDLMLDVERSNAACAALDKKQRNFDKV-------------LSEWKQ 1461
Cdd:PRK04863 864 RSQLEQAKEGLSALN-RLLPRLNLLADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQ 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1462 KYEETQAELEASQKESRSLsTELFKVKN--AYEESLDQL-------ETLRRENKNLQQEISDLTEQIAEGGKQIHEleki 1532
Cdd:PRK04863 943 DYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEMLaknsdlnEKLRQRLEQAEQERTRAREQLRQAQAQLAQ---- 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1533 KKQVEQE-KCEIQAALEE-AEASLEHEEgkilriqLELNQVKSEVDRKIAEKDEEIDQLKRNHTRV--VETMQSTLDAEI 1608
Cdd:PRK04863 1018 YNQVLASlKSSYDAKRQMlQELKQELQD-------LGVPADSGAEERARARRDELHARLSANRSRRnqLEKQLTFCEAEM 1090
|
890 900
....*....|....*....|....*...
gi 1331883584 1609 RSRNDALRvkkKMEGDLNEMEIQLNHAN 1636
Cdd:PRK04863 1091 DNLTKKLR---KLERDYHEMREQVVNAK 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1145 |
1.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 939 LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQ---A 1015
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsgG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1016 EEDKVNILTKAK---------TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKK 1086
Cdd:COG3883 101 SVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1087 EFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRE 1145
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1514-1929 |
1.28e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.35 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1514 DLTEQIAEGGKQIHELEKIKKQVEQEKCEI--------QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIaEKDEE 1585
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLltlctpcmPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1586 IDQLKRNHTRVVETMQS--TLDAEIRSRNDALRVKKKMEGDLNEMEiQLNHANRLAAESLRNYRNTQGILKETQLHLDDA 1663
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1664 LQGQEDLKEQlaivERRANLLQAEIEELRATLEQTERSRKIAEQELLDaSERVQLLHTQNTSLINTKKKLENDVSQLQTE 1743
Cdd:TIGR00618 334 VKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1744 VEEviQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVK-----DLQHRLDEAEQLalKGGKKQIQKL 1818
Cdd:TIGR00618 409 QAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlqESAQSLKEREQQ--LQTKEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1819 EARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQakvksykrqaeEAEEQSNANLSK 1898
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE-----------TSEEDVYHQLTS 553
|
410 420 430
....*....|....*....|....*....|.
gi 1331883584 1899 FRKLQHELEEAEERADIAESQVNKLRVKSRE 1929
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKE 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1677-1921 |
1.35e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1677 VERRANLLQAEIEELRAtleqtersrkiAEQELLDASERVQLLhTQNTSLINTKKKLENDVSQLQTEVEEViqesrnaee 1756
Cdd:COG4913 223 TFEAADALVEHFDDLER-----------AHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAL--------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1757 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEArvrelegEVENEQKRN 1836
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER-------EIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1837 AEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEeaEERADIA 1916
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE--AEIASLE 432
|
....*
gi 1331883584 1917 ESQVN 1921
Cdd:COG4913 433 RRKSN 437
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1132-1431 |
1.46e-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: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1132 RSKAEKQRSDLSRELEEISERLEEAggatSAQVElnkkreaEFQKLRRDLEEATLQH---------EAMAAALRKKHADS 1202
Cdd:COG3096 780 RAAREKRLEELRAERDELAEQYAKA----SFDVQ-------KLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSEL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1203 MAELAEQIDNLQRVKQKLEKEKSELKMeIDDLSSNAEVIskAKGNLEKMCRSLEDQVSELKTKE---EEQQRLINDLTAQ 1279
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLDQLKEQLQL-LNKLLPQANLL--ADETLADRLEELREELDAAQEAQafiQQHGKALAQLEPL 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1280 RAHLQTEAGEYSRLLDEKDALVSQLSRRKQ---ASTQQIEELKHQLEEETKAKNALAHALQssrhdgDLLREQYEEEQEG 1356
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQqifALSEVVQRRPHFSYEDAVGLLGENSDLN------EKLRARLEQAEEA 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1357 KAELQRALSKANSEVAQW-----------RTKYET--DAIQRTEELE-----EAKKKLAQRLQEAEEHVEAVNAKCASLE 1418
Cdd:COG3096 1000 RREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLE 1079
|
330
....*....|...
gi 1331883584 1419 KTKQRLQNEVEDL 1431
Cdd:COG3096 1080 KQLTRCEAEMDSL 1092
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1136-1810 |
1.49e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1136 EKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEamaaalrKKHADSMAELAEQidNLQR 1215
Cdd:COG5022 834 ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQEL-------KIDVKSISSLKLV--NLEL 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1216 VKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMcrsledQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLD 1295
Cdd:COG5022 905 ESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNI------DLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLK 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1296 EKDALVSQL------SRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEgKAELQRALSKANS 1369
Cdd:COG5022 979 KSTILVREGnkanseLKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSI-LKPLQKLKGLLLL 1057
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1370 EVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEhvEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQ 1449
Cdd:COG5022 1058 ENNQLQARYKALKLRRENSLLDDKQLYQLESTENLL--KTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFL 1135
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1450 RNFDKVLSEWKQKYEETQAELEASQKESrSLSTELFKVKNAY--EESLDQLETLRRENKNLQQEISDLTEQIaeggkqIH 1527
Cdd:COG5022 1136 SQLVNTLEPVFQKLSVLQLELDGLFWEA-NLEALPSPPPFAAlsEKRLYQSALYDEKSKLSSSEVNDLKNEL------IA 1208
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1528 ELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKilriqlelnqvksevdrkiaekdEEIDQLKRNHTRVVETMQSTLdaE 1607
Cdd:COG5022 1209 LFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLK-----------------------GFNNLNKKFDTPASMSNEKLL--S 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1608 IRSRNDALRVKKKMEGDLNEMEI--QLNHANRLAAESLRNYRNtqgILKETQlhLDDALQGQEDLKEQlaIVERRANLLQ 1685
Cdd:COG5022 1264 LLNSIDNLLSSYKLEEEVLPATInsLLQYINVGLFNALRTKAS---SLRWKS--ATEVNYNSEELDDW--CREFEISDVD 1336
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1686 AEIEElratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINtKKKLENDVSQLQTEVEEVIQEsrnaEEKAKKAITDA 1765
Cdd:COG5022 1337 EELEE----LIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQ-NLKSRYDPADKENNLPKEILK----KIEALLIKQEL 1407
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1331883584 1766 AMMAEELKKEQDTSAHLERMKKN---LEQTVKDLQHRLDEAEQLALKG 1810
Cdd:COG5022 1408 QLSLEGKDETEVHLSEIFSEEKSlisLDRNSIYKEEVLSSLSALLTKE 1455
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
943-1245 |
1.57e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 943 KRKLEDECSELKKDIDDLELTLAKvekekhaTENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNI 1022
Cdd:pfam07888 68 REQWERQRRELESRVAELKEELRQ-------SREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1023 LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQA 1102
Cdd:pfam07888 141 LTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1103 VEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSR-----------------ELEEISERLEEA------GGA 1159
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqaelhqarlQAAQLTLQLADAslalreGRA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1160 TSAQ--------VELNKKR----EAEFQKLRRDLEEATLQHEAMAAAL-------RKKHADSMAELAEQIDNL---QRVK 1217
Cdd:pfam07888 301 RWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdcnRVQLSESRRELQELKASLrvaQKEK 380
|
330 340
....*....|....*....|....*...
gi 1331883584 1218 QKLEKEKSELKMEIDDLSSNAEVISKAK 1245
Cdd:pfam07888 381 EQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| Nucleoporin_FG2 |
pfam15967 |
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
1206-1350 |
2.15e-05 |
|
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.
Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 49.28 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1206 LAEQIDNLQrvkqKLEKEKSELKMEIDDLSSNAevISKAKGNLEKMCRSLEDQVSEL--------KTKEEEQQRLINDLT 1277
Cdd:pfam15967 249 ICQDVENFQ----KFVKEQKQVQEEISRMSSKA--MLKVQDDIKALKQLLSVAASGLqrnslaidKLKIETAQELKNADI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1278 AQRA--------HLQTEAGEYSRlldekdALVSQLSRRKQASTQQIEELKHQLEEETKAKN------------------A 1331
Cdd:pfam15967 323 ALRTqktppglqHENTAPADYFR------SLVEQFEVQLQQYRQQIEELENHLTTQSSSSHitpqdlslamqklyqtfvA 396
|
170
....*....|....*....
gi 1331883584 1332 LAHALQSSRHDGDLLREQY 1350
Cdd:pfam15967 397 LAAQLQSVHENVKILKEQY 415
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1312-1757 |
2.30e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1312 TQQIEEL-KHQLEEETK--AKNALAHALQSSRHDgdllreqyeeeqEGKAELQRALSKANSEVAQWRTKYeTDAIQRTEE 1388
Cdd:PRK04863 252 TQSDRDLfKHLITESTNyvAADYMRHANERRVHL------------EEALELRRELYTSRRQLAAEQYRL-VEMARELAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1389 LEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERSNAACAALDKKQrnfdkvlsewkqkyEETQA 1468
Cdd:PRK04863 319 LNEAESDLEQDYQAASDHLNLVQTALRQQEKI-ERYQADLEELEERLEEQNEVVEEADEQQ--------------EENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1469 ELEASQKESRSLSTELFKvknaYEESLDQLET-----------LRRENKNLQqeISDLTEQIAEGgkQIHELEKIKKQVE 1537
Cdd:PRK04863 384 RAEAAEEEVDELKSQLAD----YQQALDVQQTraiqyqqavqaLERAKQLCG--LPDLTADNAED--WLEEFQAKEQEAT 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1538 QEKCEIQAALEEAEASLE-HEEGKILriqleLNQVKSEVDRKIAEkdeeidqlkrnhtrvvETMQSTLDAEIRSRNDALR 1616
Cdd:PRK04863 456 EELLSLEQKLSVAQAAHSqFEQAYQL-----VRKIAGEVSRSEAW----------------DVARELLRRLREQRHLAEQ 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1617 VKKkMEGDLNEMEIQLNH---ANRLAAESlrNYRNTQGILKETQL--HLDDALQGQEDLKEQLAIVERRANLLQAEIEEL 1691
Cdd:PRK04863 515 LQQ-LRMRLSELEQRLRQqqrAERLLAEF--CKRLGKNLDDEDELeqLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1692 RAtleQTERSRKIAeQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEK 1757
Cdd:PRK04863 592 QA---RIQRLAARA-PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1349-1553 |
2.51e-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: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1349 QYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEV 1428
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1429 EDLMLDVERSNAACAALDK--KQRNFDKVLSEWK-------------QKYEETQAELEASQKESRSLSTELFKVKNAYEE 1493
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1494 SLDQLETLRRENknlQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEAS 1553
Cdd:COG3883 169 AKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
960-1244 |
2.62e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.37 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 960 LELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKA--KTKLEQQVDDL 1037
Cdd:pfam09731 138 ISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQseEEAAPPLLDAA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1038 EGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEIS------NLISKIEDEQAVE------I 1105
Cdd:pfam09731 218 PETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIpvlkedNLLSNDDLNSLIAhahreiD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1106 QLQKKIKELQARIEELEeeieaerasRSKAEKQRSDLSRELEEISERLEEAGGATSAQveLNKKREAEFQKLRRDLEE-- 1183
Cdd:pfam09731 298 QLSKKLAELKKREEKHI---------ERALEKQKEELDKLAEELSARLEEVRAADEAQ--LRLEFEREREEIRESYEEkl 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1184 -ATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKA 1244
Cdd:pfam09731 367 rTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1004-1188 |
2.81e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1004 ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQEstmDIENDK 1076
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1077 QQLDEKLKKKEFEisNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIeaerasrSKAEKQRSDLSRELEEISERLEEA 1156
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 1331883584 1157 GGATSAQVElnkKREAEFQKLRRDLEEATLQH 1188
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
988-1406 |
3.22e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.92 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 988 LDEIIAKLSKEKKALQ---ETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDL-- 1062
Cdd:pfam05622 19 LDQQVSLLQEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1063 ---------KLAQEST-----MDIendKQQLDEKLKKKEFEISNLISKIEDEQaveiQLQKKIKELQArieeleeeieae 1128
Cdd:pfam05622 99 lqhrneeltSLAEEAQalkdeMDI---LRESSDKVKKLEATVETYKKKLEDLG----DLRRQVKLLEE------------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1129 rasRSKAEKQRSdlsRELEEISERleeaGGATSAQVELNKKreaEFQKLRRDLEEATLQHEAMAAALRKKHadsmaelaE 1208
Cdd:pfam05622 160 ---RNAEYMQRT---LQLEEELKK----ANALRGQLETYKR---QVQELHGKLSEESKKADKLEFEYKKLE--------E 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1209 QIDNLQRVKQKLEKEKSELKMEIDDL---SSNAEVISKAKGNLEKMCRSLEDQVSELKTKE--EEQQRLIND----LTAQ 1279
Cdd:pfam05622 219 KLEALQKEKERLIIERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRLQHEnkmlRLGQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1280 RAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAhalqSSRHDGDLLREQYEEEQEGKAE 1359
Cdd:pfam05622 299 EGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAEDSSLLKQKLEEHLEKLHE 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1331883584 1360 LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEH 1406
Cdd:pfam05622 375 AQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
850-1795 |
3.54e-05 |
|
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: 49.28 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 850 KEMATMKEDFQKTKDELAKseaKRKELEEKMVTLLKEKNDLQLQVQSEADsladaeercEQLIKNKIQLEAKikevtera 929
Cdd:TIGR01612 547 KESYELAKNWKKLIHEIKK---ELEEENEDSIHLEKEIKDLFDKYLEIDD---------EIIYINKLKLELK-------- 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 930 eeeeeinaeltAKKRKLEDECSELKKDIDdleltLAKVEKEKHATENKVK-----NLTEEMAGLDEIIAKLSKEkkaLQE 1004
Cdd:TIGR01612 607 -----------EKIKNISDKNEYIKKAID-----LKKIIENNNAYIDELAkispyQVPEHLKNKDKIYSTIKSE---LSK 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1005 THQQTLDDLQAE------EDKVNIlTKAKTKLeqqvDDLEGSLEQEKKLRMDLERAKRKLegdlklaqeSTMDIENDKQQ 1078
Cdd:TIGR01612 668 IYEDDIDALYNElssivkENAIDN-TEDKAKL----DDLKSKIDKEYDKIQNMETATVEL---------HLSNIENKKNE 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1079 LDE---KLKKKEF-EISNLISKI-EDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERL 1153
Cdd:TIGR01612 734 LLDiivEIKKHIHgEINKDLNKIlEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNY 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1154 EEAGGATSAqveLNKKREAEFQKLR--RDLEEATLQHEAMAAALRKKHAD-------SMAELAEQI------DNLQRVKQ 1218
Cdd:TIGR01612 814 DKSKEYIKT---ISIKEDEIFKIINemKFMKDDFLNKVDKFINFENNCKEkidseheQFAELTNKIkaeisdDKLNDYEK 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1219 KLEKEKS---ELKMEIDDLSSNAEVISKAKGNLeKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLD 1295
Cdd:TIGR01612 891 KFNDSKSlinEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFD 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1296 ekDALVSQLSRRKQASTQ-QIEELKHQLEEETKAKNALAHALQSSRhdGDLLREQYEEEQEGKAELQRALSKANSEVAQW 1374
Cdd:TIGR01612 970 --NTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNK--ENMLYHQFDEKEKATNDIEQKIEDANKNIPNI 1045
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1375 RTKYETDAIQRTEELEEAKKKLAQRLQEaeEHVEAVNAKCASLEKTKQRLqnevedlmldversnaacaaldkKQRNFDK 1454
Cdd:TIGR01612 1046 EIAIHTSIYNIIDEIEKEIGKNIELLNK--EILEEAEINITNFNEIKEKL-----------------------KHYNFDD 1100
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1455 VLSEWKQKYEEtqaELEASQKESRSLSTELFKVKNAYEESLDQLETLRREnknLQQEISDLtEQIAEGGKQIHELEKIKK 1534
Cdd:TIGR01612 1101 FGKEENIKYAD---EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDE---IKAQINDL-EDVADKAISNDDPEEIEK 1173
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1535 QVEQ--EKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSeVDRKIAEKD-----EEIDQLKRNHTRVVETMQSTLDae 1607
Cdd:TIGR01612 1174 KIENivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKG-INLSYGKNLgklflEKIDEEKKKSEHMIKAMEAYIE-- 1250
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1608 irsrnDALRVKKKMEGDLNEMEIQLNHANRLAAESLRN--YRNTQGILKETQLHLDDALQgqedlkEQLAIVErrANLLQ 1685
Cdd:TIGR01612 1251 -----DLDEIKEKSPEIENEMGIEMDIKAEMETFNISHddDKDHHIISKKHDENISDIRE------KSLKIIE--DFSEE 1317
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1686 AEIEELRATLEQTersrkiaeqeLLDASER---VQLLHTQNTSLINTKKKleNDVSQLQTEVEEVIQESrnaeEKAKKAI 1762
Cdd:TIGR01612 1318 SDINDIKKELQKN----------LLDAQKHnsdINLYLNEIANIYNILKL--NKIKKIIDEVKEYTKEI----EENNKNI 1381
|
970 980 990
....*....|....*....|....*....|...
gi 1331883584 1763 TDAAMMAEELKKEQDTSAHLERMKKNLEQTVKD 1795
Cdd:TIGR01612 1382 KDELDKSEKLIKKIKDDINLEECKSKIESTLDD 1414
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1192-1936 |
3.62e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1192 AAALRKKHADSMAELAEQIDNLQRVKQKLE---KEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDqVSELKTKEEE 1268
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQYRLVEMARELAelnEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQAD-LEELEERLEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1269 QQRLINDLTAQRAHLQTEAGEYSrllDEKDALVSQLSRRKQA-STQQIEELKHQleeetKAKNALAHAlqssrhdgdllr 1347
Cdd:PRK04863 367 QNEVVEEADEQQEENEARAEAAE---EEVDELKSQLADYQQAlDVQQTRAIQYQ-----QAVQALERA------------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1348 eqyeEEQEGKAELqrALSKANSEVAQWRTKYEtdaiQRTEELEEakkkLAQRLQEAEEHVEAVnAKCASLektkqrlqne 1427
Cdd:PRK04863 427 ----KQLCGLPDL--TADNAEDWLEEFQAKEQ----EATEELLS----LEQKLSVAQAAHSQF-EQAYQL---------- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1428 VEDLMLDVERSNAACAALDK-----KQRNFDKVLSEWKQKYEETQAELEASQKESRSLsTELFKVKNAYEESLDQLETLR 1502
Cdd:PRK04863 482 VRKIAGEVSRSEAWDVARELlrrlrEQRHLAEQLQQLRMRLSELEQRLRQQQRAERLL-AEFCKRLGKNLDDEDELEQLQ 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1503 REnknLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEI----------QAALE-------EAEASLEHEEGKILRIQ 1565
Cdd:PRK04863 561 EE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLaarapawlaaQDALArlreqsgEEFEDSQDVTEYMQQLL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1566 L---ELNQVKSEVDRKIAEKDEEIDQLKRNHT-------RVVETMQSTLDAEIRSR----------------------ND 1613
Cdd:PRK04863 638 ErerELTVERDELAARKQALDEEIERLSQPGGsedprlnALAERFGGVLLSEIYDDvsledapyfsalygparhaivvPD 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1614 ALRVKKKMEGD--------LNEMEIQLNHANRLAAESLRNyrntqGILKET---QL----HLDDALQGQEDLKEQLAIVE 1678
Cdd:PRK04863 718 LSDAAEQLAGLedcpedlyLIEGDPDSFDDSVFSVEELEK-----AVVVKIadrQWrysrFPEVPLFGRAAREKRIEQLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1679 RRANLLQAEIEELRATLEQTER-----SRKIA-----------EQELLDASERVQllhtqntslintkkKLENDVSQLqt 1742
Cdd:PRK04863 793 AEREELAERYATLSFDVQKLQRlhqafSRFIGshlavafeadpEAELRQLNRRRV--------------ELERALADH-- 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1743 evEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSahlermkknLEQTVKDLQHRLDEAEQLA--LKGGKKQIQKLE- 1819
Cdd:PRK04863 857 --ESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET---------LADRVEEIREQLDEAEEAKrfVQQHGNALAQLEp 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1820 --ARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTE-------EDRKNVL-RLQDLVDKLQAKVKSYKRQAEEAE 1889
Cdd:PRK04863 926 ivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAR 1005
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1890 E---QSNANL-----------SKFRKLQHELEEAEERAD-----IAESQVNKLRVKSREVHTKVSA 1936
Cdd:PRK04863 1006 EqlrQAQAQLaqynqvlaslkSSYDAKRQMLQELKQELQdlgvpADSGAEERARARRDELHARLSA 1071
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1314-1554 |
3.62e-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: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1314 QIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEgkaELQRALSKAnsevaQWRTKYETDAIQRTEELEEAK 1393
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAKA-----QQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1394 KKLAQRLQEAEEHVEAVNAKCASL-EKTKQRLQNEVEDLMLDVERSNaacaaLDKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1473 SQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTeqiAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEA 1552
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 1331883584 1553 SL 1554
Cdd:pfam06008 244 SL 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1735-1929 |
4.10e-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: 48.22 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1735 NDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQ 1814
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1815 IQKLEARVRELEGEVENEQKRNAEAV----KGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEE 1890
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1331883584 1891 QSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1929
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
855-1454 |
4.35e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 855 MKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERceqlIKNKIQLEAKIKEVTERAEEEEE 934
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSA----LNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 935 INAELTAKKRKLEDECSELKKDIDDleltlaKVEKEKHATeNKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQtLDDLQ 1014
Cdd:PRK01156 264 DLSMELEKNNYYKELEERHMKIIND------PVYKNRNYI-NDYFKYKNDIENKKQILSNIDAEINKYHAIIKK-LSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1015 AEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgdlklaqESTMDIENDKQQLDEKLKKKEFEISNLI 1094
Cdd:PRK01156 336 KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE-------EYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1095 SKIEDEQAVEIQLQKKIKELQARIEEleeeieaerasrskaekqrsdLSRELEEISERLEEAGGATSAQVelnkkreaef 1174
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRA---------------------LRENLDELSRNMEMLNGQSVCPV---------- 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1175 qkLRRDLEEATLQHeamaaaLRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKM--------EIDDLSSNAEVISKAKG 1246
Cdd:PRK01156 458 --CGTTLGEEKSNH------IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKrkeyleseEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1247 NLEKmcrsLEDQVSELKTKEEEQQRLINDLTAQRAH-LQTEAGEYSRLLDEKDAL-VSQLSRRKQASTQQIEELKHQLEE 1324
Cdd:PRK01156 530 DLED----IKIKINELKDKHDKYEEIKNRYKSLKLEdLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1325 ET----KAKNALAHALQSSRHDGDLLREQYEEEQEGKA---ELQRALSKANSEVAQW--RTKYETDAIQRTEELEEAKKK 1395
Cdd:PRK01156 606 IEigfpDDKSYIDKSIREIENEANNLNNKYNEIQENKIlieKLRGKIDNYKKQIAEIdsIIPDLKEITSRINDIEDNLKK 685
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1396 LAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSN---AACAALDKKQRNFDK 1454
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKkikKAIGDLKRLREAFDK 747
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1030-1716 |
4.91e-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: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1030 LEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLklaqESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQK 1109
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1110 KIKELqarieeleeeieaerasRSKAE---KQRSDLSRELEEISERLEEAGGATSA-QVELNKKREAEFQKlrrdlEEAT 1185
Cdd:COG3096 593 RIKEL-----------------AARAPawlAAQDALERLREQSGEALADSQEVTAAmQQLLEREREATVER-----DELA 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1186 LQHEAMAAALRKKHADSMAELAEqidnLQRVKQKLekeKSELKMEI-DDLS-SNAEVISKAKGNLEkmcrsledqvselk 1263
Cdd:COG3096 651 ARKQALESQIERLSQPGGAEDPR----LLALAERL---GGVLLSEIyDDVTlEDAPYFSALYGPAR-------------- 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1264 tkeeeQQRLINDLTAQRAHLQT----------------EAGEYSRLLDE-KDALVSQLSRR--------------KQAST 1312
Cdd:COG3096 710 -----HAIVVPDLSAVKEQLAGledcpedlyliegdpdSFDDSVFDAEElEDAVVVKLSDRqwrysrfpevplfgRAARE 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1313 QQIEELKHQLEE--ETKAKNA--------LAHALQS--SRHDGDLLREQYEEE----QEGKAELQRALSKANSEVAQWRT 1376
Cdd:COG3096 785 KRLEELRAERDElaEQYAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQ 864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1377 KY---------------------ETDAIQRTEELEEAkkklAQRLQEAEEHVEAVNAKCASLEKTKQRLQN---EVEDLM 1432
Cdd:COG3096 865 QLdqlkeqlqllnkllpqanllaDETLADRLEELREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQ 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1433 LDVERSNAACAALdkKQRNFdkVLSEWKQK-----YEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKN 1507
Cdd:COG3096 941 ADYLQAKEQQRRL--KQQIF--ALSEVVQRrphfsYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1508 LQQEISDLTEQIAEGGKQIHELEKikkqvEQEKCEIQAALEEAEASLEHEEgkilRIQLELNQV---KSEVDRKIAEKDE 1584
Cdd:COG3096 1017 YNQVLASLKSSRDAKQQTLQELEQ-----ELEELGVQADAEAEERARIRRD----ELHEELSQNrsrRSQLEKQLTRCEA 1087
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1585 EIDQLKRNHTRV---VETMQSTLDAEIRSRNDALRVKKK--MEGDLNEMEIQLNHANRLAA---ESLRNYRNTQGILKet 1656
Cdd:COG3096 1088 EMDSLQKRLRKAerdYKQEREQVVQAKAGWCAVLRLARDndVERRLHRRELAYLSADELRSmsdKALGALRLAVADNE-- 1165
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1657 qlHLDDALQGQEDLKEQLAIV-----------ER-----------RANLLQAEIEELRATLEQTERsrkiaEQELLDASE 1714
Cdd:COG3096 1166 --HLRDALRLSEDPRRPERKVqfyiavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSR-----EQKLAISSE 1238
|
..
gi 1331883584 1715 RV 1716
Cdd:COG3096 1239 SV 1240
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
843-1059 |
5.35e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 843 LKSAETEKEMATMKEDFQKTKDELAKSEAKRKELeekmvtllKEKN---DLQLQVQSEADSLADAEERCEQLIKNKIQLE 919
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEF--------RQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 920 AKIKEVTERAEEEEEINAELTAkkrklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiaklsk 997
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL--------- 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 998 eKKALQETHQQTLDDLQAEedkVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1059
Cdd:COG3206 304 -RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1194-1936 |
5.83e-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: 48.50 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1194 ALRKKHAD--SMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQR 1271
Cdd:TIGR00606 170 ALKQKFDEifSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1272 LINDLTAQRAHLqteageySRLLDEKDALVSQLSRRKQastqqIEELKHQLEEE-TKAKNALAHALQSSRHDGDLLREQY 1350
Cdd:TIGR00606 250 LKNRLKEIEHNL-------SKIMKLDNEIKALKSRKKQ-----MEKDNSELELKmEKVFQGTDEQLNDLYHNHQRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1351 EEEqegKAELQRALSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEkTKQRLQNEVED 1430
Cdd:TIGR00606 318 ERE---LVDCQRELEKLNKERRLLN--------QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLA-TRLELDGFERG 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1431 LMLDVERSNA---ACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKN 1507
Cdd:TIGR00606 386 PFSERQIKNFhtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1508 LQQEISDLTEQIAEGGKQIHELEKIKKQVEQEkceiqaALEEAEASLEHEEGKILRIQLELNQVKSEVD----------- 1576
Cdd:TIGR00606 466 LEGSSDRILELDQELRKAERELSKAEKNSLTE------TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttrtqmem 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1577 --RKIAEKDEEIDQLKRNHTRVVeTMQSTLDAEIRSRNDALRVKKKmegDLNEMEIQLNHANRLAAESLRN---YRNTQG 1651
Cdd:TIGR00606 540 ltKDKMDKDEQIRKIKSRHSDEL-TSLLGYFPNKKQLEDWLHSKSK---EINQTRDRLAKLNKELASLEQNknhINNELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1652 ILKETQLHLDDAL---QGQEDLKEQLaiverraNLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLIN 1728
Cdd:TIGR00606 616 SKEEQLSSYEDKLfdvCGSQDEESDL-------ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQ 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1729 TKKKLENDVSQLQ-------TEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD 1801
Cdd:TIGR00606 689 TEAELQEFISDLQsklrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1802 EAEQL-----ALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHErrvKELTYQteEDRKNVLRLQDLVDKLQA 1876
Cdd:TIGR00606 769 EQETLlgtimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD---LDRTVQ--QVNQEKQEKQHELDTVVS 843
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1877 KVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVSA 1936
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIRE 903
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
844-1413 |
5.84e-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: 48.30 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 844 KSAETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEadsLADAEERCEQLIKNKIQLEAKIK 923
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE---LENLEERLKALTGKHQDVTAKYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 924 EVTERAEEEEeinaeltakKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK--------NLTEEMAGLDEIIAKL 995
Cdd:pfam12128 379 RRRSKIKEQN---------NRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELReqleagklEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 996 skekKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEND 1075
Cdd:pfam12128 450 ----KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1076 KQQLDEK-------LKKKEFEISNLISKIEDEQ-----------------------AVEIQLQK--------KIKELQAR 1117
Cdd:pfam12128 526 ELQLFPQagtllhfLRKEAPDWEQSIGKVISPEllhrtdldpevwdgsvggelnlyGVKLDLKRidvpewaaSEEELRER 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1118 IEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAgGATSAQVELNKKR-EAEFQKLRRDLEEATLQH-------- 1188
Cdd:pfam12128 606 LDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA-RTALKNARLDLRRlFDEKQSEKDKKNKALAERkdsanerl 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1189 ---EAMAAALRKKHADSMAELAEQI-------------------DNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKG 1246
Cdd:pfam12128 685 nslEAQLKQLDKKHQAWLEEQKEQKreartekqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDLASLG 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1247 NLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQteageySRLLDEKDALVSQLSRRKQAstqqIEELKHQL---E 1323
Cdd:pfam12128 765 VDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQ------ETWLQRRPRLATQLSNIERA----ISELQQQLarlI 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1324 EETKAKNAlahALQSSRHDGDLLREQYEEEQEGKAELQRALSK----ANSEVAQWRTKYETDAIqrtEELEEAKKKLAQR 1399
Cdd:pfam12128 835 ADTKLRRA---KLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedANSEQAQGSIGERLAQL---EDLKLKRDYLSES 908
|
650
....*....|....
gi 1331883584 1400 LQEAEEHVEAVNAK 1413
Cdd:pfam12128 909 VKKYVEHFKNVIAD 922
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1533-1789 |
6.12e-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: 47.45 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1533 KKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVksevDRKIAEKDEEIDQLkrnhtrvvETMQSTLDAEIRsrn 1612
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRAL--------EQELAALEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1613 dalrvkkKMEGDLNEMEIQLNHANRLAAESLRN-YRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQaEIEEL 1691
Cdd:COG4942 87 -------ELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1692 RATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAItDAAMMAEE 1771
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI-ARLEAEAA 237
|
250
....*....|....*...
gi 1331883584 1772 LKKEQDTSAHLERMKKNL 1789
Cdd:COG4942 238 AAAERTPAAGFAALKGKL 255
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1389-1764 |
6.59e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1389 LEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERsnaacaaldkkqrnfdkvLSEWKQKYEETQA 1468
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE------------------LKEELRQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1469 ELEASQKESRSLSTELFKVKNAYeesLDQLETLRRENKNLQQEISDLTEQIAEggkQIHELEKIKKQVEQ---EKCEIQA 1545
Cdd:pfam07888 98 ELEEKYKELSASSEELSEEKDAL---LAQRAAHEARIRELEEDIKTLTQRVLE---RETELERMKERAKKagaQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1546 ALEEAEASLEHEEGKILRIQLELNQVKSEvdrkIAEKDEEIDQLKRNHTRVVETMQST---------LDAEIRSRNDALR 1616
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNS----LAQRDTQVLQLQDTITTLTQKLTTAhrkeaeneaLLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1617 VKKK----MEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDA----LQGQEDLKEQLAIVERRANLLQAEI 1688
Cdd:pfam07888 248 ASERkvegLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGrarwAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1689 EELRATLEQTERSRKIAEQEL--------LDASERVQLLHTQNTSLINTKKKLEndvsQLQTEVEEVIQESRNAEEKAKK 1760
Cdd:pfam07888 328 QRLEERLQEERMEREKLEVELgrekdcnrVQLSESRRELQELKASLRVAQKEKE----QLQAEKQELLEYIRQLEQRLET 403
|
....
gi 1331883584 1761 AITD 1764
Cdd:pfam07888 404 VADA 407
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1480-1707 |
6.96e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1480 LSTELFKVKNAYE---ESLDQLETLRRENKNLQQEISDLTEQIAEGGK---QIHELEKIKKQVEQ----EKceIQAALEE 1549
Cdd:COG0497 153 LEELLEEYREAYRawrALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEEEELEEERRRlsnaEK--LREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1550 AEASLEHEEGKILRIqleLNQVKSEVDRkIAEKDEEIDQLkrnhtrvVETMQSTLD------AEIRSRNDALrvkkkmEG 1623
Cdd:COG0497 231 ALEALSGGEGGALDL---LGQALRALER-LAEYDPSLAEL-------AERLESALIeleeaaSELRRYLDSL------EF 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1624 D---LNEMEIQLNHANRLAaeslRNYRNTqgilketqlhLDDALQGQEDLKEQLAIVERRANL---LQAEIEELRATLEQ 1697
Cdd:COG0497 294 DperLEEVEERLALLRRLA----RKYGVT----------VEELLAYAEELRAELAELENSDERleeLEAELAEAEAELLE 359
|
250
....*....|....*
gi 1331883584 1698 -----TERSRKIAEQ 1707
Cdd:COG0497 360 aaeklSAARKKAAKK 374
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1283-1805 |
7.35e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.72 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1283 LQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEeetKAKNALAHAlqssRHDGDLLREQYEEEQEGKAELQR 1362
Cdd:pfam05701 47 VQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE---RAQTEEAQA----KQDSELAKLRVEEMEQGIADEAS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1363 ALSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLAQRLQE---AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERS 1438
Cdd:pfam05701 120 VAAKAQLEVAKARhAAAVAELKSVKEELESLRKEYASLVSErdiAIKRAEEAVSASKEIEKTVEELTIELIATKESLESA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1439 NAACaaLDKKQRNFDKVLSeWKQKYEETQAELEASQKESRSLSTELFKVKNAYEEsldqLETLRRENKNLQQEISDLTE- 1517
Cdd:pfam05701 200 HAAH--LEAEEHRIGAALA-REQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSK----LETASALLLDLKAELAAYMEs 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1518 QIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEH--EEGKILRIQLElnQVKSEVDRKIAEKDEeidqlkrnhTR 1595
Cdd:pfam05701 273 KLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKakDEVNCLRVAAA--SLRSELEKEKAELAS---------LR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1596 VVETMQST----LDAEIRSRNDALRVKKKMEGDLNEMEI----QLNHANRLAAESLRNYRNTQGILKETQLHLDDAlqgq 1667
Cdd:pfam05701 342 QREGMASIavssLEAELNRTKSEIALVQAKEKEAREKMVelpkQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQA---- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1668 edlKEQLAIVERRANLLQAEIEELRAtleqterSRKIAeqelLDASErvQLLHTQNTSLINTKKKLENDVSQLQTEVEEV 1747
Cdd:pfam05701 418 ---KAAASTVESRLEAVLKEIEAAKA-------SEKLA----LAAIK--ALQESESSAESTNQEDSPRGVTLSLEEYYEL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1748 IQESRNAEEKAKKAITDAAMMAEELKKEQDTS-AHLERMKKNLEQTVKDLQHRLDEAEQ 1805
Cdd:pfam05701 482 SKRAHEAEELANKRVAEAVSQIEEAKESELRSlEKLEEVNREMEERKEALKIALEKAEK 540
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1457-1913 |
7.59e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1457 SEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEisdlTEQIAEGGKQIHELEKIKKQV 1536
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1537 EQEKCEIQAALEEAEAslehEEGKILRIQLELNQVKSEVdrKIAEKDEEIDQLKRNHTRVVETMQSTLdaeiRSRNDALR 1616
Cdd:TIGR00618 259 QQLLKQLRARIEELRA----QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKM----RSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1617 VKKKMEGDLNEMEIQLNHANRLAAESLRNYR--NTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELR-- 1692
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDahEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQre 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1693 ----ATLEQTERSRKI------AEQELLDASERVQLLHTQNTSLINTKKKLE-NDVSQLQTEVEEVIQESRNAEEKAKKA 1761
Cdd:TIGR00618 409 qatiDTRTSAFRDLQGqlahakKQQELQQRYAELCAAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1762 ITDAAMMAEELKKEQdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNA---- 1837
Cdd:TIGR00618 489 KAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAslke 563
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1838 ---EAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERA 1913
Cdd:TIGR00618 564 qmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1756-1928 |
7.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1756 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggkKQIQKLEARVRELEGEVENEQKR 1835
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1836 naeaVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQA-EEAEEQSNANLSKFRKLQHELEEAEERAD 1914
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 1331883584 1915 IAESQVNKLRVKSR 1928
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1375-1510 |
7.97e-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: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1375 RTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQrnfdK 1454
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1455 VLSEWKQKYEETQAELEASQKESRSLSTELFKVknayeesLDQLETLRRENKNLQQ 1510
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQV-------LDKVQEIHEDCSVLLQ 133
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
1106-1549 |
8.12e-05 |
|
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: 47.73 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1106 QLQKKIKELqarieeleeeieaerasRSKAEKQRSDLSRELEEISeRLEEAGGATSAQVELNKKREAEFQKLRRDLEEAt 1185
Cdd:pfam14817 81 ELQKEIERL-----------------RAEISRLDKQLEARELELS-REEAERERALDEISDSRHRQLLLEAYDQQCEEA- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1186 lqheamaaalRKKHADSMAELAEQIDNLQRVKQKLEKEK--SELKmeiddlSSNAEVI---SKAKGNLEKMCRSLEDQVS 1260
Cdd:pfam14817 142 ----------RKILAEDHQRLQGQLQQLRDAARKAEKEVvfGDSK------GSKSSVIalePQVLRDVREACELRAQFLQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1261 ELktkeeeqqrlindltaQRAHLQTEAGEYSRLLDEkdalvsQLSRRKQASTQQIEELKHQLeeetkAKNALAHALQ--S 1338
Cdd:pfam14817 206 EL----------------LESSLKAYEGSGIHMNRD------QRRAVIQHWLSAVETLLTSH-----PPSHLLQALEhlA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1339 SRHdgdllreqyeeeqegKAELQRALSKAN--SEVAQWRTKYETDAIQRTE-ELEEAKKKLAQRLQEAEEHVEAVNAKCA 1415
Cdd:pfam14817 259 ARE---------------KTAIQEETESLDvrADAEALRFRYESNHLLDVSsDESSDLPSVRQLLERQWAHVQQFLNELA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1416 SLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEwkqkyEETQAELEASQKESRSLSTELFKVKNAYEESL 1495
Cdd:pfam14817 324 ETRSRCQQLQARLQGLKDEAELESLGIGDTSQNDSLLRQVLEL-----ELQAAGLAASRDTLRSECQQLNKLARERQEAL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1496 DQLETlrrenknLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEE 1549
Cdd:pfam14817 399 RSLQK-------KWQRILDFRQLVSELQEQIRALIKGNSAAKAFLIRQPAEARE 445
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-1069 |
8.66e-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: 47.07 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 856 KEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEI 935
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 936 NAELTAKKRKLEDEcSELK-----KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTL 1010
Cdd:COG4942 106 LAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1011 DDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEST 1069
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1391-1805 |
1.09e-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: 47.16 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1391 EAKKKLA---QRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldversnaacaaldKKQRNFDKVLSEWKQKYEETQ 1467
Cdd:pfam06160 83 KAKKALDeieELLDDIEEDIKQILEELDELLESEEKNREEVEELK--------------DKYRELRKTLLANRFSYGPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1468 AELEASQKESRSLSTELFKVKNA--YEESLDQLETLRRENKNLQQEISDLTEQIAEGGK----QIHELEKIKKQVEQEK- 1540
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTelpdQLEELKEGYREMEEEGy 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1541 ----CEIQAALEEAEASLEHEEGKILRIQLElnqvksEVDRKIAEKDEEIDQLkrnhtrvvetmQSTLDAEIRSRNDALR 1616
Cdd:pfam06160 229 alehLNVDKEIQQLEEQLEENLALLENLELD------EAEEALEEIEERIDQL-----------YDLLEKEVDAKKYVEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1617 VKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTqgilketqlhlDDALQGQEDLKEQLAIVERRANLLQAEIEELRATle 1696
Cdd:pfam06160 292 NLPEIEDYLEHAEEQNKELKEELERVQQSYTLN-----------ENELERVRGLEKQLEELEKRYDEIVERLEEKEVA-- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1697 qtersRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKK------------AITD 1764
Cdd:pfam06160 359 -----YSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKsnlpglpesyldYFFD 433
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1331883584 1765 AAMMAEELKKEqdtsahLERMKKNLEQtvkdLQHRLDEAEQ 1805
Cdd:pfam06160 434 VSDEIEDLADE------LNEVPLNMDE----VNRLLDEAQD 464
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
977-1300 |
1.10e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.45 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 977 KVKNLTEEMAGLDEIIA----KLSKEKKALQETHQQTLDDLQaeeDKVNILTKAKTKLEQQVDdlegsleqekKLRMDLE 1052
Cdd:pfam00038 19 KVRFLEQQNKLLETKISelrqKKGAEPSRLYSLYEKEIEDLR---RQLDTLTVERARLQLELD----------NLRLAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1053 RAKRKLEGDLKLAQESTMDIENDKQQLDEK-LKKKEFEisnliSKIEDEQAvEIQLQKKIKElqarieeleeeieaeras 1131
Cdd:pfam00038 86 DFRQKYEDELNLRTSAENDLVGLRKDLDEAtLARVDLE-----AKIESLKE-ELAFLKKNHE------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1132 rskaekqrsdlsrelEEISErLEEAGGATSAQVELNKKREAEfqkLRRDLEEATLQHEAMAAALRK--------KHADSM 1203
Cdd:pfam00038 142 ---------------EEVRE-LQAQVSDTQVNVEMDAARKLD---LTSALAEIRAQYEEIAAKNREeaeewyqsKLEELQ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1204 AELAEQIDNLQRVKQklekEKSELKMEIDDLSSNAEviskakgNLEKMCRSLEDQVSELKTKEEEQ----QRLINDLTAQ 1279
Cdd:pfam00038 203 QAAARNGDALRSAKE----EITELRRTIQSLEIELQ-------SLKKQKASLERQLAETEERYELQladyQELISELEAE 271
|
330 340
....*....|....*....|....*
gi 1331883584 1280 ----RAHLQTEAGEYSRLLDEKDAL 1300
Cdd:pfam00038 272 lqetRQEMARQLREYQELLNVKLAL 296
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
977-1235 |
1.12e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 977 KVKNLTEEMAGLDEIIaKLSKEKKALQETHQQTLDDLQAE--EDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLEra 1054
Cdd:PHA02562 175 KIRELNQQIQTLDMKI-DHIQQQIKTYNKNIEEQRKKNGEniARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1055 krKLEGDLKLAQESTMDIENDKQQL--DEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQarieeleeeieaerasr 1132
Cdd:PHA02562 252 --DPSAALNKLNTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ----------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1133 skaeKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEAtLQHEAMAAALRKKHADSMAELAEQIDN 1212
Cdd:PHA02562 313 ----HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250 260
....*....|....*....|...
gi 1331883584 1213 LQrvkqKLEKEKSELKMEIDDLS 1235
Cdd:PHA02562 388 LD----KIVKTKSELVKEKYHRG 406
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1135-1865 |
1.18e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1135 AEKQR-SDLSRELEEISER---LEEAGGATSAQveLNKKREAEFQ--KLRR---DLEEATLQHEAMAAALrkkhadsmAE 1205
Cdd:COG3096 303 EEQYRlVEMARELEELSAResdLEQDYQAASDH--LNLVQTALRQqeKIERyqeDLEELTERLEEQEEVV--------EE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1206 LAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVIS----------KAKGNLEKMCR-------SLEDQVSELKTKEEE 1268
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQtraiqyqqavQALEKARALCGlpdltpeNAEDYLAAFRAKEQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1269 QQRLINDL-----TAQRAHLQTE---------AGEYSR---------LLDEKDALVSQLSRRKQASTQ--QIEELKHQLE 1323
Cdd:COG3096 453 ATEEVLELeqklsVADAARRQFEkayelvckiAGEVERsqawqtareLLRRYRSQQALAQRLQQLRAQlaELEQRLRQQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1324 EETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQR---- 1399
Cdd:COG3096 533 NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELR--------QQLEQLRARIKELAARapaw 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1400 --LQEAEEHV-EAVNAKCASLEKTKQRLQNEVEDLM-LDVERSNAACA--ALDKKQRN-------FDKVLSEWKQK---- 1462
Cdd:COG3096 605 laAQDALERLrEQSGEALADSQEVTAAMQQLLEREReATVERDELAARkqALESQIERlsqpggaEDPRLLALAERlggv 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1463 -----YE----ETQAELEASQKESRS------LSTELFKVK----------------NAYEESLDQLETLR--------- 1502
Cdd:COG3096 685 llseiYDdvtlEDAPYFSALYGPARHaivvpdLSAVKEQLAgledcpedlyliegdpDSFDDSVFDAEELEdavvvklsd 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1503 ------------------RENK--NLQQEISDLTEQIAEGGKQIHELEKIKKQVEQ----------------EKCEIQAA 1546
Cdd:COG3096 765 rqwrysrfpevplfgraaREKRleELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQR 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1547 LEEAEASLEHEEGKILRIQLELNQVKsevdrkiaekdEEIDQLKrnhtRVVETMQSTLDAEIRSRNDALRVK-KKMEGDL 1625
Cdd:COG3096 845 RSELERELAQHRAQEQQLRQQLDQLK-----------EQLQLLN----KLLPQANLLADETLADRLEELREElDAAQEAQ 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1626 NEMEIQLNHANRLaAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQL----AIVERRANLLQAE-----------IEE 1690
Cdd:COG3096 910 AFIQQHGKALAQL-EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalsEVVQRRPHFSYEDavgllgensdlNEK 988
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1691 LRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEV-IQESRNAEEKAKkaitdaamma 1769
Cdd:COG3096 989 LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgVQADAEAEERAR---------- 1058
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1770 eELKKEQDTSAHLERMKKNleQTVKDLQHRLDEAEQLAlkggkKQIQKLEARVRELEGEVENeQKRNAEAVKGLRKH--- 1846
Cdd:COG3096 1059 -IRRDELHEELSQNRSRRS--QLEKQLTRCEAEMDSLQ-----KRLRKAERDYKQEREQVVQ-AKAGWCAVLRLARDndv 1129
|
890 900
....*....|....*....|.
gi 1331883584 1847 ERRV--KELTYQTEEDRKNVL 1865
Cdd:COG3096 1130 ERRLhrRELAYLSADELRSMS 1150
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1190-1405 |
1.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1190 AMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSsnaEVISKAKGNLEKmcrsLEDQVSELKTKEEEQ 1269
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDK----LQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1270 QRLINDLTAQRAHLQTEAGEYSRLLDEKD--ALVSQLSRRKQASTQQ---IEELKHQLEEETKAKNALAHALQSsrhdgd 1344
Cdd:COG3883 85 REELGERARALYRSGGSVSYLDVLLGSESfsDFLDRLSALSKIADADadlLEELKADKAELEAKKAELEAKLAE------ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 1345 lLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEE 1405
Cdd:COG3883 159 -LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1381-1675 |
1.34e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1381 DAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNevedlmldversnaACAALDKKQRNFDKVLSEWK 1460
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ--------------APAKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1461 QKYEETQAELEASQKESR--SLSTELFKVKNAYEESLDQLETLRRENKNLQQEISdlteqiaEGGKQIHELEKIKKQVEQ 1538
Cdd:PRK11281 112 EETRETLSTLSLRQLESRlaQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALY-------ANSQRLQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1539 EKCEI---QAALEEAEASLeheegkiLRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDAL 1615
Cdd:PRK11281 185 GGKALrpsQRVLLQAEQAL-------LNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1616 RvKKKMEGDLNEMEIQLNHANRL-AAESLRNYRNTQGILKETQL-------------HLDDALQGQEDLKEQLA 1675
Cdd:PRK11281 258 S-EKTVQEAQSQDEAARIQANPLvAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQIS 330
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1208-1638 |
1.36e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1208 EQIDNLQRVKQKLEkeksELKMEIDDLssnAEVISKAKGNLEKMCRSLEDQVSELKTK---EEEQQRLiNDLTAQRAHLQ 1284
Cdd:PRK11281 70 ALLDKIDRQKEETE----QLKQQLAQA---PAKLRQAQAELEALKDDNDEETRETLSTlslRQLESRL-AQTLDQLQNAQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1285 TEAGEYSRLLdekdalVSQLSR--RKQAST----QQIEELKHQLEEETKAKNALAHALQssrhdgdllrEQYEEEQ---E 1355
Cdd:PRK11281 142 NDLAEYNSQL------VSLQTQpeRAQAALyansQRLQQIRNLLKGGKVGGKALRPSQR----------VLLQAEQallN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1356 GKAELQRALSKANS---EVAQWRTKYETDAIQRTEeleeakkKLAQRLQEAeehveaVNAKCASL-EKTKQRLQNevedl 1431
Cdd:PRK11281 206 AQNDLQRKSLEGNTqlqDLLQKQRDYLTARIQRLE-------HQLQLLQEA------INSKRLTLsEKTVQEAQS----- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1432 mldVERSNAACA-ALDKKQRNFDKVLSewkqkyeetQAELEASQKeSRSLSTELFKVKNayeesldQLETLRRENKNL-- 1508
Cdd:PRK11281 268 ---QDEAARIQAnPLVAQELEINLQLS---------QRLLKATEK-LNTLTQQNLRVKN-------WLDRLTQSERNIke 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1509 ----------------QQ--------EISDLTEQIAEggkqihelekikkqveqekceiqaaleeaeasleheegkiLRI 1564
Cdd:PRK11281 328 qisvlkgslllsrilyQQqqalpsadLIEGLADRIAD----------------------------------------LRL 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1565 -QLELNQVKSevdrKIAEKDEEIDQLKRNHTRVVEtmqstlDAEIRSRNDALRVKKKMEGDLN-EMEIQLNHANRL 1638
Cdd:PRK11281 368 eQFEINQQRD----ALFQPDAYIDKLEAGHKSEVT------DEVRDALLQLLDERRELLDQLNkQLNNQLNLAINL 433
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1498-1937 |
1.43e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.82 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1498 LETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAAL--------EEAEASLEHEEGKILRIQLELN 1569
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1570 QVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNT 1649
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1650 QGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1729
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1730 KKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALK 1809
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1810 GGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAE 1889
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1331883584 1890 EQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1256-1483 |
1.44e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1256 EDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHA 1335
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1336 LQ-------------SSRHDGDLLreqyeeeqeGKAELQRALSKANSEVAQwrtkyetDAIQRTEELEEAKKKLAQRLQE 1402
Cdd:COG3883 95 LYrsggsvsyldvllGSESFSDFL---------DRLSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1403 AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLST 1482
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
.
gi 1331883584 1483 E 1483
Cdd:COG3883 239 A 239
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1344-1536 |
1.47e-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: 46.96 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1344 DLLREQYEEEQE-GKAELQR---ALSKAnsevaqwRTKYETDaIQRTEE----LEEAKKKLAQRLQEAEEHVEAVNAKCa 1415
Cdd:pfam10168 542 QVFREEYLKKHDlAREEIQKrvkLLKLQ-------KEQQLQE-LQSLEEerksLSERAEKLAEKYEEIKDKQEKLMRRC- 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1416 slEKTKQRLqNEVEDLMLDVERSNAA-CAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRslstelfkvKNAYEES 1494
Cdd:pfam10168 613 --KKVLQRL-NSQLPVLSDAEREMKKeLETINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRK---------KSSLSLS 680
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1331883584 1495 LDQLETLRrenKNLQQEisdlTEQIAEggkQIHELEKIKKQV 1536
Cdd:pfam10168 681 EKQRKTIK---EILKQL----GSEIDE---LIKQVKDINKHV 712
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1685-1912 |
1.47e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1685 QAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLENDVSQLQtEVEEVIQESRNAEEKAKKAITD 1764
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1765 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-DEAEQLalkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGL 1843
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1844 RKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVksykrQAEEAEEQSNANLSKFRKLQHELEEAEER 1912
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1107-1858 |
1.65e-04 |
|
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: 46.74 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1107 LQKKIKELQARIEE-LEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKL-------- 1177
Cdd:pfam10174 1 LQAQLRDLQRENELlRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLqltiqalq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1178 -----RRDLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMC 1252
Cdd:pfam10174 81 delraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1253 RSLED--QVSELKTKEEEQQrliNDLTAQRAHLQTEAGEYSRLLDEKD----ALVSQLSRRKQAST--------QQIEEL 1318
Cdd:pfam10174 161 KKLLEmlQSKGLPKKSGEED---WERTRRIAEAEMQLGHLEVLLDQKEkeniHLREELHRRNQLQPdpaktkalQTVIEM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1319 K-----------HQLEEEtkaknalahaLQSSRHDGDLLREQYEEE--------------QEGKAELQRALSKANSEVAQ 1373
Cdd:pfam10174 238 KdtkisslerniRDLEDE----------VQMLKTNGLLHTEDREEEikqmevykshskfmKNKIDQLKQELSKKESELLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1374 WRTKYETdaiqrteeleeakkkLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDversnaacaaLDKKQRNFD 1453
Cdd:pfam10174 308 LQTKLET---------------LTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLR----------LEEKESFLN 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1454 KvlsewKQKYeetqaeLEASQKESRSLSTELFKVKnayeeslDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIK 1533
Cdd:pfam10174 363 K-----KTKQ------LQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1534 KQVEQEKCEIQAALEEAEASLEHEEGKILRIqlelnqvKSEVDRKIAEKDEEIDQLKRN-----------HTRVVETMQS 1602
Cdd:pfam10174 425 KSLQTDSSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKESS 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1603 TLDAEIRSRNDALRVKKKmEGDLNEMEIQLNhanrlaaESLRNYRNTQGILKETQlHLDDALQGQEDLKEQLAIVERR-- 1680
Cdd:pfam10174 498 LIDLKEHASSLASSGLKK-DSKLKSLEIAVE-------QKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEva 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1681 -----ANLLQAEIEELRATLEQTE-----RSRKIAEQElldaSERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQE 1750
Cdd:pfam10174 569 rykeeSGKAQAEVERLLGILREVEnekndKDKKIAELE----SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRR 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1751 SRNAEEKAKKAITDAAMMA-EELKKEQD-TSAHLERMKKNLEQTVKDLQH-RLDEAEQLALKGGKKQiQKLEARVRELEG 1827
Cdd:pfam10174 645 EDNLADNSQQLQLEELMGAlEKTRQELDaTKARLSSTQQSLAEKDGHLTNlRAERRKQLEEILEMKQ-EALLAAISEKDA 723
|
810 820 830
....*....|....*....|....*....|....*...
gi 1331883584 1828 EV------ENEQKRNAEAVKGL-RKHERRVKELTYQTE 1858
Cdd:pfam10174 724 NIallelsSSKKKKTQEEVMALkREKDRLVHQLKQQTQ 761
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1224-1478 |
2.00e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.75 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1224 KSELKMEIDDLSSNAEVISKAKgnlekmcRSLEDQvselKTKEEEQQRLINDLTAQRAHLqteAGEYSRLLD-EKDALVS 1302
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQ-------NALADK----ERAEADRQRLEQEKQQQLAAI---SGSQSQLEStDQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1303 QLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQegKAELQRALSKANSEVAqwrtkyetda 1382
Cdd:NF012221 1603 NGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL--LDRVQEQLDDAKKISG---------- 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1383 iqrtEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDlmldversnaacAALDKKQRNFDKVLSEWKQK 1462
Cdd:NF012221 1671 ----KQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDD------------AKADAEKRKDDALAKQNEAQ 1734
|
250
....*....|....*.
gi 1331883584 1463 YEETQAELEASQKESR 1478
Cdd:NF012221 1735 QAESDANAAANDAQSR 1750
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1676-1917 |
2.03e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.82 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1676 IVERRANLLQAEIEELratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEViqesrnaE 1755
Cdd:COG1842 2 IFKRLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1756 EKAKKAitdaammaeeLKKEQDTSAH--LERmKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLEARVRELEGEVEN-- 1831
Cdd:COG1842 72 EKARLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELKAKKDTlk 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1832 EQKRNAEAVKGLRKHERRVkeltyQTEEDRKNVLRLQDLVDKLQAKVKSYkrqAEEAEEQSnanlskfrkLQHELEEAEE 1911
Cdd:COG1842 140 ARAKAAKAQEKVNEALSGI-----DSDDATSALERMEEKIEEMEARAEAA---AELAAGDS---------LDDELAELEA 202
|
....*.
gi 1331883584 1912 RADIAE 1917
Cdd:COG1842 203 DSEVED 208
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1148-1397 |
2.06e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1148 EISERLEEAggatsAQVELNKKR-EAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEqidnlqRVKQKLEKEKSE 1226
Cdd:PRK05035 437 EIRAIEQEK-----KKAEEAKARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALA------RVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1227 LKMEIDDLSSNAEVIS--KAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQL 1304
Cdd:PRK05035 506 IVIKAGARPDNSAVIAarEARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1305 SRRKQASTQQIEELKHQLEEET------KAKNALAHALQSSRHDG-DLLREQYEEEQEGKAELQRALSKAnsevaqwRTK 1377
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQVaevdpkKAAVAAAIARAKAKKAEqQANAEPEEPVDPRKAAVAAAIARA-------KAR 658
|
250 260
....*....|....*....|
gi 1331883584 1378 YETDAIQRTEELEEAKKKLA 1397
Cdd:PRK05035 659 KAAQQQANAEPEEAEDPKKA 678
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
856-1747 |
2.09e-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: 46.58 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 856 KEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLE--AKIKEVTERAEEEE 933
Cdd:TIGR01612 1103 KEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDdpEEIEKKIENIVTKI 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 934 EINAELTAKKRKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIiaklsKE 998
Cdd:TIGR01612 1183 DKKKNIYDEIKKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI-----KE 1257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 999 KKALQETHQQTLDDLQAEEDKVNI--------LTKAKTKLEQQVDDLEGSLE--QEKKLRMDLERAKRKLEGDLKLAQES 1068
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEMETFNIshdddkdhHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQKNLLDAQKH 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1069 TMDI-------------------------------------ENDKQQLD--EKLKKKEFEISNL---ISKIE---DEQAV 1103
Cdd:TIGR01612 1338 NSDInlylneianiynilklnkikkiidevkeytkeieennKNIKDELDksEKLIKKIKDDINLeecKSKIEstlDDKDI 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1104 EiQLQKKIKELQARIEELEEEIEAERAS--------------------------RSKAEKQRSDLSRELEEISERLEEAG 1157
Cdd:TIGR01612 1418 D-ECIKKIKELKNHILSEESNIDTYFKNadennenvlllfkniemadnksqhilKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1158 G------ATSAQVELNKKReaeFQKLRRDLEEatLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQK--LEKEKSELKM 1229
Cdd:TIGR01612 1497 GckdeadKNAKAIEKNKEL---FEQYKKDVTE--LLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKfiLEAEKSEQKI 1571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1230 E--------IDDLSSNAEVISKAKGNLEKMCRSLED---QVSELKTKeeeqqrlINDLTAQRAHLQTEAGEYSrlLDEKD 1298
Cdd:TIGR01612 1572 KeikkekfrIEDDAAKNDKSNKAAIDIQLSLENFENkflKISDIKKK-------INDCLKETESIEKKISSFS--IDSQD 1642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1299 ALVSQLSRRKQASTQQIEELKHQ---LEEETKAKNALAHALQSSRHDGDLLREQY---------EEEQEGKAELQRALSK 1366
Cdd:TIGR01612 1643 TELKENGDNLNSLQEFLESLKDQkknIEDKKKELDELDSEIEKIEIDVDQHKKNYeigiiekikEIAIANKEEIESIKEL 1722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1367 ANSEVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQEAEE-------HVEAVNAKCASLEKTKQRLQNEVEDLMLDVE 1436
Cdd:TIGR01612 1723 IEPTIENLISSFNTndlEGIDPNEKLEEYNTEIGDIYEEFIElyniiagCLETVSKEPITYDEIKNTRINAQNEFLKIIE 1802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1437 RSNAACAALDK-KQRNFDKVLSEWKQKYEETQAeleasqkesrSLSTELFKVKNAYEESLDQLETLRRE-NKNLQQEISD 1514
Cdd:TIGR01612 1803 IEKKSKSYLDDiEAKEFDRIINHFKKKLDHVND----------KFTKEYSKINEGFDDISKSIENVKNStDENLLFDILN 1872
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1515 LTEQIAEG--GKQIH----ELEKIKKQVEQEKCEIQAALEEAE-------------ASLEHEEGKILRIqLELNQVKSEV 1575
Cdd:TIGR01612 1873 KTKDAYAGiiGKKYYsykdEAEKIFINISKLANSINIQIQNNSgidlfdniniailSSLDSEKEDTLKF-IPSPEKEPEI 1951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1576 DRKIAEK-DEEIDQLKRN---HTRVVETM-----QSTLDAEIRSRNDALRV----KKKMEGDLNEMEIQLNHANRLAAES 1642
Cdd:TIGR01612 1952 YTKIRDSyDTLLDIFKKSqdlHKKEQDTLniifeNQQLYEKIQASNELKDTlsdlKYKKEKILNDVKLLLHKFDELNKLS 2031
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1643 LrNYRNTQGILKET-QLHLDDALQGQEDLKEQLAIvERRANLLQAEIEELRATLEQTERSRKIAEQELLDASErvqllht 1721
Cdd:TIGR01612 2032 C-DSQNYDTILELSkQDKIKEKIDNYEKEKEKFGI-DFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSE------- 2102
|
1050 1060
....*....|....*....|....*.
gi 1331883584 1722 QNTSLINTKKKLENDVSQLQTEVEEV 1747
Cdd:TIGR01612 2103 EKDNIIQSKKKLKELTEAFNTEIKII 2128
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1358-1537 |
2.16e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1358 AELQRALSKANSEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldve 1436
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1437 rSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD-QLETLRRENKNLQQEISDL 1515
Cdd:COG3206 261 -QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQL 339
|
170 180
....*....|....*....|..
gi 1331883584 1516 TEQIAEGGKQIHELEKIKKQVE 1537
Cdd:COG3206 340 EARLAELPELEAELRRLEREVE 361
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1464-1832 |
2.18e-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: 45.83 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1464 EETQAELEASQKESRSLSTELfkvknayEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEI 1543
Cdd:pfam19220 37 EAILRELPQAKSRLLELEALL-------AQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1544 QAAL-------EEAEASLEHEEGKILRIQLELNQVKSEV---DRKIAEKDEEIDQLKRNHTRvvetmqstLDAEIRSRNd 1613
Cdd:pfam19220 110 RIELrdktaqaEALERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGELATARERLAL--------LEQENRRLQ- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1614 alRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAiVERRAnlLQAEIEELRA 1693
Cdd:pfam19220 181 --ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHR-AERAS--LRMKLEALTA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1694 TLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEviQESRNAE-EKAKKAITD-AAMMAEE 1771
Cdd:pfam19220 256 RAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER--RTQQFQEmQRARAELEErAEMLTKA 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331883584 1772 LKkeqDTSAHLERMkknlEQTVKDLQHRLDEAEQLALKggkkQIQKLEARVRELEGEVENE 1832
Cdd:pfam19220 334 LA---AKDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
857-1087 |
2.37e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 46.30 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 857 EDFQKTKDELAKSEAKRKELEEKMVTLLKEK--NDLQLQVQSEADSLADaeerceqliknkiQLEAKIKEVTERAEEEEE 934
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEKKLESKsgNKNKMEAKAQANSQKD-------------EIFALINKEANRDARAIA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 935 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL-------DEIIAKLSKEKKALQETHQ 1007
Cdd:pfam18971 677 YTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSvkdlginPEWISKVENLNAALNEFKN 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1008 QTLDDLQAeedkvniLTKAKTKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESTMDIEN-DKQQLDEKLKK 1085
Cdd:pfam18971 757 GKNKDFSK-------VTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQK 829
|
..
gi 1331883584 1086 KE 1087
Cdd:pfam18971 830 NE 831
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1347-1708 |
2.44e-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: 45.90 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1347 REQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-AEEHVEAVNAKCASLEKTKQRLQ 1425
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1426 NEVEDLMLDVERSNAAcaALDKKQRNFDKVLSEWKQKYEETQAELEASQKE----SRSLSTELFKVKNAYEESLDQLETL 1501
Cdd:pfam09731 157 QAVKAHTDSLKEASDT--AEISREKATDSALQKAEALAEKLKEVINLAKQSeeeaAPPLLDAAPETPPKLPEHLDNVEEK 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1502 RRENKNLQQEISDLTEQIAEGGKQ-IHELEKIKKQVEQEKCEIQAAL-EEAEASLEHEEGKILRIQLELNQVKSEVDRK- 1578
Cdd:pfam09731 235 VEKAQSLAKLVDQYKELVASERIVfQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAELKKREEKHi 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1579 ---IAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDA--LRVKKKMEgdlNEMEIQLNHANRLAAESLRNYRNTQGIL 1653
Cdd:pfam09731 315 eraLEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERerEEIRESYE---EKLRTELERQAEAHEEHLKDVLVEQEIE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1654 KETQLhlddalqgQEDLKEQlaiVERRANLLQAEIEELRATLEQTER---SRKIAEQE 1708
Cdd:pfam09731 392 LQREF--------LQDIKEK---VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
863-1089 |
2.49e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 863 KDELAKSEAKRKELEEkMVTLLKEKNDLQLQVQ------SEADSL--------ADAEERCEQLIKNKIQLEAKIKEVTER 928
Cdd:PLN02939 142 KNILLLNQARLQALED-LEKILTEKEALQGKINilemrlSETDARiklaaqekIHVEILEEQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 929 AEEEEEINAELTAKKRKLEDECSELKKDIDDLELT---LAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKK----A 1001
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETeerVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYdcwwE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1002 LQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQE-----------------KKLRMDLERAKRKLEGDLKL 1064
Cdd:PLN02939 301 KVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEAnvskfssykvellqqklKLLEERLQASDHEIHSYIQL 380
|
250 260
....*....|....*....|....*
gi 1331883584 1065 AQESTMDIENDKQQLDEKLKKKEFE 1089
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1752-1917 |
2.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1752 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRL-DEAEQlALKGGKKQIQKLEARVRELEGEVE 1830
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1831 NEQKRnaeavkgLRKHERRVkeltyqtEEDRKNVLRLQDLVDKLQAKVKSyKRQAEEAEEQSNANLSKFRKLQHELEEAE 1910
Cdd:PRK12704 100 RKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELEE-LIEEQLQELERISGLTAEEAKEILLEKVE 164
|
....*....
gi 1331883584 1911 E--RADIAE 1917
Cdd:PRK12704 165 EeaRHEAAV 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1086-1314 |
2.95e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1086 KEFEISNLISKIEDEQAVEIQLQKKIKELQARIeeleeeieaerasrSKAEKQRSDLSRELEEISerLEEAGGATSAQ-V 1164
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQKNGLVD--LSEEAKLLLQQlS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1165 ELNKKREAefqkLRRDLEEAtlqhEAMAAALRKKHADSMAELAEQIDNlqRVKQKLEKEKSELKMEIDDLSSN------- 1237
Cdd:COG3206 223 ELESQLAE----ARAELAEA----EARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARytpnhpd 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1238 --------AEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQ----LS 1305
Cdd:COG3206 293 vialraqiAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELyeslLQ 372
|
....*....
gi 1331883584 1306 RRKQASTQQ 1314
Cdd:COG3206 373 RLEEARLAE 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1622-1839 |
3.00e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1622 EGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERS 1701
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1702 RKIAE---------------QELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDaa 1766
Cdd:COG3883 95 LYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1767 mmAEELKKEQdtsahlERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEA 1839
Cdd:COG3883 173 --LEAQQAEQ------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1660-1935 |
3.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1660 LDDALQGQEDLKEQLAIVER-----RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhtqntslintkkkle 1734
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLE----------------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1735 nDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQhrLDEAEQLALKggkKQ 1814
Cdd:PRK02224 245 -EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER---LEELEEERDDLLAEAG--LDDADAEAVE---AR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1815 IQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNA 1894
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1331883584 1895 NLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVS 1935
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1192-1317 |
3.32e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1192 AAALRKKHADSMAElaeQIDNLQRVKQKLEKEKSELKMEIDDLSSnaevisKAKGNLEKMCRSLEDQVSELKTKEEEQQR 1271
Cdd:COG0542 398 AAARVRMEIDSKPE---ELDELERRLEQLEIEKEALKKEQDEASF------ERLAELRDELAELEEELEALKARWEAEKE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1331883584 1272 LINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEE 1317
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1133-1338 |
3.37e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.40 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1133 SKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKL----------RRDLEEATLQHEAMAAALRKKHADS 1202
Cdd:pfam05667 236 TPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELlssfsgssttDTGLTKGSRFTHTEKLQFTNEAPAA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1203 MAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNaevISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDL------ 1276
Cdd:pfam05667 316 TSSPPTKVETEEELQQQREEELEELQEQLEDLESS---IQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYkvkkkt 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1277 --------------------TAQR-AHLQTEAGEY-SRLLDEKDALVSQLSRRKQASTQQIEELK------HQLEEETKA 1328
Cdd:pfam05667 393 ldllpdaeeniaklqalvdaSAQRlVELAGQWEKHrVPLIEEYRALKEAKSNKEDESQRKLEEIKelrekiKEVAEEAKQ 472
|
250
....*....|
gi 1331883584 1329 KNALAHALQS 1338
Cdd:pfam05667 473 KEELYKQLVA 482
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1204-1397 |
3.46e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1204 AELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRahl 1283
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1284 qteagEYSRLLDEKDAlvsqLSRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEqegKAELQRA 1363
Cdd:COG1579 90 -----EYEALQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1331883584 1364 LSKANSEVAQWRTKYETDAIQRTEELEEAKKKLA 1397
Cdd:COG1579 158 LEELEAEREELAAKIPPELLALYERIRKRKNGLA 191
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1132-1337 |
3.68e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1132 RSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREaeFQKLRRDLEEatlqheamaaalrkkhadsmaELAEQID 1211
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEE--IHKLRNEFEK---------------------ELRERRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1212 NLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQ-QRL--INDLTAQRAhlqteag 1288
Cdd:PRK12704 83 ELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELerISGLTAEEA------- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331883584 1289 eYSRLLDEkdaLVSQLSRRKQASTQQIEElKHQLEEETKAKNALAHALQ 1337
Cdd:PRK12704 156 -KEILLEK---VEEEARHEAAVLIKEIEE-EAKEEADKKAKEILAQAIQ 199
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1525-1717 |
3.89e-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: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1525 QIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVD---RKIAEKDEEIDQLKRNHTRVVETMQ 1601
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDklqAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1602 ------STLDAEIRSRNDalrvkkkmeGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLA 1675
Cdd:COG3883 97 rsggsvSYLDVLLGSESF---------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1331883584 1676 IVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1717
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1378-1620 |
3.98e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.60 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1378 YETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKcASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNfdkvls 1457
Cdd:NF012221 1529 YILDNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------ 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1458 ewkqkyEETQAELEASQKESRSLSTELFKV----------KNAYEESLDQLetlrREN------KNLQQEISDlTEQIAe 1521
Cdd:NF012221 1602 ------TNGQAQRDAILEESRAVTKELTTLaqgldaldsqATYAGESGDQW----RNPfaggllDRVQEQLDD-AKKIS- 1669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1522 gGKQIhelEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKiaeKDEEIDQLKRNHTRVVETMQ 1601
Cdd:NF012221 1670 -GKQL---ADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR---KDDALAKQNEAQQAESDANA 1742
|
250
....*....|....*....
gi 1331883584 1602 STLDAEIRSRNDALRVKKK 1620
Cdd:NF012221 1743 AANDAQSRGEQDASAAENK 1761
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1654-1924 |
4.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1654 KETQLHLDDALQGQEDL---KEQLAIVERRANLLQAEIEELratleqtERSRKIAEQELLDASERVQLLhtqNTSLINTK 1730
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1731 K--KLENDVSQLQTEVEEVIQESRNAEEKakkaitdaAMMAEELKKEQDTSahLERMKKNLE--QTVKDLQHR------- 1799
Cdd:PRK04863 349 KieRYQADLEELEERLEEQNEVVEEADEQ--------QEENEARAEAAEEE--VDELKSQLAdyQQALDVQQTraiqyqq 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1800 ----LDEAEQ------LALKGGKKQIQKLEARVRELEGEV-ENEQK-RNAEAVKglRKHE------RRV----------- 1850
Cdd:PRK04863 419 avqaLERAKQlcglpdLTADNAEDWLEEFQAKEQEATEELlSLEQKlSVAQAAH--SQFEqayqlvRKIagevsrseawd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1851 --KELTYQTEEDRKNVLRLQDLVDKLQA------KVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNK 1922
Cdd:PRK04863 497 vaRELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSE 576
|
..
gi 1331883584 1923 LR 1924
Cdd:PRK04863 577 AR 578
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1456-1773 |
4.21e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1456 LSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQ 1535
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1536 VEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR-KIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDA 1614
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1615 LRVKKKMEGDLNEMEIQLnhanRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRAT 1694
Cdd:COG4372 214 RELAEELLEAKDSLEAKL----GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 1695 LEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELK 1773
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1705-1896 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1705 AEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEViqesRNAEEKAKKAITDAAMMAEELKKE-QDTSAHLE 1783
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEiEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1784 RMKKNLEQ--TVKDLQHRLDEAEQLalkggKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTyqteedr 1861
Cdd:COG1579 77 KYEEQLGNvrNNKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1331883584 1862 knvLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANL 1896
Cdd:COG1579 145 ---AELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1453-1752 |
5.07e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1453 DKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKI 1532
Cdd:PLN02939 113 NEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1533 KKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEvdrKIAEKDeEIDQLKRNHTRVVETMQSTLDAEirsrn 1612
Cdd:PLN02939 193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAETEERVFKLE----- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1613 dalRVKKKMEGDLNEMEIQLNHANrlaAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELR 1692
Cdd:PLN02939 264 ---KERSLLDASLRELESKFIVAQ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1693 ATLEQTERSR------KIAEQELLDASERVQLLHTQNTSLIntkKKLENDVSQLQTEVEEVIQESR 1752
Cdd:PLN02939 338 ASLKEANVSKfssykvELLQQKLKLLEERLQASDHEIHSYI---QLYQESIKEFQDTLSKLKEESK 400
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1730-1929 |
5.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1730 KKKLENDVSQLQTEVEEvIQESRNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKKNL-----EQTVKDLQHRLD 1801
Cdd:COG4913 220 EPDTFEAADALVEHFDD-LERAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1802 EAEQlALKGGKKQIQKLEARVRELEGEVEN-EQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKS 1880
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1881 YKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNK-LRVKSRE 1929
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1794-1937 |
6.31e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1794 KDLQHRLDEAEQLALKggkKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELtyqteedRKNVLRLQDLVDK 1873
Cdd:COG1196 216 RELKEELKELEAELLL---LKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-------RLELEELELELEE 285
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1874 LQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
957-1367 |
6.59e-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: 44.29 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 957 IDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiiaklskekkALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDD 1036
Cdd:pfam19220 33 IEPIEAILRELPQAKSRLLELEALLAQERAAYG-----------KLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1037 LEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQA 1116
Cdd:pfam19220 102 AEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1117 RIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAggatsaqvelnkkrEAEFQKLRRDLEEA--TLQHEAMAAA 1194
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAE--------------QAERERAEAQLEEAveAHRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1195 LRKKHADSMAELAEQIDNLQRvkqklekekselkmeiDDLSSNAEVISKAKgnlekmcRSLEDQVSELKTKEEEQQRLIN 1274
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEAR----------------NQLRDRDEAIRAAE-------RRLKEASIERDTLERRLAGLEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1275 DLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQA---STQQIEELKHQLEEETKAKNALAHALQSSRHDgdlLREQYE 1351
Cdd:pfam19220 305 DLERRTQQFQEMQRARAELEERAEMLTKALAAKDAAlerAEERIASLSDRIAELTKRFEVERAALEQANRR---LKEELQ 381
|
410
....*....|....*.
gi 1331883584 1352 EEQEGKAELQRALSKA 1367
Cdd:pfam19220 382 RERAERALAQGALEIA 397
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1280-1581 |
7.15e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.62 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1280 RAHLQTEAGEYSRLLDEKD-----ALVSQLSRRKQASTQQIEELKHQLEEE--TKAKNALAHALQSSRHDGDLLREQYEE 1352
Cdd:NF033838 64 ESHLEKILSEIQKSLDKRKhtqnvALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1353 ------EQEGKAELQRALSKANSEVAQWRT----KYETDAIQRTEELEEAKKKL-----AQRLQEAEEHVEAVNAKCASL 1417
Cdd:NF033838 144 atkkveEAEKKAKDQKEEDRRNYPTNTYKTleleIAESDVEVKKAELELVKEEAkeprdEEKIKQAKAKVESKKAEATRL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1418 EKTKQrlqnevedlmlDVERsnaacaALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELF---KVKNAYEES 1494
Cdd:NF033838 224 EKIKT-----------DREK------AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPAtpdKKENDAKSS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1495 LDQL--ETLRRENKNLQQEISDLTEQIAEGGKQIHELEK---------IKKQVEQEKCEIQAALEEAEASLEHEEGKILR 1563
Cdd:NF033838 287 DSSVgeETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPR 366
|
330
....*....|....*...
gi 1331883584 1564 IQLELNQVKSEVDRKIAE 1581
Cdd:NF033838 367 NEEKIKQAKAKVESKKAE 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1743-1937 |
7.35e-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: 44.67 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1743 EVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQtVKDLQHRLDEAEQLALKGGK----KQIQKL 1818
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER---LRREREKAER-YQALLKEKREYEGYELLKEKealeRQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1819 EARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKN-VLRLQDLVDKLQAKVKSYKRQAEEAEEqsnanls 1897
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKER------- 315
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1331883584 1898 kfrklqhELEEAEERADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:TIGR02169 316 -------ELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1654-1923 |
7.36e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1654 KETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTK-KK 1732
Cdd:COG5185 261 QNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGiQN 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1733 LENDVSQLQTEVEEVIQESRnAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGK 1812
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIK-EEIENIVGEVELSKSSEELDSFKDT---IESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1813 KQIQKLEARVRELEG---EVENEQKRNAEAVKGLRKHERRVKELTYQ---------TEEDRKNVLRLQDLVDKLQAKVKS 1880
Cdd:COG5185 417 AADRQIEELQRQIEQatsSNEEVSKLLNELISELNKVMREADEESQSrleeaydeiNRSVRSKKEDLNEELTQIESRVST 496
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1331883584 1881 YKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKL 1923
Cdd:COG5185 497 LKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1254-1378 |
7.56e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1254 SLEDQVS----ELKTKEEEQQRL---INDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKHQLeeet 1326
Cdd:PRK09039 78 DLQDSVAnlraSLSAAEAERSRLqalLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL---- 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1327 kakNALAHALQSSrhdgdllrEQYEEEQEGKAE-----LQRALSKANSEVAQWRTKY 1378
Cdd:PRK09039 154 ---AALEAALDAS--------EKRDRESQAKIAdlgrrLNVALAQRVQELNRYRSEF 199
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1237-1407 |
7.82e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1237 NAEVISKAKgnlekmcrsleDQVSELKTKEEEqqrLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIE 1316
Cdd:PRK00409 500 PENIIEEAK-----------KLIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1317 ELKHQLEEEtkAKNALAHALQSSrhdGDLLREQYEEEQEGKAElqralskansevaqwrtkyetdaiQRTEELEEAKKKL 1396
Cdd:PRK00409 566 KLLEEAEKE--AQQAIKEAKKEA---DEIIKELRQLQKGGYAS------------------------VKAHELIEARKRL 616
|
170
....*....|.
gi 1331883584 1397 AQRLQEAEEHV 1407
Cdd:PRK00409 617 NKANEKKEKKK 627
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1670-1937 |
1.01e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1670 LKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKklENDVSQLQTEVEEVIQ 1749
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1750 ESRNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQiQKLEARVRELEgEV 1829
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQ-RKIQQQKVEME-QI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1830 ENEQKrNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEa 1909
Cdd:pfam17380 426 RAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE- 503
|
250 260
....*....|....*....|....*...
gi 1331883584 1910 EERADIAESQVNKLRVKSREVHTKVSAE 1937
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
865-1036 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 865 ELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKr 944
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 945 kledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKvniLT 1024
Cdd:COG1579 90 ----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---LE 162
|
170
....*....|..
gi 1331883584 1025 KAKTKLEQQVDD 1036
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1077-1243 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1077 QQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARieeleeeieaerasRSKAEKQRSDLSRELEEISERL--- 1153
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE--------------LEDLEKEIKRLELEIEEVEARIkky 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1154 EEAGGATSAQVELNK-KREAEFQKLRR-DLEEATLQHEAMAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEI 1231
Cdd:COG1579 79 EEQLGNVRNNKEYEAlQKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|..
gi 1331883584 1232 DDLSSNAEVISK 1243
Cdd:COG1579 159 EELEAEREELAA 170
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1132-1379 |
1.18e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1132 RSKAEKQRSDLSRELEEISERLEEaggatsaqvELNKKR--EAEFQKLRRDLEEATLqheamaaalrkkhadSMAELAEQ 1209
Cdd:pfam00038 70 RARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATL---------------ARVDLEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1210 IDNLQR----VKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEK----MCRSLEDQVSELKTKEEEQQRlindltAQRA 1281
Cdd:pfam00038 126 IESLKEelafLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSalaeIRAQYEEIAAKNREEAEEWYQ------SKLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1282 HLQTEAGEYSRLLDEKDALVSQLSRRKQASTQQIEELKhqleeetKAKNALAHALQSSRHDGDLLREQYeeeQEGKAELQ 1361
Cdd:pfam00038 200 ELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK-------KQKASLERQLAETEERYELQLADY---QELISELE 269
|
250
....*....|....*...
gi 1331883584 1362 RALSKANSEVAQWRTKYE 1379
Cdd:pfam00038 270 AELQETRQEMARQLREYQ 287
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1677-1916 |
1.23e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1677 VERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEviqesrnaee 1756
Cdd:pfam00038 45 PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDE---------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1757 kAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQL-------------ALKGGKKQIQKLEARVR 1823
Cdd:pfam00038 115 -ATLARVDLEAKIESLKEE------LAFLKKNHEEEVRELQAQVSDTQVNvemdaarkldltsALAEIRAQYEEIAAKNR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1824 -ELE-------GEVENEQKRNAEAVKGLRkherrvKELTyqteEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNAN 1895
Cdd:pfam00038 188 eEAEewyqsklEELQQAAARNGDALRSAK------EEIT----ELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQ 257
|
250 260
....*....|....*....|...
gi 1331883584 1896 LSKFRKLQHELEEA--EERADIA 1916
Cdd:pfam00038 258 LADYQELISELEAElqETRQEMA 280
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1437-1581 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1437 RSNAACAALDKKQRNFDKVLSEWKQKYEET--QAELEAsQKESRSLSTELFKVKNAYEESLDQLE-TLRRENKNLQQEIS 1513
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEA-KEEIHKLRNEFEKELRERRNELQKLEkRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331883584 1514 DLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEH------EEGKilriQLELNQVKSEVDRKIAE 1581
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEAK----EILLEKVEEEARHEAAV 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1609-1805 |
1.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1609 RSRNDALRVKKKMEGDLNEMEIQLnhanRLAAESLRNYRNTQGILkETQLHLDDALQGQEDLKEQLAIVERRANLLQAEI 1688
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKEL----EEAEAALEEFRQKNGLV-DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1689 EELRATLEQTE-------RSRKIAE--QELLDASERVQLLHTQNT----SLINTKKKLENDVSQLQTEVEEVIQESRNAE 1755
Cdd:COG3206 243 AALRAQLGSGPdalpellQSPVIQQlrAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1756 EKAKKAITDAAMMAEELKKEQDTSAH-------LERMKKNLEQTVKDLQHRLDEAEQ 1805
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEleaelrrLEREVEVARELYESLLQRLEEARL 379
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1149-1473 |
1.35e-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: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1149 ISERLEEAGGATSAQVELNKKREAEFQKL--RRDLEEATLQHEA---MAAALRKKHADSMAELAEQIDNLQRVKQKLEKE 1223
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAemdRQAAIYAEQERMAMERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1224 K---SELKMEIDDLSSNAEVISKAKGNLEKMCRSLEdQVSELKTKEEEQQRLINDLTAQRAHLQTEageysrlldEKDAL 1300
Cdd:pfam17380 364 RirqEEIAMEISRMRELERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAE---------QEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1301 VSQLSRRKQASTQQIEELKhqlEEEtkaknalahalQSSRHDGDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYET 1380
Cdd:pfam17380 434 QREVRRLEEERAREMERVR---LEE-----------QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1381 DAIQRTEELEEAKKKLAQRLQEAEEHVEAV----NAKCASLEKTKQRLQNE---VEDLMLDVERSNAACAALDKKQRNFD 1453
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQKAIyeeeRRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMEREREMMR 579
|
330 340
....*....|....*....|
gi 1331883584 1454 KVLSEwkqkyEETQAELEAS 1473
Cdd:pfam17380 580 QIVES-----EKARAEYEAT 594
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
846-1004 |
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 1331883584 846 AETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKiQLEAKIKev 925
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQK-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331883584 926 teraeeeeeINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLSKEKKALQE 1004
Cdd:COG1579 97 ---------EIESLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1622-1923 |
1.40e-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: 43.79 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1622 EGDLnEMEIQL--NHANRL-----AAESLRNYrntQGILKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELR-- 1692
Cdd:COG3096 322 ESDL-EQDYQAasDHLNLVqtalrQQEKIERY---QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsq 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1693 -ATLEQ---TERSRKIAEQELLDASERVQLLhTQNTSLinTKKKLENDVSQLQTEVEEVIQESRNAEEK-----AKKAIT 1763
Cdd:COG3096 398 lADYQQaldVQQTRAIQYQQAVQALEKARAL-CGLPDL--TPENAEDYLAAFRAKEQQATEEVLELEQKlsvadAARRQF 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1764 DAAM-----MAEELKKEQDTSAHLE-----RMKKNLEQTVKDLQHRLDEAEQLA---------LKGGKKQI--------- 1815
Cdd:COG3096 475 EKAYelvckIAGEVERSQAWQTAREllrryRSQQALAQRLQQLRAQLAELEQRLrqqqnaerlLEEFCQRIgqqldaaee 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1816 -----QKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKnvlrLQDLVDKLQAKVKSYKRQAEEAEE 1890
Cdd:COG3096 555 leellAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLA----AQDALERLREQSGEALADSQEVTA 630
|
330 340 350
....*....|....*....|....*....|...
gi 1331883584 1891 QSNANLSKFRKLQHELEEAEERADIAESQVNKL 1923
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1454-1658 |
1.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1454 KVLSEWKQKYEETQAEL--EASQKESRSLSTELFKVKNAYEESLDQLETLRRENK--NLQQEISDLTEQIAEGGKQIHEL 1529
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1530 EKIKKQVEQEKCEIQAALEEAEAS---------LEHEEGKILRIQLELNQVKS----------EVDRKIAEKDEEIDQLK 1590
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331883584 1591 RNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQL 1658
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
838-1203 |
1.42e-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: 43.95 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 838 KIKPLLKSAETEKEM------------ATMKEDFQKTKDELAKSEAKRKELE--EKMVTLLKEKNDLQLQ----VQSEAD 899
Cdd:pfam15921 462 KVSSLTAQLESTKEMlrkvveeltakkMTLESSERTVSDLTASLQEKERAIEatNAEITKLRSRVDLKLQelqhLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 900 SLADAEERCEQLiknKIQLEAKIKEVTERAEEEEEINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATEN 976
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKDKVIEILRQQIENMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 977 KVKNLTEEMAGLDEIIAKL----SKEKKALQETHQ---QTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQE-KKLR 1048
Cdd:pfam15921 619 KIRELEARVSDLELEKVKLvnagSERLRAVKDIKQerdQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLK 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1049 MDLERAKRKLEgdlklaqestmdiendkqQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAE 1128
Cdd:pfam15921 699 MQLKSAQSELE------------------QTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNA 760
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1129 RASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSM 1203
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
846-1029 |
1.46e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 846 AETEKEMATMKEDFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQ---------LQVQSEADSLA--DAEERCEQLIKN 914
Cdd:COG4942 58 AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeelaellraLYRLGRQPPLAllLSPEDFLDAVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 915 KIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK 994
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
170 180 190
....*....|....*....|....*....|....*
gi 1331883584 995 LSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTK 1029
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1305-1549 |
1.63e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1305 SRRKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDGDLLREQYEEEQEGKAELQ---RALSKANSEVAQWRTKYETD 1381
Cdd:pfam00038 46 SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEndlVGLRKDLDEATLARVDLEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1382 AIQRTEEL-------EEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldversnaacaaldkkQRNFDK 1454
Cdd:pfam00038 126 IESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIA----------------AKNREE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1455 VLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTE----QIAEGGKQIHELE 1530
Cdd:pfam00038 190 AEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEEryelQLADYQELISELE 269
|
250
....*....|....*....
gi 1331883584 1531 kikKQVEQEKCEIQAALEE 1549
Cdd:pfam00038 270 ---AELQETRQEMARQLRE 285
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1387-1756 |
1.77e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1387 EELEEAKKKLAQ-RLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEE 1465
Cdd:PRK04778 86 EQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1466 TQAELEasqKESRSLSTELFKVKNA-----YEESLDQLETLRRENKNLQQEISDLTEQIAEGGK----QIHELE------ 1530
Cdd:PRK04778 166 ALDELE---KQLENLEEEFSQFVELtesgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTelpdQLQELKagyrel 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1531 ----------KIKKQVEQEKCEIQAALEE-AEASLEHEEGKILRIQLELNQVKSEVDRKIAEK---DEEIDQLKRNHTRV 1596
Cdd:PRK04778 243 veegyhldhlDIEKEIQDLKEQIDENLALlEELDLDEAEEKNEEIQERIDQLYDILEREVKARkyvEKNSDTLPDFLEHA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1597 VETMQsTLDAEIR--------SRNDALRVKKkMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQE 1668
Cdd:PRK04778 323 KEQNK-ELKEEIDrvkqsytlNESELESVRQ-LEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1669 DLKEQLA---IVERRAN-LLQAEIEELRATLEQTERSR--KIAE---QELLDASERVQLLHTQ-NTSLINTKK------K 1732
Cdd:PRK04778 401 KLSEMLQglrKDELEAReKLERYRNKLHEIKRYLEKSNlpGLPEdylEMFFEVSDEIEALAEElEEKPINMEAvnrlleE 480
|
410 420
....*....|....*....|....
gi 1331883584 1733 LENDVSQLQTEVEEVIQESRNAEE 1756
Cdd:PRK04778 481 ATEDVETLEEETEELVENATLTEQ 504
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1243-1304 |
1.88e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 1.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331883584 1243 KAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQL 1304
Cdd:pfam08614 71 RSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDL 132
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1731-1923 |
2.12e-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: 41.94 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1731 KKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAAMMAEELkkeQDTSAHLERMKKNLEQTvkdlQHRLDEAEQLA--- 1807
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRI---QLLEEELERTEERLAEA----LEKLEEAEKAAdes 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1808 ---LKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQ-------AK 1877
Cdd:pfam00261 77 ergRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEeelkvvgNN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1331883584 1878 VKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKL 1923
Cdd:pfam00261 157 LKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1577-1924 |
2.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1577 RKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKET 1656
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1657 QLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEND 1736
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1737 VSQLQTEVEEVIQEsrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQ 1816
Cdd:COG4372 166 LAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1817 KLEARVRELEGEVENEQKRNAEA-VKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNAN 1895
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340
....*....|....*....|....*....
gi 1331883584 1896 LSKFRKLQHELEEAEERADIAESQVNKLR 1924
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1756-1937 |
2.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1756 EKAKKAITdaamMAEELKKEQDTSAHLERmkKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELEGEVENEQKR 1835
Cdd:COG1196 210 EKAERYRE----LKEELKELEAELLLLKL--RELEAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1836 NAEAVKGLRKHERRVKELtyqtEEDRknvlrlqdlvDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADI 1915
Cdd:COG1196 283 LEEAQAEEYELLAELARL----EQDI----------ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180
....*....|....*....|..
gi 1331883584 1916 AESQVNKLRVKSREVHTKVSAE 1937
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEA 370
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1132-1924 |
2.86e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1132 RSKAEKQRSDLSRELEEIS--------ERLEEAggATSAQvELNKKREAEFQKLRR----DLEEATLQHEAMAAALRKKh 1199
Cdd:NF041483 446 RGEAEQLRAEAVAEGERIRgearreavQQIEEA--ARTAE-ELLTKAKADADELRStataESERVRTEAIERATTLRRQ- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1200 adsmaelAEQidNLQRVKQKLEKEKSELKMEIDDLSSNAEviSKAKGNLEKMCRSLE-------DQVSELKTKEEEQqrl 1272
Cdd:NF041483 522 -------AEE--TLERTRAEAERLRAEAEEQAEEVRAAAE--RAARELREETERAIAarqaeaaEELTRLHTEAEER--- 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1273 indLTAQRAHLQTEAGEYSRLLDEKdalVSQLSRRKQASTQQIEELKHQLEEETKAKNALAHALQS-SRHDGD-----LL 1346
Cdd:NF041483 588 ---LTAAEEALADARAEAERIRREA---AEETERLRTEAAERIRTLQAQAEQEAERLRTEAAADASaARAEGEnvavrLR 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1347 REQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiqrTEELEEAKKKLAQRLQEAEEHVEAVNAKcASLEKTKQRLQN 1426
Cdd:NF041483 662 SEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEA---AEALAAAQEEAARRRREAEETLGSARAE-ADQERERAREQS 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1427 EvedlmldversnaacaaldkkqrnfdKVLSEWKQKYEETQAELEASQKESRSLSTELfkVKNAYEESLDQLETLRRENK 1506
Cdd:NF041483 738 E--------------------------ELLASARKRVEEAQAEAQRLVEEADRRATEL--VSAAEQTAQQVRDSVAGLQE 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1507 NLQQEISDLtEQIAEggkqiHELEKIKKQVEQEKCEIQA-ALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEE 1585
Cdd:NF041483 790 QAEEEIAGL-RSAAE-----HAAERTRTEAQEEADRVRSdAYAERERASEDANRLRREAQEETEAAKALAERTVSEAIAE 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1586 IDQLKRN---HTRVVETMQStlDAEIRSRNDALRVKKKMEGDLNEMEIQL-NHANRLAAESLRNY-RNTQGILKETQLHL 1660
Cdd:NF041483 864 AERLRSDaseYAQRVRTEAS--DTLASAEQDAARTRADAREDANRIRSDAaAQADRLIGEATSEAeRLTAEARAEAERLR 941
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1661 DDALQGQEDLK-EQLAIVERRANLLQAEIEELRATLEQT--------ERSRKIAEQELLDASERVQLLHTQ--------- 1722
Cdd:NF041483 942 DEARAEAERVRaDAAAQAEQLIAEATGEAERLRAEAAETvgsaqqhaERIRTEAERVKAEAAAEAERLRTEareeadrtl 1021
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1723 NTSLINTKKKLENDVSQLQTEVEEVIQES----RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQH 1798
Cdd:NF041483 1022 DEARKDANKRRSEAAEQADTLITEAAAEAdqltAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKA 1101
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1799 RLDEAEQLAlkGGKKQIQKLEARVRELEGEVENEqkrnaeaVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKV 1878
Cdd:NF041483 1102 RTDADELLV--GARRDATAIRERAEELRDRITGE-------IEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEA 1172
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1331883584 1879 KSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLR 1924
Cdd:NF041483 1173 KAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIK 1218
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1544-1699 |
2.95e-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: 42.03 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1544 QAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKiAEKDEEIDQLKRNHTRVVETMQSTldaeirsrndalrvkkkmEG 1623
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESEL-AISRQDYDGATAQLRAAQAAVKAA------------------QA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1624 DLNEMEIQLNHANRLAAESL----------RNYRNTQGILKETQLHLDDA-LQGQEDLKEQLAIVERRANLLQAEIEELR 1692
Cdd:pfam00529 118 QLAQAQIDLARRRVLAPIGGisreslvtagALVAQAQANLLATVAQLDQIyVQITQSAAENQAEVRSELSGAQLQIAEAE 197
|
....*..
gi 1331883584 1693 ATLEQTE 1699
Cdd:pfam00529 198 AELKLAK 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1537-1766 |
3.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1537 EQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDR---KIAEKDEEIDQLKRNhtrvVETMQSTLDAEIRSRND 1613
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAE----IAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1614 ALRVKKKMEGDLNEMEIQLNhanrlaAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLaiverranllqaeiEELRA 1693
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLG------SESFSDFLDRLSALSKIADADADLLEELKADKAEL--------------EAKKA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1694 TLEQTERSRKIAEQELLDASERVQLLHTQNTSLINtkkKLENDVSQLQTEVEEVIQESRNAEEKAKKAITDAA 1766
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLA---QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1268-1539 |
3.50e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1268 EQQRLINDlTAQR------AHLQTEAGEYSRLLDEKDALVSQLSRRKQAS---TQQIEELKHQLEEETKAknalahALQS 1338
Cdd:COG0497 133 EHQSLLDP-DAQRelldafAGLEELLEEYREAYRAWRALKKELEELRADEaerARELDLLRFQLEELEAA------ALQP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1339 srhdgdllreqyEEEQEGKAELQRAlskANSEvaqwrtKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLE 1418
Cdd:COG0497 206 ------------GEEEELEEERRRL---SNAE------KLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1419 KTKQRLQN---EVEDLMLDVERsnaACAALDKKQRNFDKV---LSEW---KQKYEETQAELEASQKEsrsLSTELFKVKN 1489
Cdd:COG0497 265 ELAERLESaliELEEAASELRR---YLDSLEFDPERLEEVeerLALLrrlARKYGVTVEELLAYAEE---LRAELAELEN 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1490 AyEESLDQLEtlrrenknlqQEISDLTEQIAEGGKQIHEL-----EKIKKQVEQE 1539
Cdd:COG0497 339 S-DERLEELE----------AELAEAEAELLEAAEKLSAArkkaaKKLEKAVTAE 382
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1263-1444 |
3.67e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1263 KTKEEEQQRLINDLTAQRAHLQTEAGEYSRLLDEKDALVSQLSRRKQAS---------TQQIEELKHQLEEETKAKnALA 1333
Cdd:PRK07735 17 RAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAaakakaaalAKQKREGTEEVTEEEKAK-AKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1334 HALQSSRHDGDLLREQYEEEQEGKAELQRALSKANSeVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAK 1413
Cdd:PRK07735 96 KAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKA-AAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAK 174
|
170 180 190
....*....|....*....|....*....|.
gi 1331883584 1414 CASLEKTKQRLQNEVEDLMLDVERSNAACAA 1444
Cdd:PRK07735 175 AKAAALAKQKAAEAGEGTEEVTEEEKAKAKA 205
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1166-1404 |
3.72e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1166 LNKKREAEFQKLRR----DLEEatLQHEAMAAALRKKHADSMaELAEQIDNLQRVKQKLEKEKSEL-KMEIDDLSSNAEV 1240
Cdd:PRK05771 14 LKSYKDEVLEALHElgvvHIED--LKEELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKkKVSVKSLEELIKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1241 ISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAqrahLQTEAGEYSRLLDEK--DALVSQLSRRKQASTQQIEEL 1318
Cdd:PRK05771 91 VEEELEKIEKEIKELEEEISELENEIKELEQEIERLEP----WGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1319 KHQLEEETKAKNALAHALQSSRHDGDLLR-------------------EQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1379
Cdd:PRK05771 167 ENVEYISTDKGYVYVVVVVLKELSDEVEEelkklgferleleeegtpsELIREIKEELEEIEKERESLLEELKELAKKYL 246
|
250 260
....*....|....*....|....*
gi 1331883584 1380 TDAIQRTEELEEAKKKLAQRLQEAE 1404
Cdd:PRK05771 247 EELLALYEYLEIELERAEALSKFLK 271
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1653-1886 |
3.72e-03 |
|
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: 41.98 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1653 LKETQLHLDDALQGQEDLKEQLAIVERRANLLQAEIEELRATLEQTER---SRKIAEQELLDASERVQLLHTQNTSLINT 1729
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddSGTPGGKKYLLLQKQLEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1730 KKKLENDVSQLQTEVEEViqESRNAEekakkaITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalk 1809
Cdd:pfam05622 82 RDDYRIKCEELEKEVLEL--QHRNEE------LTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEDLGDL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1810 ggKKQIQKLEAR---VRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAE 1886
Cdd:pfam05622 151 --RRQVKLLEERnaeYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKE 228
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1308-1525 |
3.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1308 KQASTQQIEELKHQLEEETKAKNALAHALQSsrhdgdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiQRTE 1387
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1388 ELeeakKKLAQRLQEAEEHVEAVNA------------KCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKV 1455
Cdd:COG3883 87 EL----GERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1456 lsewKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQ 1525
Cdd:COG3883 163 ----KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
940-1180 |
3.78e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 940 TAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLSKEKKALQETHqqTLD-DLQAEED 1018
Cdd:PRK05771 71 PLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPWG--NFDlDLSLLLG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1019 KVNILTKAKTKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAqestMDIENDKQQLDEKLKKKEFEISNLISKIE 1098
Cdd:PRK05771 142 FKYVSVFVGTVPEDKLEELKLESDVEN-----VEYISTDKGYVYVVV----VVLKELSDEVEEELKKLGFERLELEEEGT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1099 DEQAVEiQLQKKIKELqarieeleeeieaerasrskaEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLR 1178
Cdd:PRK05771 213 PSELIR-EIKEELEEI---------------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFL 270
|
..
gi 1331883584 1179 RD 1180
Cdd:PRK05771 271 KT 272
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1082-1231 |
3.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1082 KLKKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELEEeieaerasRSKAEKQRSDLSRELEEISERLEEAGGATS 1161
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL--------RNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1162 AQVELNKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELaEQIDNLQR---VKQKLEKEKSELKMEI 1231
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLTAeeaKEILLEKVEEEARHEA 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
951-1283 |
4.36e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 951 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKL 1030
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1031 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKK 1110
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1111 IKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEA 1190
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1191 MAAALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDDLSSNAEVISKAKGNLEKMCRSLEDQVSELKTKEEEQQ 1270
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330
....*....|...
gi 1331883584 1271 RLINDLTAQRAHL 1283
Cdd:COG4372 347 LVGLLDNDVLELL 359
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1684-1767 |
4.66e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1684 LQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRnaeEKAKKAIT 1763
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK---QKRKEITD 223
|
....
gi 1331883584 1764 DAAM 1767
Cdd:PRK11448 224 QAAK 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1313-1476 |
4.76e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1313 QQIEELKHQLEEETKAKNALAHALQSsrhdgdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDaiqrTEELEEA 1392
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY----EEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1393 KKklaqrlqeaEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEA 1472
Cdd:COG1579 86 RN---------NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....
gi 1331883584 1473 SQKE 1476
Cdd:COG1579 157 ELEE 160
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1660-1926 |
4.93e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.84 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1660 LDDALQGQEDLKEQLAIVERRANLLQAEIE----------ELRATLEQTERSRK---IAEQELLdaSERVQLLHTQ---- 1722
Cdd:PLN03188 928 MDGVLSKEDFLEEELASLMHEHKLLKEKYEnhpevlrtkiELKRVQDELEHYRNfydMGEREVL--LEEIQDLRSQlqyy 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1723 -NTSLINTKK-----KLENDVSQLQTEVEEVIQES--RNAEEKAKK-------AITDAAMMAEELKKEQDTSAHL-ERMK 1786
Cdd:PLN03188 1006 iDSSLPSARKrnsllKLTYSCEPSQAPPLNTIPEStdESPEKKLEQerlrwteAESKWISLAEELRTELDASRALaEKQK 1085
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1787 KNLEqTVKDLQHRLDEAEQLALKGGKKQIQK----------LEARVRELEGEVENEQKRNAEAvkGLRKHERR-----VK 1851
Cdd:PLN03188 1086 HELD-TEKRCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKKAAARA--GVRGAESKfinalAA 1162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1852 ELTYQTEEDRKNVLRLQDLVDKLQAKVksykRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAE-------SQVNKLR 1924
Cdd:PLN03188 1163 EISALKVEREKERRYLRDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLK 1238
|
..
gi 1331883584 1925 VK 1926
Cdd:PLN03188 1239 RK 1240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1655-1931 |
4.96e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1655 ETQLHLDDALQGQEDL---KEQLAiverranLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHT---QNTSLIN 1728
Cdd:COG3096 279 ERRELSERALELRRELfgaRRQLA-------EEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalrQQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1729 TKKKLENDVSQL--QTEVEEVIQESR------------------------------------------NAEEKAKKAITD 1764
Cdd:COG3096 352 YQEDLEELTERLeeQEEVVEEAAEQLaeaearleaaeeevdslksqladyqqaldvqqtraiqyqqavQALEKARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1765 AAMMAEELKKEQdtsAHLERMKKNLEQTVKDLQHRLDEAEQlalkgGKKQIQKLEARVRELEGEVENEQKRNAeAVKGLR 1844
Cdd:COG3096 432 PDLTPENAEDYL---AAFRAKEQQATEEVLELEQKLSVADA-----ARRQFEKAYELVCKIAGEVERSQAWQT-ARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1845 KHErrvkelTYQTEEDRKNVLR--LQDLvDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNK 1922
Cdd:COG3096 503 RYR------SQQALAQRLQQLRaqLAEL-EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAE 575
|
....*....
gi 1331883584 1923 LRVKSREVH 1931
Cdd:COG3096 576 AVEQRSELR 584
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
940-1324 |
5.12e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 940 TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEd 1018
Cdd:PRK11281 47 ALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQ- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1019 kvniltkaktkLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEstmdIENdkqQLDEKLKKKE 1087
Cdd:PRK11281 126 -----------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---LLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1088 FEISNLISKIEDEQA-VEIQLQKKIKELQARIEELeeeieaerasrSKAEKQRSdlsrELEEISERLEEAggATSAQVEL 1166
Cdd:PRK11281 188 ALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQ-----------DLLQKQRD----YLTARIQRLEHQ--LQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1167 NKKREAEFQKLRRDLEEATLQHEAMAAALRKKHADSMAELAEQI------------DNLqRVKQKLEK-EKSE--LKMEI 1231
Cdd:PRK11281 251 NSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLDRlTQSErnIKEQI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1232 DDLSSN---AEVISKAKGNL--EKMCRSLEDQVSELKTKEEE--QQRliNDLTAQRAHLQT-EAGEYSRLLDE-KDALVS 1302
Cdd:PRK11281 330 SVLKGSlllSRILYQQQQALpsADLIEGLADRIADLRLEQFEinQQR--DALFQPDAYIDKlEAGHKSEVTDEvRDALLQ 407
|
410 420
....*....|....*....|..
gi 1331883584 1303 QLSRRKQASTQQIEELKHQLEE 1324
Cdd:PRK11281 408 LLDERRELLDQLNKQLNNQLNL 429
|
|
| 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 1331883584 1812 KKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKEL---TYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEA 1888
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1331883584 1889 EEQSNAnLSKFRKLQH----------------ELEEAEERADIAESQV 1920
Cdd:COG2433 492 KRKLER-LKELWKLEHsgelvpvkvvekftkeAIRRLEEEYGLKEGDV 538
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1168-1332 |
5.33e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.97 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1168 KKREAEFQKLRRDLEEATLQheAMAAALRKKHADS-MAELAEQIDNLqrvkqkleKEKSELKMEiddlssnaEVISKAKG 1246
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH--------DVVLKKTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1247 NLEKMCRSLEDQVSELktkeeeQQRLInDLTAQRAHLqteageySRLLDEKDALVSQLSRRKQASTQQIEELKHQLEEET 1326
Cdd:pfam05911 82 EWEKIKAELEAKLVET------EQELL-RAAAENDAL-------SRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCE 147
|
....*.
gi 1331883584 1327 KAKNAL 1332
Cdd:pfam05911 148 KEINSL 153
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1671-1929 |
5.76e-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: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1671 KEQLAIvERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQE 1750
Cdd:pfam17380 339 QERMAM-ERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1751 SRNAEEKAKKAitdaammAEELKKEQDTSAHLERmKKNLEQTVKDLQHRLDEAEQLalkggkkQIQKLEARVRELEGEVE 1830
Cdd:pfam17380 418 QKVEMEQIRAE-------QEEARQREVRRLEEER-AREMERVRLEEQERQQQVERL-------RQQEEERKRKKLELEKE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1831 NEQKRNAEavkglrkhERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKsyKRQAEEAEEQSNANLSKFRKLQHELEE-- 1908
Cdd:pfam17380 483 KRDRKRAE--------EQRRKILEKELEERKQAMIEEERKRKLLEKEME--ERQKAIYEEERRREAEEERRKQQEMEErr 552
|
250 260
....*....|....*....|..
gi 1331883584 1909 -AEERADIAESQVNKLRVKSRE 1929
Cdd:pfam17380 553 rIQEQMRKATEERSRLEAMERE 574
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1495-1750 |
5.85e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1495 LDQLETLRRENKNLQQEISDLTEQ---------------IAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEG 1559
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1560 K---------ILRIQL-ELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEME 1629
Cdd:pfam00038 97 LrtsaendlvGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1630 IQL-NHANRLAAESLRNYRNTQGILKETQLHLDDALQGQedlKEQLAIVERRANLLQAEIEELRATLEQTERSrkIAEQE 1708
Cdd:pfam00038 177 AQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQKASLERQ--LAETE 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1331883584 1709 lldasERVQLLHTQNTSLINtkkKLENDVSQLQTEVEEVIQE 1750
Cdd:pfam00038 252 -----ERYELQLADYQELIS---ELEAELQETRQEMARQLRE 285
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
888-1100 |
5.98e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 888 NDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEeeinaelTAKKRKLEDECSELKKDIDDLELTLAKV 967
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQA-------SRKLRETQNTLNQLNKQIDELNASIAKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 968 EKEKHATEnkvKNLTEEM---------AGLDEIiakLSKEKKALQETHQQTLDDL-QAEEDKVNILTKAKTKLEQQVDDL 1037
Cdd:PRK11637 116 EQQQAAQE---RLLAAQLdaafrqgehTGLQLI---LSGEESQRGERILAYFGYLnQARQETIAELKQTREELAAQKAEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331883584 1038 EGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIEN----DKQQLDEkLKKKEFEISNLISKIEDE 1100
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqkDQQQLSE-LRANESRLRDSIARAERE 255
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1782-1900 |
5.99e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1782 LERMKK-NLEQTVKDLQHRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVkglrkheRRVKELT 1854
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1331883584 1855 YQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEE-------AEEQSNANLSKFR 1900
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1452-1622 |
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 1331883584 1452 FDKVLSEWKQKYEETQAE--LEASQKESRSLSTElfKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIaeggkQIHEl 1529
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL-----LQKE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1530 EKIKKQVEqekceiqaALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKD---EEIDQLKRNHTR--VVETMQSTL 1604
Cdd:PRK12704 96 ENLDRKLE--------LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqelERISGLTAEEAKeiLLEKVEEEA 167
|
170
....*....|....*...
gi 1331883584 1605 DAEIrsrndALRVKKKME 1622
Cdd:PRK12704 168 RHEA-----AVLIKEIEE 180
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1676-1830 |
6.77e-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: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1676 IVERRANLLQAEIEELratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEndvsqlqTEVEEVIQESRNAE 1755
Cdd:pfam04012 1 IFKRLGRLVRANIHEG---LDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLE-------RRLEQQTEQAKKLE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331883584 1756 EKAKKAITDAAmmaEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLEARVRELEGEVE 1830
Cdd:pfam04012 71 EKAQAALTKGN---EELARE------ALAEKKSLEKQAEALETQLAQQRSAVEQL-RKQLAALETKIQQLKAKKN 135
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1443-1641 |
7.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1443 AALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQIAEg 1522
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1523 gkQIHELEKIKKQ------VEQEKC-----------EIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEE 1585
Cdd:COG4942 109 --LLRALYRLGRQpplallLSPEDFldavrrlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1586 IDQLKRNHTRVVETMQStLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAE 1641
Cdd:COG4942 187 RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1374-1922 |
7.73e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1374 WRTkYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERsnaacAALDKKQRNFD 1453
Cdd:pfam05701 26 WKA-HRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLER-----AQTEEAQAKQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1454 KVLSewKQKYEETqaELEASQKESRSLSTELFKVKNAYEESLDQLETLRRENKNLQQEISDLTEQ----IAEGGKQIHEL 1529
Cdd:pfam05701 100 SELA--KLRVEEM--EQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSErdiaIKRAEEAVSAS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1530 EKIKKQVEQEKCEIQAALEEAE----ASLEHEEGKIlRIQLELNQVKSEVDRKIAEKDEEIDQLkRNHTRVVETMQSTLD 1605
Cdd:pfam05701 176 KEIEKTVEELTIELIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1606 AeirsrNDALRVKKKMEgdLNE-MEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALQGQEDLKEQLAIVERRANLL 1684
Cdd:pfam05701 254 T-----ASALLLDLKAE--LAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1685 QAEIEELR---ATLEQTERSRKIAeqelldaservqllhtqntslintkkklendVSQLQTEVEEVIQESRNAEEKAKKA 1761
Cdd:pfam05701 327 RSELEKEKaelASLRQREGMASIA-------------------------------VSSLEAELNRTKSEIALVQAKEKEA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1762 itdAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalKGGKKQIQ-KLEARVRELEGEVENEqKRNAEAV 1840
Cdd:pfam05701 376 ---REKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQA--KAAASTVEsRLEAVLKEIEAAKASE-KLALAAI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1841 KGLRKHERRvKELTYQTEEDRKNVLRLQDLvdklqakvKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQV 1920
Cdd:pfam05701 450 KALQESESS-AESTNQEDSPRGVTLSLEEY--------YELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEV 520
|
..
gi 1331883584 1921 NK 1922
Cdd:pfam05701 521 NR 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
874-1233 |
8.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 874 KELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSEL 953
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 954 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQ 1033
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1034 VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEISNLISKIEDEQAVEIQLQKKIKE 1113
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1114 LQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMAA 1193
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1331883584 1194 ALRKKHADSMAELAEQIDNLQRVKQKLEKEKSELKMEIDD 1233
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1775-1937 |
8.37e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1775 EQDTSAHLERMKKNLEQtvkdlqhrLDEAEQLALKGgKKQIQKLEaRVRELEGEVEnEQKRNAEAVKGLR------KHER 1848
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYA-AARERLAELEYLRaalrlwFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1849 RVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQ-SNANLSKFRKLQHELEEAEERADIAESQVNKLRVKS 1927
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170
....*....|
gi 1331883584 1928 REVHTKVSAE 1937
Cdd:COG4913 369 AALGLPLPAS 378
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
963-1163 |
8.53e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 963 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLE 1042
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1043 ------QEKKLRMD-----------------------LERAKRKLEGDLKLAQEstmDIENDKQQLDEKLKKKEFEISNL 1093
Cdd:COG3883 90 eraralYRSGGSVSyldvllgsesfsdfldrlsalskIADADADLLEELKADKA---ELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1094 ISKIEDEQAVEIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQ 1163
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1489-1936 |
8.72e-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: 41.16 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1489 NAYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLEL 1568
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1569 ---NQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMqSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRN 1645
Cdd:TIGR04523 113 kndKEQKNKLEVELNKLEKQKKENKKNIDKFLTEI-KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1646 YRNTQGILKETQLHLDDALQgqedlkeqlaiverRANLLQAEIEELRATLEQTERSRKIAEQELldaSERVQLLHTQNTS 1725
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQ--------------KNKSLESQISELKKQNNQLKDNIEKKQQEI---NEKTTEISNTQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1726 LINTKKKLENDVSQLQTEVEEVIQESRNAEEKaKKAITDAAMMAEELK--KEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1803
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EKQLNQLKSEISDLNnqKEQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1804 EQlALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERR-------VKELTYQTEEDRKNVLRLQDLVDKLQA 1876
Cdd:TIGR04523 334 NK-IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1877 KVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVSA 1936
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1685-1894 |
8.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1685 QAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQTEVEEVIQESRNAEEKAKKAITD 1764
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1765 AAM------MAEELKKEQDTSAHLERMkknleQTVKDLQhrldEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAE 1838
Cdd:COG3883 95 LYRsggsvsYLDVLLGSESFSDFLDRL-----SALSKIA----DADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331883584 1839 AvkglrkhERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNA 1894
Cdd:COG3883 166 L-------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1007-1100 |
9.03e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 40.61 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1007 QQTLDDLQAEEDKVNI--------LTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQ------------ 1066
Cdd:pfam03148 232 EQTANDLRAQADAVNFalrkrieeTEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKLAQtrlenrtyrpnv 311
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1331883584 1067 ESTMD------------IENDKQQLDEKLKKKEFEISNLI---SKIEDE 1100
Cdd:pfam03148 312 ELCRDeaqyglvdevkeLEETIEALKQKLAEAEASLQALErtrLRLEED 360
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1044-1403 |
9.10e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1044 EKKLRMDLERAK-----------RKLEGDLKLAQESTMDIENDKQ-------------QLDEKLKKKEFEISNLISKI-- 1097
Cdd:PRK10929 25 EKQITQELEQAKaaktpaqaeivEALQSALNWLEERKGSLERAKQyqqvidnfpklsaELRQQLNNERDEPRSVPPNMst 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1098 -EDEQAVeIQLQKKIKELQARIEELEEEIEAERASRSKAEKQRSDLSRELEEISERLEEAGGATSAQVE-LNKKREAEFQ 1175
Cdd:PRK10929 105 dALEQEI-LQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQaQLTALQAESA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1176 KLRRDLEEatLQHEAMAAALRKKHADSMAELA----EQIDN-LQRVKQKL---EKEKSELKMEiddlssNAEVISKAKGN 1247
Cdd:PRK10929 184 ALKALVDE--LELAQLSANNRQELARLRSELAkkrsQQLDAyLQALRNQLnsqRQREAERALE------STELLAEQSGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1248 LEKmcrsleDQVSELKTKEE----------------EQQRLINDLTAQ-RAHLQT--EAGEY---SRLLDEkdALVSQLS 1305
Cdd:PRK10929 256 LPK------SIVAQFKINRElsqalnqqaqrmdliaSQQRQAASQTLQvRQALNTlrEQSQWlgvSNALGE--ALRAQVA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 1306 RRKQASTQQieelkhQLEEEtkaknaLAHALQSSRHDGDLLREQYEEEQEGKAELQrALSKANSEV--AQWRTKYE--TD 1381
Cdd:PRK10929 328 RLPEMPKPQ------QLDTE------MAQLRVQRLRYEDLLNKQPQLRQIRQADGQ-PLTAEQNRIldAQLRTQREllNS 394
|
410 420
....*....|....*....|....*
gi 1331883584 1382 AIQ--RTEELEEAKKKLAQ-RLQEA 1403
Cdd:PRK10929 395 LLSggDTLILELTKLKVANsQLEDA 419
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
840-1089 |
9.18e-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: 40.88 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 840 KPLLKSAETEKEMATMKEDFQKTKDELAKSEAKRKELEE----------KMVTLLKEKNDLQLQVQSEADSLADAEER-- 907
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaekarqaemdRQAAIYAEQERMAMERERELERIRQEERKre 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 908 CEQLIKNKIQLE-AKIKEVTERAEEEEEINAEL-----TAKKRKLEDECSELKKDIDDLELTLAKVEKEKhATENKVKNL 981
Cdd:pfam17380 362 LERIRQEEIAMEiSRMRELERLQMERQQKNERVrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-ARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331883584 982 TEEMAGLDEIIAKLSKEKKALQETHQQtlddlQAEEDKVNILTKAKTKLEQQVDD------LEGSLEQEKKLRMDLERAK 1055
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLELEKEKRDRKRAEeqrrkiLEKELEERKQAMIEEERKR 515
|
250 260 270
....*....|....*....|....*....|....
gi 1331883584 1056 RKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFE 1089
Cdd:pfam17380 516 KLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| |
