|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-773 |
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: 1327.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14913 319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEassgGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD----SGKKKVAKKKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14913 555 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14913 635 GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-773 |
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: 1317.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES---GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKvvKGKAEA 578
Cdd:cd01377 398 EQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 579 HFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEassggaaKKGAKKKGSSFQTVSALF 658
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGG-------GGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 659 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 738
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....*
gi 1958661053 739 EGQyIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01377 629 KGF-DDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-773 |
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: 1303.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEAsSGGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGAS-AGGGAKKGGKKKGSSFQTVSALFR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14912 560 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14912 640 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-773 |
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: 1265.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEassGGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAE---EGGGKKGGKKKGSSFQTVSALFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14910 558 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14910 638 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-773 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1264.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEE--SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEassgGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14918 479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAD----SGAKKGAKKKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-773 |
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: 1263.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEassGGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAE---GGGGKKGGKKKGSSFQTVSALFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14915 558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14915 638 GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-773 |
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: 1219.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSgaQTAEAEASSGGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFS--NYAGAEAGDSGGSKKGGKKKGSSFQTVSAVFR 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14923 558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14923 638 GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-773 |
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: 1163.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGE--KKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 419 TVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 577
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 578 AHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEaSSGGAAKKGAKKKGSSFQTVSAL 657
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDST-EDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 658 FRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 737
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1958661053 738 PEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-773 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1145.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEassgGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAP----IEKGKGKAKKGSSFQTVSALHR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14917 555 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14917 635 GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-773 |
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: 1131.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAN-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14916 400 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAeasSGGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADT---GDSGKGKGGKKKGSSFQTVSALHR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14916 557 ENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 636
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14916 637 GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-773 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1036.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV--------GRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 248 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQ-GEISVASI 326
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 327 DDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPR 406
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 407 VKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSA 564
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 565 NFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGA 644
Cdd:pfam00063 470 HFQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 645 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 724
Cdd:pfam00063 547 RTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1958661053 725 FKQRYKVLNASAIPEGQyIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:pfam00063 627 FVQRYRILAPKTWPKWK-GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-773 |
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: 1033.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-------LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 579
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAeassGGAAKKGAKKKGSSFQTVSALFR 659
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDS----AIQFGEKKRKKGASFQTVASLHK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14929 549 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPK 628
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14929 629 SKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-785 |
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: 997.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 81 NPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVR 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS----------GSNTEVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 241 NDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQG- 319
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 320 EISVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAAYLQGLNSADL 398
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 399 LKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQ 478
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 479 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYe 557
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 558 QHLGKSANFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEaeassg 637
Cdd:smart00242 468 QHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNA------ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 638 gaakkgakKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 717
Cdd:smart00242 539 --------GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFP 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 718 SRILYADFKQRYKVLNASAIPEGQyIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRD 785
Cdd:smart00242 611 YRLPFDEFLQRYRVLLPDTWPPWG-GDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-773 |
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: 981.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSDG------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 421 EQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 500
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 501 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGK-AEAH 579
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 580 FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAeassggaakKGAKKKGSSFQTVSALFR 659
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG---------SKKQKRGSSFMTVSNFYR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 660 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 739
Cdd:cd14934 547 EQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQ 626
|
650 660 670
....*....|....*....|....*....|....
gi 1958661053 740 GqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14934 627 G-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-773 |
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: 970.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA----KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd14909 317 VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVK-GKAEA 578
Cdd:cd14909 397 EQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 579 HFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFS--GAQTAEAEassggAAKKGAKKKGSSFQTVSA 656
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAdhAGQSGGGE-----QAKGGRGKKGGGFATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 657 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 736
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*..
gi 1958661053 737 IPEGQyiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14909 632 IQGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-773 |
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: 838.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATIAvtgekKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPF----VSQGEISVASIDDQEELMA 334
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 335 TDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNE 412
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 413 YVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 491 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKP 569
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 570 KvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSmktlaylfsgaqtaeaeassggaakkgakkkgs 649
Cdd:cd00124 475 R----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS--------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 650 sfqtvsaLFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 729
Cdd:cd00124 518 -------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRY 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1958661053 730 KVLNASAIPEGQYiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd00124 591 RILAPGATEKASD-SKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1119 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 832.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 30 RPFDAKTSVFVAEPKESFVKGTIQskdaGKVTVKTEAGATLTVKEDQIFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKER 109
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKVT----EEGKKEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 110 YAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNT 189
Cdd:COG5022 90 YNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 190 KRVIQYFAtiAVTGekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETY 269
Cdd:COG5022 170 KRIMQYLA--SVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 270 LLEKSRVTFQLKAERSYHIFYQITSNKkPELIEMLLITTNPYDYPFVSQGE-ISVASIDDQEELMATDSAIDILGFTNDE 348
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 349 KVSIYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVG 428
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 429 ALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 508
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 509 IEWTFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYEQ-HLGKSANFQKPKVVKGKaeahFSLIHY 585
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 586 AGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEaeassggaakkgakkKGSSFQTVSALFRENLNKL 665
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE---------------SKGRFPTLGSRFKESLNSL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 666 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQYI-- 743
Cdd:COG5022 619 MSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwk 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 744 -DSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGFLARVEYQKMVERRESIFCIQ 822
Cdd:COG5022 699 eDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 823 YNIRAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELaKSEAKRKELEEKMVSLLKEKNDLQLQVQAEA 902
Cdd:COG5022 779 HGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKA 857
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 903 EGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHA 977
Cdd:COG5022 858 KKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKL 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 978 TEN-KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLE 1056
Cdd:COG5022 937 LNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTK 1016
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1057 RAKRKLEGDLKLAQEsiMDIENEKQQLDERLKKKEFEMSNLQSKIEdeqaigiQLQKKIKELQ 1119
Cdd:COG5022 1017 QLKELPVEVAELQSA--SKIISSESTELSILKPLQKLKGLLLLENN-------QLQARYKALK 1070
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-773 |
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: 792.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKK-----KEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMAT 335
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 336 DSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQGLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 415 TKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 494 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeqhlgkSANFQKPKVVK 573
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 574 G--KAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSF 651
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 652 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1958661053 732 LNASAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-773 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 768.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD----HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 419 TVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 497 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPKVVK 573
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 574 GKAEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQ----TAEAEASSGGAAKKGAKKKGS 649
Cdd:cd14920 473 DKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 650 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 729
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1958661053 730 KVLNASAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14920 631 EILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-773 |
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: 712.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPKvvKGK 575
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKV-VQEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 576 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTA---EAEASSGGAAKKGAKKKGSSFQ 652
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIvglDKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 733 NASAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-773 |
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: 695.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKGK 575
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 576 AEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTA----EAEASSGGAAKKGAKKKGSSF 651
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIvgldQMAKMTESSLPSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 652 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1958661053 732 LNASAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-773 |
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: 683.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATiaVTGEKKKEEVTsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGETQV--------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI-TSNKKPELIEMLLitTNPYDYPFVSQGE-ISVASIDDQEELMATD 336
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLcAAASLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 337 SAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 417 GQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 495 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK-SANFQKPKVVK 573
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 574 GKaeahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKtlaylfsgaqtaeaeassggaakkgakkkgssFQT 653
Cdd:cd01380 468 TA----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------------------KKT 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 654 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLN 733
Cdd:cd01380 512 VGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLL 591
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1958661053 734 ASAipEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01380 592 PSK--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-773 |
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 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTV 420
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 421 EQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 499
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 500 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKvvKGKA 576
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEA--EASSGGAAKKGAKKKGSSFQTV 654
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGldKVSGMSEMPGAFKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 655 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 734
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 1958661053 735 SAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-773 |
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: 667.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 498
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 499 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKGK 575
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 576 AEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTA----EAEASSGGAAKKGAKKKGSSF 651
Cdd:cd14919 472 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIigldQVAGMSETALPGAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 652 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1958661053 732 LNASAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14919 630 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-773 |
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: 656.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATDSAID 340
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQT 419
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 498 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVKG 574
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 575 KAEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQ--TAEAEASSGGAAKKGAKKKGSSFQ 652
Cdd:cd14930 473 QAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgiVGLEQVSSLGDGPPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 733 NASAIPEGqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14930 631 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-773 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 636.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGekkkeevtsgkmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGS-------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSA 338
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 419 TVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 498 VLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFqkpkvvKGKA 576
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKtLAYLFSgaqTAEAEASSGGAAKKGAKKKGSSFQTVSA 656
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFA---SKMLDASRKALPLTKASGSDSQKQSVAT 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 657 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 736
Cdd:cd01383 533 KFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPED 612
|
650 660 670
....*....|....*....|....*....|....*..
gi 1958661053 737 IPEGQYIDSkkASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01383 613 VSASQDPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-773 |
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: 635.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFAtiAVTGeKKKEEVTSGKmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSG-GSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAAYLQGLNSADLLKALCYPRVKVGNEY---VTKG 417
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 418 QTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhm 496
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 497 FVL--EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyEQHLGKSANFQKPKVV 572
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 573 KGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaqtaeaeassggaAKKGAKKKGSSFQ 652
Cdd:cd01378 468 FELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF---------------PEGVDLDSKKRPP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd01378 533 TAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLL 612
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 733 NASAIPEGQYIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01378 613 SPKTWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-773 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 626.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIavtgekkkeevtSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSAI 339
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 418 QTVEQVTNAVGALAKAMYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPkvv 572
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 573 KGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGGaakkgakkkgssfQ 652
Cdd:cd01381 462 KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS-------------P 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 653 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 732
Cdd:cd01381 529 TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 733 nASAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01381 609 -VPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-773 |
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: 603.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFAtiAVTGEkkkeevtsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNN-----------HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK--PELIEmLLITTNPYDYPFVSQ-GEISVASIDDQEELMATDS 337
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 338 AIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 417 GQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKvvKGK 575
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 576 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFS-GAQTAEAEASSGGAAKKGAKKKGSSFQTV 654
Cdd:cd14883 464 WKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTyPDLLALTGLSISLGGDTTSRGTSKGKPTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 655 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 734
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 1958661053 735 SAIPEGQYIDsKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14883 624 RARSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-773 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 581.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATIAvtgekkKEEVTSGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG------GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDS 337
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 338 AIDILGFTNDEKVSIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADKAAYLQGLNSADLL--------KALCYPRVKV 409
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEFHLKAAAELLmcdekaleDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 410 GNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 489
Cdd:cd01384 306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 490 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSANFQK 568
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 569 PKvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAeassggaakkgakKKG 648
Cdd:cd01384 464 PK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT-------------SSS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 649 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 728
Cdd:cd01384 527 SKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1958661053 729 YKVLnASAIPEGQYiDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 773
Cdd:cd01384 607 FGLL-APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-773 |
4.03e-171 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 536.67 E-value: 4.03e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 176 LITGESGAGKTVNTKRVIQYFATI----AVTGEKKKEEVTSGKMQ--GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGEISVASIDDQ 329
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 330 EELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAAYLQGLNSADLLKALCYPRVK 408
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 409 VGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYEQHLGK 562
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 563 S------------ANFQKPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYqKSSMKTLAYLFSGAQta 630
Cdd:cd14890 479 SgsggtrrgssqhPHFVHPKF---DADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELI-KQSRRSIREVSVGAQ-- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 631 eaeassggaakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIR 710
Cdd:cd14890 553 ---------------------------FRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQ 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 711 ICRKGFPSRILYADFKQRYKVLNASAipegqyiDSKKASEKLLGSI-DIDHTQYKFGHTKVFFK 773
Cdd:cd14890 606 IRQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-773 |
2.29e-170 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 534.14 E-value: 2.29e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 182 GAGKTVNTKRVIQYFATIAvtgekkkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESW------------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLittnpydypfvsqgeiSVASIDDQEELMATDSAIDI 341
Cdd:cd01382 152 VGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 342 LGFTNDEKVSIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AAYLQGLNSADLLKALCYpRVKVGNE 412
Cdd:cd01382 216 IGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 413 YVTKGQ------TVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 486
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 487 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLgKSAN 565
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 566 FQKPKvvKGKAEAH--------FSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaqtaeaEASSG 637
Cdd:cd01382 447 LSIPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF--------ESSTN 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 638 GAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 717
Cdd:cd01382 517 NNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 718 SRILYADFKQRYKvlnasaipegQYIDSK----------KASEKLLGSIDIDhtqYKFGHTKVFFK 773
Cdd:cd01382 597 SRTSFHDLYNMYK----------KYLPPKlarldprlfcKALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-773 |
1.63e-167 |
|
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: 527.34 E-value: 1.63e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEVtsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF--- 255
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV---------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 256 ------GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS-----------------------NKKPELIEMLLI 306
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 307 TT-NPYDYPFVSqGEISVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTE 382
Cdd:cd14888 231 EPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 383 VADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIG 461
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 462 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEE 540
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 541 CMFPKATDTSFKNKLYEQHlgksANFQKPKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTL 620
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKH----KGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 621 AYLFSgaqtaeaeasSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQL 700
Cdd:cd14888 544 SNLFS----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQL 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 701 RCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasAIPEGQyidskkasekllgsidIDHTQYKFGHTKVFFK 773
Cdd:cd14888 614 KYGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1930 |
8.40e-166 |
|
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: 536.68 E-value: 8.40e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 853 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER 932
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 933 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQ 1012
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1013 TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEF 1092
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1093 EMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNK 1172
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1173 KREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL 1252
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1253 EKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKA 1332
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1333 KNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVE 1412
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1413 AVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMK 1492
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1493 NAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLEL 1572
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1573 NQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRN 1652
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1653 TQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLIN 1732
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1733 TKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAL 1812
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1813 KGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1892
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1958661053 1893 EEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVK 1930
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-773 |
1.32e-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: 521.26 E-value: 1.32e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTgekkkeevTSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS--------TNG-----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSnkKPELIEMLLITTNPyDYPFVSQGE-ISVASIDDQEELMATDSA 338
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLQGLNSADLLKALCYPRVKVgneyvt 415
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEI------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 416 KGQ-------TVEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14872 299 KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSanF 566
Cdd:cd14872 379 LQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--T 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 567 QKPKVVKGkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSggaakkgakk 646
Cdd:cd14872 456 FVYAEVRT-SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKV---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 647 kgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 726
Cdd:cd14872 525 ------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1958661053 727 QRYKVLNaSAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14872 599 KRYRFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-773 |
2.06e-164 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 518.56 E-value: 2.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEdQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELiEMLLITTNPYDYPFvSQGEISVASIDDQEELMATDSA 338
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 417 GQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKgka 576
Cdd:cd14903 387 FKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 577 eAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFS-GAQTAEAEASSGGAAKKGAKKKGSSFQTVS 655
Cdd:cd14903 463 -TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKeKVESPAAASTSLARGARRRRGGALTTTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 656 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnas 735
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF--- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 736 aIPEGQYIDSKKAS--EKLLGSIDIDH-TQYKFGHTKVFFK 773
Cdd:cd14903 619 -LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-773 |
4.25e-163 |
|
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: 516.16 E-value: 4.25e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 183 AGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGE-ISVASIDDQEELMATDSAID 340
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQ 418
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 419 TVEQVTNAVGALAKAMYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 494
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 495 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYEQHLGKSANFQKPKvvk 573
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 574 gKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTL-------------------------AYLFSGAQ 628
Cdd:cd01385 466 -VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwavlrafframaAFREAGRR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 629 TAEAEASSGGAAKKGAKKKGSSFQ------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 702
Cdd:cd01385 545 RAQRTAGHSLTLHDRTTKSLLHLHkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 703 NGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPEGQyIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-773 |
2.91e-161 |
|
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: 508.74 E-value: 2.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIavtgekkkeevtsGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL-------------GKANnRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKpeLIEMLLITTNPYDYPFVSQGEISVASIDD--QEEL 332
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIyaglAEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 333 MATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAAYLQGLNSADLLKALCYPRVK 408
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 409 VGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLyEQHL 560
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF-HNNI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 561 gKSANFQKPKvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAylfsgaqtaeaeassggaa 640
Cdd:cd01379 460 -KSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 641 kkgakkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 720
Cdd:cd01379 516 -----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 721 LYADFKQRYKVL--NASAIPEGqyidSKKASEKLLGSIDIDHtqYKFGHTKVFFK 773
Cdd:cd01379 585 LFADFLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-773 |
4.61e-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: 509.29 E-value: 4.61e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIAVTGEKKKEEvtsgkmqgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGK 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNLVTE------------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQI------TSNKKPELIEmllittnPYDYPFVSQG-EISVASIDDQEELM 333
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELlaglpaQLRQKYGLQE-------AEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 334 ATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----AYLQGLNSADLLKALCYPRVK 408
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 409 VGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd01387 300 TRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 489 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQ 567
Cdd:cd01387 380 QYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 568 KPKVvkGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSgAQTAEAEASSGGAAKKGAKKK 647
Cdd:cd01387 458 KPRM--PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS-SHRAQTDKAPPRLGKGRFVTM 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 648 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 727
Cdd:cd01387 533 KPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFID 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1958661053 728 RYKVLNASAIPEG-QYIDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 773
Cdd:cd01387 613 RYRCLVALKLPRPaPGDMCVSLLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-771 |
5.02e-161 |
|
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: 509.33 E-value: 5.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 172 --NQSILITGESGAGKTVNTKRVIQYFATIAvTGEKKKEEVTSgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS-SATTHGQNATE---RENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNP-YDYPFVSQGEISVASIDD 328
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 329 QEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY-LQGLNSADLLKALCYPRV 407
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 408 KVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 486 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSA 564
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 565 NFQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMktlAYLFSgaqtaeaeassggaakkga 644
Cdd:cd14901 475 SFSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSN---AFLSS------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 645 kkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 724
Cdd:cd14901 531 --------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDA 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 725 FKQRYKVLNAS------AIPEGQYIDSKKASEKLLGSIDIDHTQykFGHTKVF 771
Cdd:cd14901 603 FVHTYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-773 |
8.98e-156 |
|
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: 494.70 E-value: 8.98e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAvtgeKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQ-GEISVASIDDQEELMATDSA 338
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AAYLQGLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 414 VTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 494 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVvk 573
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRV-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 574 gkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGAkkkgssfQT 653
Cdd:cd14873 464 --AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR-------PT 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 654 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL- 732
Cdd:cd14873 535 VSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLm 614
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 733 NASAIPEgqyiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14873 615 RNLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-773 |
8.92e-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: 491.97 E-value: 8.92e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVAAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 256 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGE-ISVASIDDQEELMA 334
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 335 TDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAAYLQGLNSADLLKALCYpRVKVGne 412
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 413 yvTKGQTVE------QVTNAVGALAKAMYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14892 320 --ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 555 LYEQHLGKSANFQKPKVvkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMktlaylfsgaqtaeaea 634
Cdd:cd14892 477 YHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 635 ssggaakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRK 714
Cdd:cd14892 536 -----------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRRE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 715 GFPSRILYADFKQRYKVLNASAIPEGQYIDSKKASE--KLLGSI---DIDHTQYKFGHTKVFFK 773
Cdd:cd14892 593 GFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTarKKCEEIvarALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-773 |
1.55e-146 |
|
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: 468.79 E-value: 1.55e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 261 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEEL-----MAT 335
Cdd:cd14897 151 LLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrqMFH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 336 DSaIDIL---GFTNDEKVSIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AAYLQGLNSADLLKALCYPRV 407
Cdd:cd14897 230 DL-TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 408 KVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCIN 482
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 483 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLyEQHLG 561
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 562 KSANFQKPKvvKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaqtaeaeassggaak 641
Cdd:cd14897 462 ESPRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF----------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 642 kgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 721
Cdd:cd14897 521 -------------TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIK 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 722 YADFKQRYKVLNASAipegqyidSKKASEKLLGSIDIDHTQ----YKFGHTKVFFK 773
Cdd:cd14897 588 YEDFVKRYKEICDFS--------NKVRSDDLGKCQKILKTAgikgYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-732 |
4.73e-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: 461.31 E-value: 4.73e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATiaVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ--AGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 246 RFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYqitsnkkpeliEMLLittnpydypfvSQGEISVAS 325
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFY-----------EMAI-----------GASEAARKR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 326 iDDQEELMAtdsAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAAYLQGLNSADL 398
Cdd:cd14900 219 -DMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 399 LKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGFEIFDF 473
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 474 NSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFK 552
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 553 NKLYEQhLGKSANFQKPKVVKGKaeAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQkssmktlaylfSGAQtaea 632
Cdd:cd14900 454 SKLYRA-CGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-----------YGLQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 633 eassggaakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIC 712
Cdd:cd14900 516 -------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
|
650 660
....*....|....*....|
gi 1958661053 713 RKGFPSRILYADFKQRYKVL 732
Cdd:cd14900 571 RAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-773 |
2.36e-142 |
|
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: 458.34 E-value: 2.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVT-------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSS 245
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 246 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYP--FVSQGEIS 322
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRydYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 323 -VASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQGLNSADLL 399
Cdd:cd14907 243 eVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 400 KALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEIF 471
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 472 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 548
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 549 TSFKNKLYEQHlgksANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGaq 628
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSG-- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 629 taeaEASSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEG 708
Cdd:cd14907 556 ----EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLES 631
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 709 IRICRKGFPSRILYADFKQRYKVLNasaipegqyidskkasekllgsididhTQYKFGHTKVFFK 773
Cdd:cd14907 632 IRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-773 |
5.85e-139 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 448.24 E-value: 5.85e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATIAvtGEKKKEEVtsgkmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKTI----------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDS 337
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 338 AIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKAAYLQGLNSADLLKALCYPRVKVGNEYVTKG 417
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 418 QTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 497 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQH--LGKSANFQKPKVVKg 574
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 575 kaeAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGAKkkgssfQTV 654
Cdd:cd14904 466 ---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAP------KSL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 655 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 734
Cdd:cd14904 537 GSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1958661053 735 saiPEGQYIDSKKASEKLLGSIDIDHT-QYKFGHTKVFFK 773
Cdd:cd14904 617 ---PSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-773 |
4.91e-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: 4.91e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 178 TGESGAGKTVNTKRVIQYFAtiavtgekkkeEVTSGKMQgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgT 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIM-----------ELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI---TSNKKPELIEMLlittNPYDYPFVSQGEisvasidDQEELMA 334
Cdd:cd14889 149 NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGA-------GCKREVQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 335 T--------DSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQGLNSADLLKALCYP 405
Cdd:cd14889 218 YwkkkydevCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 406 RVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSLEQL 479
Cdd:cd14889 298 VTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 480 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLyEQH 559
Cdd:cd14889 375 CINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKL-NIH 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 560 LGKSANFqkpKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSG--AQTAEAEASSG 637
Cdd:cd14889 454 FKGNSYY---GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAtrSRTGTLMPRAK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 638 GAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 717
Cdd:cd14889 530 LPQAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFS 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 718 SRILYADFKQRYKVLNASAIPEGqyidSKKASEKLLGSIDIdhTQYKFGHTKVFFK 773
Cdd:cd14889 610 WRPSFAEFAERYKILLCEPALPG----TKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
24-832 |
6.32e-135 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 442.93 E-value: 6.32e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 24 RIEAQNRPFDAKTSVFV-------------AEPKESFVKGTIQ-SKDAGKVTVK---TEAGATLTVKEDQIF----PMNP 82
Cdd:PTZ00014 16 RRNSNVEAFDKSGNVLKgfyvwtdkapavkEDPDLMFAKCLVLpGSTGEKLTLKqidPPTNSTFEVKPEHAFnansQIDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 83 PKYDkieDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR-GKKRQEAPPHIFSISDN 161
Cdd:PTZ00014 96 MTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 162 AYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRN 241
Cdd:PTZ00014 173 ALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSK-----------SGNMDLKIQNAIMAANPVLEAFGNAKTIRN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 242 DNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEI 321
Cdd:PTZ00014 242 NNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKL-KSLEEYKYINPKCL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 322 SVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-----PDGTEVADKAAYLQGLNSA 396
Cdd:PTZ00014 321 DVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 397 DLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:PTZ00014 401 SLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKPMGIFSILEEECMFPKATDTS 550
Cdd:PTZ00014 481 EQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKGKSVLSILEDQCLAPGGTDEK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 551 FKNKLYEQhLGKSANFQKPKVVKGKaeaHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTA 630
Cdd:PTZ00014 555 FVSSCNTN-LKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVE 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 631 EAEASSGgaakkgakkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIR 710
Cdd:PTZ00014 631 KGKLAKG--------------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQ 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 711 ICRKGFPSRILYADFKQRYKVLNAsAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQ 790
Cdd:PTZ00014 697 LRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAA 775
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1958661053 791 ---LITRTQAMCRGFLARveyQKMVERRESIFCIQYNIRAFMNVK 832
Cdd:PTZ00014 776 wepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-730 |
1.13e-131 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 430.08 E-value: 1.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYR--------GKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTledQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEmLLITTNPYDYPFVSQGEISVA----- 324
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkrav 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 325 SIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAAYLQGLNSAD 397
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 398 LLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAGF 468
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 469 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKAT 547
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 548 DTSFKNKLYEQHLGksanfqkpkvvkgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLfsGA 627
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI--GA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 628 QTAEAEASSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLE 707
Cdd:cd14902 535 DENRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLE 614
|
650 660
....*....|....*....|...
gi 1958661053 708 GIRICRKGFPSRILYADFKQRYK 730
Cdd:cd14902 615 AVRIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-739 |
7.10e-131 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 426.63 E-value: 7.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 250 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQI------TSNKKPELIEMLLITTN-PYDYPFVSQGEI- 321
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLlrggdeEEHEKYEFHDGITGGLQlPNEFHYTGQGGAp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 322 SVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAAYLQGLNSADL 398
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 399 LKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSL 476
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNK 554
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 555 LYEQHL-------GKSANFQKPKVVKGKaeAHFSLIHYAGTVDYNI-TGWLDKNKDPLNETVVGLYQkssmktlaylfSG 626
Cdd:cd14908 479 LYETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFE-----------SG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 627 AQtaeaeassggaakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 706
Cdd:cd14908 546 QQ-----------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVL 596
|
650 660 670
....*....|....*....|....*....|...
gi 1958661053 707 EGIRICRKGFPSRILYADFKQRYKVLnASAIPE 739
Cdd:cd14908 597 EAVRVARSGYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-773 |
8.85e-131 |
|
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: 425.23 E-value: 8.85e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNPEVvAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 175 ILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQG------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 248
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 249 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQ-GEISVASI 326
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 327 DDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAAYLQGLNSADLLKAL 402
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 403 CYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 481
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 482 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHl 560
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 561 GKSANFQKPKvVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNEtvvglyqkssmkTLAYLFSGaqtaeaeassggaa 640
Cdd:cd14891 475 KRHPCFPRPH-PKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPE------------DFEDLLAS-------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 641 kkgakkkgssfqtvSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 720
Cdd:cd14891 527 --------------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 721 LYADFKQRYKVLNASAI------PEGQYIdskkasEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14891 593 TYAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-773 |
5.44e-125 |
|
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: 410.88 E-value: 5.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVAAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 170 RENQSILITGESGAGKTVNTKRVIQYfatIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNY---LAESSKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 250 FIRIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPE-LIEMLLITTNPYDYPFVSQGEISV 323
Cdd:cd14895 155 FVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 324 AS--IDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA----------------- 384
Cdd:cd14895 235 RNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 385 -DKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQY----- 458
Cdd:cd14895 315 lDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 459 ------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPM 531
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 532 GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGL 611
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 612 YQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAM 691
Cdd:cd14895 551 LGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 692 EHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASaipegQYIDSKKASEkLLGSIDIDHTQykFGHTKVF 771
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRVF 702
|
..
gi 1958661053 772 FK 773
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-773 |
8.42e-123 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 402.83 E-value: 8.42e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFATIAvtgekkkeevtSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAK-----------SGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTnPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 414 VTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 494 HHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSANFQ 567
Cdd:cd14876 389 DIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 568 KPKVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGgaakkgakkk 647
Cdd:cd14876 462 PAKV---DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG---------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 648 gssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 727
Cdd:cd14876 529 ----SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLY 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1958661053 728 RYKVLNAsAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14876 605 QFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-773 |
1.25e-121 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 399.15 E-value: 1.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIavtgEKKKEEVTSGKMQGTLedqiisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEI-SVASIDDQEELMATDSA 338
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAAYLQglNSADLLKALCYPRVKVGN-EYV 414
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLLQ--VPPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 415 TKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 492
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 493 NHHMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKV 571
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 572 vkgkAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFsgaQTAEAEASSGGAAKkgakkkgssf 651
Cdd:cd14896 463 ----PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF---QEAEPQYGLGQGKP---------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 652 qTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 731
Cdd:cd14896 526 -TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGA 604
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1958661053 732 LNASAIPEgqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14896 605 LGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-732 |
2.37e-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: 376.11 E-value: 2.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 178 TGESGAGKTVNTKRVIQYFATIAVTgekkKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS----PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 258 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLitTNPYDYPFVSQGEISVasidDQEELMATD 336
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHL--PEGAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 337 SAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEY 413
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 414 VT--KGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 490
Cdd:cd14880 313 QVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 491 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKP 569
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 570 KVVKgkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGAKkkgs 649
Cdd:cd14880 472 KLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL---- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 650 sfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 729
Cdd:cd14880 545 ---TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERY 621
|
...
gi 1958661053 730 KVL 732
Cdd:cd14880 622 KLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-735 |
1.06e-109 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 367.38 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFatIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTT 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 259 GKLASADIETYLLEKSRVTFQL-KAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQ-------- 329
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFKSQssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 330 -------EELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAAYLQGLNSADLL 399
Cdd:cd14906 241 nnktesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 400 KALCYPRVKVGNE--YVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRIN----QQLDTKQPRQY-------FIGVLDIA 466
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnQNTQSNDLAGGsnkknnlFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 467 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 545
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 546 ATDTSFKNKLYEQHLGKSANFQKPkvvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFS 625
Cdd:cd14906 480 GSEQSLLEKYNKQYHNTNQYYQRT-----LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 626 GAQTAEAEASSGGAAKKgakkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGV 705
Cdd:cd14906 555 QQITSTTNTTKKQTQSN----------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGV 624
|
650 660 670
....*....|....*....|....*....|
gi 1958661053 706 LEGIRICRKGFPSRILYADFKQRYKVLNAS 735
Cdd:cd14906 625 LNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-730 |
1.81e-108 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 364.03 E-value: 1.81e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 170 RENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKM-----QGTLEDQIISANPLLEAFGNAKTVRNDNS 244
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 245 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNK----KPELIEMLLITTNPYDYPFVSQG 319
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 320 EISVA--SIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 385
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 386 KAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQL--------------- 450
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 451 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-K 529
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 530 PMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVV 609
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 610 GLYQKSSMKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSFQT----VSALFRENLNKLMTNLRSTHPHFVRCIIPNET 685
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1958661053 686 KTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 730
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-773 |
1.41e-105 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 353.42 E-value: 1.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEVtsgkmqgtledqIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQSL------------ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEISVA-SIDDQEELMATDSA 338
Cdd:cd14886 155 GLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILgFTNDEKVSIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14886 234 LEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 416 KGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14886 313 SPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyEQHLgKSANFqkpkvVKG 574
Cdd:cd14886 393 VFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 575 K-AEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSggaakkgakkkgssfQT 653
Cdd:cd14886 465 KgSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG---------------KF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 654 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL- 732
Cdd:cd14886 530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILi 609
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1958661053 733 --NASAIPEGQyiDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14886 610 shNSSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-773 |
9.38e-105 |
|
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: 352.38 E-value: 9.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 182 GAGKTVNTKRVIQYFATIAVTGEKKkeeVTSGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV---LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFvsqGEISVASIDD----QEELMATDS 337
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 338 AIDILGFTNDEKVSIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAAYLQGLNSADLLKALCYPRVKVGNEYV 414
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 415 TKGQTVEQVTN------------AVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 476
Cdd:cd01386 306 TTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 477 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 541
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 542 MFPKATDTSFKNKLYeQHLGKSANFQKPKVVKgKAEA--HFSLIHYAGT--VDYNITGWLDKNK-DPLNETVVGLYQKSS 616
Cdd:cd01386 466 LYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 617 MKTlaylfsGAQTAEAeassggaakkgakkkgssfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPN------ETKTPGA 690
Cdd:cd01386 544 KET------AAVKRKS---------------------PCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSP 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 691 MEHELVLH------QLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL----NASAIPEGQYIDSKKASEKLLGSIDIDH 760
Cdd:cd01386 597 AAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEK 676
|
730
....*....|...
gi 1958661053 761 TQYKFGHTKVFFK 773
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-773 |
6.46e-103 |
|
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: 346.03 E-value: 6.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFAtiavtgeKKKEEVTSGKMQGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYLG-------QLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 255 F-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISV------ASID 327
Cdd:cd14875 156 FdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 328 DQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQgLNSADLLKalCYpRV 407
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRE--CF-LV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 408 KVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINF 483
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 484 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQHLGK 562
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 563 SANFQKPkvvKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSgAQTAEAEASsggaakk 642
Cdd:cd14875 469 SPYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS-TEKGLARRK------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 643 gakkkgssfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 722
Cdd:cd14875 538 ---------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 723 ADF-KQRYKVLNASAIPEGQYIDSKKASEKLLGS----IDIDHTQYKFGHTKVFFK 773
Cdd:cd14875 609 EQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-736 |
1.63e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 310.29 E-value: 1.63e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvynpEVVAAYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 176 LITGESGAGKTVNTKRVIQYFatiavtgekkkeeVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYL-------------VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 256 gtTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpeliemLLITTNPYDYPFVSQGEISVasIDDQEELMAT 335
Cdd:cd14898 140 --DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 336 DSAIDILGFTNDEkvSIYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVT 415
Cdd:cd14898 210 CSAMKSLGIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 416 KGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 495
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 496 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKsanfqkpkvVKGK 575
Cdd:cd14898 363 MFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGF---------INTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 576 AEAHFSLIHYAGTVDYNITGWLDKNKdplnetvvglyQKSSMKTLAYLfsGAQTAEAEassggaakkgakkkgssfQTVS 655
Cdd:cd14898 433 ARDKIKVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNL--LINDEGSK------------------EDLV 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 656 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 735
Cdd:cd14898 482 KYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
.
gi 1958661053 736 A 736
Cdd:cd14898 562 L 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-773 |
1.99e-90 |
|
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: 309.44 E-value: 1.99e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 178 TGESGAGKTVNTKRVIQYFATiavtgekkkeevTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 258 TGK-LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGE----ISVASIDDQEEL 332
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 333 MATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNE 412
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 413 YVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 488
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 489 QQFFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQ 567
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 568 KPKVVKGKAE-------AHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTaeaeassggaa 640
Cdd:cd14878 469 YSPMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLV----------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 641 kkgakkkgssfqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRI 720
Cdd:cd14878 538 ------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 721 LYADFKQRYKVLnASAIPEGQyidsKKASEKLLGSIDIDHTQ---YKFGHTKVFFK 773
Cdd:cd14878 606 SFSDFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-773 |
4.64e-90 |
|
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: 307.71 E-value: 4.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEvvaaYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 182 GAGKTVNTKRVIQYFatiaVTGEKKKEEVTSgkmqgTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNEISN-----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPyDYPFVSQGEISVASIDDQEELMATDSAIDI 341
Cdd:cd14937 146 VSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 342 LGFtNDEKVSIYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTK 416
Cdd:cd14937 225 MNM-HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 417 GQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 496
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 497 FVLEQEEYKKEGIEWTFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYEQHLGKSANFQKPKVVKGKA 576
Cdd:cd14937 384 YEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEAEASSggaakkgakkkgssfQTVSA 656
Cdd:cd14937 459 NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK---------------NLITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 657 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYKVLNASA 736
Cdd:cd14937 524 KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYST 602
|
650 660 670
....*....|....*....|....*....|....*..
gi 1958661053 737 IPEGQYIDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 773
Cdd:cd14937 603 SKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-773 |
1.34e-86 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 300.41 E-value: 1.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 172 NQSILITGESGAGKTVNTKRVIQYFAtiAVTGEKKkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLA--AVSDRRH------GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 252 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtnpYDYPFVSqgeisvasidDQEE 331
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGDPEST----------DLRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 332 LMATDSAIDILGftnDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---AAYLQGLNS----- 395
Cdd:cd14887 220 ITAAMKTVGIGG---GEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvt 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 396 -------ADLLKALCYPRVKVGNEYV------------TKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPR 456
Cdd:cd14887 297 easrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 457 QY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----D 515
Cdd:cd14887 377 SEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 516 FGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYEQHLGK----SANFQK 568
Cdd:cd14887 457 FSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKN 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 569 PKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNEtvvglyqkssmkTLAYLFSGAQTAEAEASSGGAAKKGAKKKG 648
Cdd:cd14887 537 ITPALSRENLEFTVSHFACDVTYDARDFCRANREATSD------------ELERLFLACSTYTRLVGSKKNSGVRAISSR 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 649 SsfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 728
Cdd:cd14887 605 R--STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1958661053 729 YKVLNASAIPEgqYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14887 683 YETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-772 |
2.63e-84 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 291.38 E-value: 2.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNPEVVAAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRENQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 176 LITGESGAGKTVNTKRVIQYFATIAVTGEKkkeevtsgkmqGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 254
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK-----------GTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 255 FGTTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQITSNKKPELIEMLLITTNP-YDYPFVSQG--EISVASIDDQE 330
Cdd:cd14879 157 FNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGLDDPSdYALLASYGChpLPLGPGSDDAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 331 ---ELMAtdsAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQGLNSADLLKALCYp 405
Cdd:cd14879 236 gfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTY- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 406 RVKvgneYVTKgqtvEQVT---NAVGA------LAKAMYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD--- 472
Cdd:cd14879 312 KTK----LVRK----ELCTvflDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstg 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 473 FNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTS 550
Cdd:cd14879 384 GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 551 FKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGlyqkssmktlayLFSGAQTa 630
Cdd:cd14879 463 MLEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVN------------LLRGATQ- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 631 eaeassggaakkgakkkgssfqtvsalFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIR 710
Cdd:cd14879 530 ---------------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAA 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 711 ICRKGFPSRILYADFKQRYKvlnasaiPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFF 772
Cdd:cd14879 583 RLRVEYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-721 |
5.83e-77 |
|
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: 271.01 E-value: 5.83e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 172 NQSILITGESGAGKTVNTKRVIQYFATIavtgekkkeevtSGKMQGT-LEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI------------QTDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 251 IRIHFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGE- 320
Cdd:cd14884 149 NLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 321 -----------ISVASIDDQEELMATDSA-----IDILGFTNDEKVSI---YKLTGAVMHYGNMKFKQkqreeqaepdgt 381
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 382 evadkAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRIN---------QQLDT 452
Cdd:cd14884 297 -----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 453 KQPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDfgmdLAACIELIEK 529
Cdd:cd14884 372 EDIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 530 PMGIFSILEEECMFP----KATDTSFKNKLY----EQHLGK--SANFQKPKVVKGKAEAH------FSLIHYAGTVDYNI 593
Cdd:cd14884 448 IAKIFRRLDDITKLKnqgqKKTDDHFFRYLLnnerQQQLEGkvSYGFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 594 TGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTAEaeassggaakkgakkkgssFQTVSALFRENLNKLMTNLRSTH 673
Cdd:cd14884 528 NNWIDKNSDKIETSIETLISCSSNRFLREANNGGNKGN-------------------FLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1958661053 674 PHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRIL 721
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-753 |
5.33e-69 |
|
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: 245.79 E-value: 5.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNPEVVAAYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 181 SGAGKTVNTKRVI-QYFatiavtgekkkeEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 259
Cdd:cd14881 77 SGSGKTYASMLLLrQLF------------DVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKP-ELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 338
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 339 IDILG--FTNdekvsIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLqGLNSADLLKALcYPRVKVgneyvTK 416
Cdd:cd14881 224 LGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAALL-GVSGAALFRGL-TTRTHN-----AR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 417 GQTVEQVTNA------VGALAKAMYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTN 485
Cdd:cd14881 292 GQLVKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 486 EKLQQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYEQHLGkS 563
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-N 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 564 ANFQKPKVVKGKAeahFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKtlaylFSgaqtaeaeassggaakkg 643
Cdd:cd14881 449 PRLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCN-----FG------------------ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 644 akkkgssFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 723
Cdd:cd14881 503 -------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFK 575
|
650 660 670
....*....|....*....|....*....|
gi 1958661053 724 DFKQRYKVLnASAIPEGQYIDSKKASEKLL 753
Cdd:cd14881 576 AFNARYRLL-APFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-773 |
2.21e-68 |
|
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: 244.26 E-value: 2.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 182 GAGKTVNTKRVIQYFATIavtgekkkeevtsGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL-------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 262 ASADIETYLLEKSRVTFQLKAERSYHIFYQI--TSNKKPELIEMLLITTNPYDY----PFVSQGEISVASIDDQEELMAT 335
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFydFIEAQNRLKEYNLKAGRNYRYlripPEVPPSKLKYRRDDPEGNVERY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 336 DSAIDIL---GFTNDEKVSIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNE 412
Cdd:cd14882 230 KEFEEILkdlDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 413 YVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 487
Cdd:cd14882 308 AERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNTLNEQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 488 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILeeecmfpkatDTSFKNKLYEQHLGKSANFQ 567
Cdd:cd14882 386 MQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYII----------DDASRSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 568 KPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFSGAQTaeaeassggaakkgakkk 647
Cdd:cd14882 456 HSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 648 gSSFQTVSALFR----ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 723
Cdd:cd14882 518 -RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQ 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1958661053 724 DFKQRYKVLnasAIPEGQYIDSKKASEKLLgSIDIDHTQYKFGHTKVFFK 773
Cdd:cd14882 597 EFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-730 |
2.50e-65 |
|
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: 237.95 E-value: 2.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 173 QSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 253 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKK--PELIEMLLITTNPYDYPFVSQG--EISVASID- 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 328 -DQEELMATDSAIDIlgfTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAAYL-----QGLNSADLL 399
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCAlkdpaQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 400 KAlcYPRV------------KVGNEYVT--KGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQL----DTKQPRQYFIG 461
Cdd:cd14893 321 EV--EPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 462 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELI 527
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 528 E-KPMGIFSILEEECMFPKATDTSFKNKLY---EQHLGKS-----ANFQKPKVVKGKA-EAHFSLIHYAGTVDYNITGWL 597
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgnEAVGGLSrpnmgADTTNEYLAPSKDwRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 598 DKNKDPLNETVVGLYQkSSMKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSFQTVSALFRENLN-------------- 663
Cdd:cd14893 559 SKNMLSISSTCAAIMQ-SSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqad 637
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661053 664 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 730
Cdd:cd14893 638 ALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-716 |
1.20e-64 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 234.22 E-value: 1.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 185 KTVNTKRVIQYFATIAVTGEKkkeevtsgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASA 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 265 DIETYLLEKSRVTFQLKAERSYHIFYQ----ITSNKKPeliEMLLITTNPYDYpFVSQGEISVASIDDQEELMATDSAID 340
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQflkgITDEEKA---AYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 341 ILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKAAYlqglnsADLLKALCYPRVKVGNEYVT-KGQT 419
Cdd:cd14905 229 FFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 420 VEQVTNAVGALAKAMYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 497
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 498 VLEQEEYKKEGIEW-TFIDFgMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLyeqhlgksANFQKPKVVKGKA 576
Cdd:cd14905 373 KQEQREYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 577 EAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKtlaYLFS-------GAQTAEAEassgGAAKKGAKKKGS 649
Cdd:cd14905 441 PNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITK---YLFSrdgvfniNATVAELN----QMFDAKNTAKKS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 650 SFQTVSALFR------ENLNK-----------------------LMTNLRSTHP---------HFVRCIIPNETKTPGAM 691
Cdd:cd14905 514 PLSIVKVLLScgsnnpNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTF 593
|
650 660
....*....|....*....|....*
gi 1958661053 692 EHELVLHQLRCNGVLEGIRICRKGF 716
Cdd:cd14905 594 DVKSVNEQIKSLCLLETTRIQRFGY 618
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-732 |
2.29e-64 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 232.07 E-value: 2.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 180 ESGAGKTVNTKRVIQYFATiavtgeKKKEEVTSgkmqgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS------QPKSKVTT--------KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 260 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMATDSAI 339
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 340 DILGFTNDEKVSIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----AYLQGLNSADLLKALCyPRVKVGNEYv 414
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 415 tkgqTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 493
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 494 HHMFVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSAnFQK 568
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 569 pkvVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSMKTLAYLFS--GAQTAEaeassggaakkgakk 646
Cdd:cd14874 444 ---ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFEsySSNTSD--------------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 647 kgsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 726
Cdd:cd14874 506 ---MIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFA 582
|
....*.
gi 1958661053 727 QRYKVL 732
Cdd:cd14874 583 RQYRCL 588
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-253 |
2.20e-61 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 207.58 E-value: 2.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 122 FCVTVNPYKWLPVYNPEVV-AAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 201 VTGEKKKEE---VTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 253
Cdd:cd01363 81 FNGINKGETegwVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-771 |
1.67e-44 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 174.25 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 179 GESGAGKTVNTKRVIQYFA-----------TIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 247
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 248 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASID 327
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 328 DQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 384
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 385 DKAAYLQ----GLNSADLLKALCYPRVkVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYF- 459
Cdd:cd14938 319 VKNLLLAckllSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 460 --IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM--GIFS 535
Cdd:cd14938 398 nyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 536 ILEEECMfPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAhFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKS 615
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 616 SMKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSF--------QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKT 687
Cdd:cd14938 556 ENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 688 P-GAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAsaipegqyiDSKKASEKLLGSIDIDHTQYKFG 766
Cdd:cd14938 636 ElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 1958661053 767 HTKVF 771
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1180-1937 |
2.52e-30 |
|
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: 131.33 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1180 KMRRdlEEATLQHEATAATLrKKHADSVAELGEQIDNLQRVKQKLEK-----------EKSEMKMEIDDLASNVETVSKA 1248
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1249 KGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEE 1328
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1329 EVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAE 1408
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-SKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1409 EHVEavnakcaSLEKTKQRLQNEVEDlmLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTEL 1488
Cdd:TIGR02168 407 ARLE-------RLEDRRERLQQEIEE--LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1489 FKMKNAYEES---LDQLETLKRENKNLQQEISDLT---EQIAEGGKRIHELEKIKKQVEQekcELQAALEEAEASL--EH 1560
Cdd:TIGR02168 478 DAAERELAQLqarLDSLERLQENLEGFSEGVKALLknqSGLSGILGVLSELISVDEGYEA---AIEAALGGRLQAVvvEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1561 EEGKILRIQLelnQVKSEIDRK--IAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEI--QL 1636
Cdd:TIGR02168 555 LNAAKKAIAF---LKQNELGRVtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDL 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1637 NHANRMAAEALRNYRNtqgILKDTQLHLDDALRGQEDLKEQLAMVERRanllqAEIEELRATLEQTERSRKIAEQELLDA 1716
Cdd:TIGR02168 632 DNALELAKKLRPGYRI---VTLDGDLVRPGGVITGGSAKTNSSILERR-----REIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1717 SERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEK---AKKAITDA----AMMAEELKKEQDTSAHLERM 1789
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKELTELeaeiEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1790 KKNMEQTVKDLQLRLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNIL 1869
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1870 RLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTK 1937
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1596 |
2.94e-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: 127.88 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 847 LKSAETEKEMAtmkEEFQKTKDELAKSEAKrkELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKI 926
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 927 KEVTERAED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 998
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 999 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN 1078
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1079 EKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLS----------- 1147
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervrggravee 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1148 -------------RELEEISER----LEEAGGA------------TSAQIEMNKKREA------EFQKMRRDLEEATLQH 1192
Cdd:TIGR02169 515 vlkasiqgvhgtvAQLGSVGERyataIEVAAGNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1193 EATAAtlrkKHADSVAELGEQIDNLQR-------VKQKLEKEKSEM---KM-----EIDDLASNVETVSKAKGNLEKMCR 1257
Cdd:TIGR02169 595 EDGVI----GFAVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRLMgkyRMvtlegELFEKSGAMTGGSRAPRGGILFSR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1258 TLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALA 1337
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1338 HALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQAAEEHVEAVNAK 1417
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1418 CASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEE 1497
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1498 SLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK------KQVEQEKCELQAALEEAE-----ASLEHEEGKIL 1566
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKR 987
|
810 820 830
....*....|....*....|....*....|.
gi 1958661053 1567 RIQLELNQVKSEIDRK-IAEKDEEIDQLKRN 1596
Cdd:TIGR02169 988 LDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
983-1801 |
9.52e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 126.32 E-value: 9.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 983 KNLTEEMAGldetIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLR--------MD 1054
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelallvLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1055 LERAKRKLE---GDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEA 1131
Cdd:TIGR02168 234 LEELREELEelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1132 ERASRAKAEKQRSDLSR---ELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVA 1208
Cdd:TIGR02168 314 LERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK----VA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1209 ELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKmcRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQ 1288
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1289 TESGEFSRQLDEKEALVSQLsRGKQAFTQQIEELKRQLEEEVKakNALAHALQSSRHDcDLLREQYEEEQESKAELQRAL 1368
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGVK--ALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1369 SKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVED 1434
Cdd:TIGR02168 544 GGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1435 LMLDV----------------------------------------ERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1474
Cdd:TIGR02168 621 LLGGVlvvddldnalelakklrpgyrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1475 EASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEA 1554
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1555 EASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRvVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEI 1634
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1635 QLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELL 1714
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1715 DASERVQLLHTQNTSLINTKK-KLETDISQIQGEMEDIvqearnaeEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKN 1792
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRL--------ENKIKELGPVNLAAiEEYEELKERYDFLTAQKED 1011
|
....*....
gi 1958661053 1793 MEQTVKDLQ 1801
Cdd:TIGR02168 1012 LTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1749 |
2.28e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.17 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKSEAKRKELE------EKMVSLLKEKNDLQLQV-----QAEAEGLADAEERCDQLIKTK 919
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 920 IQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKL 999
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1000 TKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENE 1079
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1080 KQQLDERLKKKEFEMSNLQskIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE- 1158
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDs 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1159 --------EAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAelgeqIDNLQRVKQKLEKEKSE 1230
Cdd:TIGR02168 494 lerlqenlEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1231 MKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQ-----TESGEFSRQLDEKEALV 1305
Cdd:TIGR02168 569 ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvddlDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1306 SQ----------LSRGKQAFTQQIEELKRQLEEevkaknalahalqssrhdcdlLREQYEEEQESKAELQRALSKANSEv 1375
Cdd:TIGR02168 649 TLdgdlvrpggvITGGSAKTNSSILERRREIEE---------------------LEEKIEELEEKIAELEKALAELRKE- 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1376 aqwrtkyetdaiqrTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKqrn 1455
Cdd:TIGR02168 707 --------------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER--- 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1456 fdkiLAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK 1535
Cdd:TIGR02168 770 ----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1536 IKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQlkrnhIRVVESMQSTLDAEIRSR 1615
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE-----LRELESKRSELRRELEEL 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1616 NDAIrikKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEEL 1695
Cdd:TIGR02168 921 REKL---AQLELRLEGLEVRIDNLQERLSE-------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1696 -RATLEqtersrkiAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEME 1749
Cdd:TIGR02168 985 gPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1595 |
2.09e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 122.09 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 930 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQea 1009
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-- 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1010 hqqtlddlqaeedkvNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRK-LEGDLKLAQESIMDIENEKQQLDERLK 1088
Cdd:TIGR02168 400 ---------------NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1089 KKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER------LEEAGG 1162
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyeaaIEAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1163 ATSAQIEMNKKREAefqkmrRDLEEATLQHEATAATL----RKKHADSVAELGEQIDNLQRVKQ---KLEKEKSEMKMEI 1235
Cdd:TIGR02168 545 GRLQAVVVENLNAA------KKAIAFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGvakDLVKFDPKLRKAL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1236 DDLASNVETVSkakgNLekmcrtleDQVSELKSKEEEQQRLI---NDLTTQRGRL-----QTESGEFSRQ--LDEKEALV 1305
Cdd:TIGR02168 619 SYLLGGVLVVD----DL--------DNALELAKKLRPGYRIVtldGDLVRPGGVItggsaKTNSSILERRreIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1306 SQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQY---EEEQESKAELQRALSKANSEVAQWRTKY 1382
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarlEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1383 ETDAIQRTEELEEAKKKLAQRlqaaEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvertNAACAALDKKQRNFDKILAE 1462
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALDELRAELTLL-------NEEAANLRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1463 WKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ 1542
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1543 EKCELQAALEEAEASLEHEEGKILRIQLELN-----------QVKSEIDRKIAEKDEEIDQLKR 1595
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSeeysltleeaeALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
924-1810 |
2.95e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 111.70 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 924 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDETIAK 998
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 999 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAK-IKLEQQVDDLEGSLEQekklrmdlerakrkLEGDLKLAQESIMDIE 1077
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqLRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1078 NEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERL 1157
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1158 EEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhaDSVAELGEQIDNLQRVKQKLEKEKSEMkmeidd 1237
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQLAADLSKYEQEL------ 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1238 lasnvetvskakgnlekmcRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEA-------LVSQLSR 1310
Cdd:TIGR02169 472 -------------------YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1311 GKQAFTQQIEELKRQ------LEEEVKAKNA--LAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKY 1382
Cdd:TIGR02169 533 VGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1383 ETD---AIQRT---EELEEAKKKLAQ-RLQAAE-EHVEAVNA------KCASLEKTKQRLQNEVEDLMLDVERTNAACAA 1448
Cdd:TIGR02169 613 EPAfkyVFGDTlvvEDIEAARRLMGKyRMVTLEgELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1449 LDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGtelfkmknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGK 1528
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE--------------QEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1529 RIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQL-ELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQst 1607
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-- 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1608 ldaEIRSRNDAIRIKKKMEGDlnemeiQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANL 1687
Cdd:TIGR02169 837 ---ELQEQRIDLKEQIKSIEK------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1688 LQAEIEELRATLEQTERSRKIAEQELldaservqllhtqntSLINTKKKLETDISQIQGEMEDiVQEARNAEEKAKKAIT 1767
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEEL---------------SEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALE 971
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1958661053 1768 DAAMMA-EELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQL 1810
Cdd:TIGR02169 972 PVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
855-1436 |
4.72e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 855 EMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAE 934
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 935 DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1014
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1015 DDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEM 1094
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1095 SNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQR---------SDLSRELEEISERLEEAGGATS 1165
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavliGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1166 AQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDnlqRVKQKLEKEKSEMKMEIDDLASNVETV 1245
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1246 SKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQ 1325
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1326 LEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALskansevaqwrtKYETDAIQRTEELEEAKKKLAQRLQ 1405
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA------------LEELPEPPDLEELERELERLEREIE 777
|
570 580 590
....*....|....*....|....*....|....*...
gi 1958661053 1406 -------AAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1436
Cdd:COG1196 778 algpvnlLAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1126-1916 |
6.93e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 110.54 E-value: 6.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1126 EeeieaerasrAKAEKQRsdlsRELEEISERLEEaggatsAQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHAD 1205
Cdd:TIGR02169 169 D----------RKKEKAL----EELEEVEENIER------LDLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1206 SVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQ-QRLINDLTTQR 1284
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1285 GRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1364
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1365 QRalskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtna 1444
Cdd:TIGR02169 384 RD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK---- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1445 acaALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLgtelfkmknayEESLDQLETLKRENKNLQQEISDLTEQIA 1524
Cdd:TIGR02169 452 ---KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-----------QRELAEAEAQARASEERVRGGRAVEEVLK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1525 EGGKRIHELekiKKQVEQEKCELQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE--IDRKIA 1584
Cdd:TIGR02169 518 ASIQGVHGT---VAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErrDLSILS 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1585 EKDE--------EIDQLKRNHIR-------VVESMQS-----------TLDAEI-----------RSRNDAIRIKKKMEG 1627
Cdd:TIGR02169 595 EDGVigfavdlvEFDPKYEPAFKyvfgdtlVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPA 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1628 DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1707
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1708 IAEQELLDASERVQLLHTQNTSLINTKKKLETDIS-----QIQGEMEDIVQE-------ARNAEEKAKKAITDAAMMAEE 1775
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEvsriearLREIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1776 LKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVK 1855
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1856 ELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSkFRKLQHELEEAEER 1916
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1148-1937 |
1.06e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.77 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1148 RELEEISERLEEAggatsaQIEMNKKREaEFQKMRRDLEEAtlqhEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1227
Cdd:TIGR02169 177 EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1228 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQ-QRLINDLTTQRGRLQTESGEFSRQLDEKEALVS 1306
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1307 QLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRalskansEVAQWRTKYEtDA 1386
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLE-KL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1387 IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaALDKKQRNFDKILAEWKQK 1466
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-------KQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1467 YEETHAELEASQKEARSLgtelfkmknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELekiKKQVEQEKCE 1546
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKL-----------QRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGSVGER 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1547 LQAALEEAEAS------LEHEEGKILRIQ------------LELNQVKSE--IDRKIAEKDE--------EIDQLKRNHI 1598
Cdd:TIGR02169 537 YATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratfLPLNKMRDErrDLSILSEDGVigfavdlvEFDPKYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1599 R-------VVESMQSTLDAEIRSRndairiKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQ 1671
Cdd:TIGR02169 617 KyvfgdtlVVEDIEAARRLMGKYR------MVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1672 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkKKLETDISQIQGEMEdi 1751
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------------EELEEDLSSLEQEIE-- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1752 vqearNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKnmEQTVKDLQLRLDEAEqlalkggkKQIQKLEARVRELEG 1831
Cdd:TIGR02169 755 -----NVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQ 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1832 EVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELE 1911
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820
....*....|....*....|....*.
gi 1958661053 1912 EAEERADIAESQVNKLRVKSREVHTK 1937
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1317-1918 |
1.30e-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: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1317 QQIEELKRQ-----------LEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVaqwrtkyetd 1385
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1386 aiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQ 1465
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1466 KYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKC 1545
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1546 ELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRsRNDAIRIKKKM 1625
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1626 EGDLNE------------------MEIQLNHANRMAAEALRNYRNTQGILKDTQlhldDALRGQEDLKEQLAmveRRANL 1687
Cdd:COG1196 504 EGFLEGvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA---GRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1688 LQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTkkkLETDISQIQGEMEDIVQEARNAEEKAKKAIT 1767
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL---LGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1768 DAAMMAEELK--KEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVK 1845
Cdd:COG1196 654 EGGSAGGSLTggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1846 GLRKHERRVKELTYQTEEDRKNILRLQDLvDKLQAKVKSYKRQAEE-------AEEqsntnlskfrklqhELEEAEERAD 1918
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDL-EELERELERLEREIEAlgpvnllAIE--------------EYEELEERYD 798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
985-1870 |
2.18e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 108.62 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 985 LTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEGSLEQEKKLRM----DLE 1056
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLkekeALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1057 RAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIED---EQAIGIQ-----LQKKIKELQARIEELEEE 1128
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgeEEQLRVKekigeLEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1129 IEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEAtlqhEATAATLRKKHADSVA 1208
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1209 ELGE----------QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLIN 1278
Cdd:TIGR02169 393 KLEKlkreinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1279 DLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK----------RQL----EEEVKA-KNALAHALQSS 1343
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvAQLgsvgERYATAiEVAAGNRLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1344 RHDCDLLREQYEEEQESKaELQRA----LSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNakca 1419
Cdd:TIGR02169 553 VVEDDAVAKEAIELLKRR-KAGRAtflpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE---- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1420 SLEkTKQRLQNEVEDLMLD---VERTNAACAALDKKQRNFDKILAEwKQKYEETHAELEASQKEARSLGTELFKMKNAYE 1496
Cdd:TIGR02169 628 DIE-AARRLMGKYRMVTLEgelFEKSGAMTGGSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1497 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEkcelqaaLEEAEASLEHEEGKILRIQLELNQVK 1576
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE-------IENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1577 SEIDRKIAEKDEEIDQLKRNHIRVVEsmqstldaEIRSRNDAIrikkkmegdLNEMEIQLN--HANRMAAEALRNyrntq 1654
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLE--------EEVSRIEAR---------LREIEQKLNrlTLEKEYLEKEIQ----- 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1655 gilkdtqlhldDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTersrkiaEQELLDASERvqllhtqntslintK 1734
Cdd:TIGR02169 837 -----------ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-------EAALRDLESR--------------L 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1735 KKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQtvkdlqlrlDEAEQLALKG 1814
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE---------IPEEELSLED 955
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1815 GKKQIQKLEARVRELEG-------EVESEQKRNVEAVKGLRKHERR---VKELTYQTEEDRKNILR 1870
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKREVFM 1021
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
223-718 |
1.14e-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: 105.98 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 223 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 291
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 292 ITS--NKKPEL----IEMLLITTNPYDYPFVSQGEISVASIDDQEELMATD--------SAIDILGFTNDEKVSIYKLTG 357
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 358 AVMHYGNMKFKQKQREEQAEPDGT---EVADKAAYLQGLNSADLL-KALCYPRVKVGNEYVTKGQTVE--QVTNAVGALA 431
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLeRMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 432 KAMYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLqqFFNH 494
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--YARE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 495 HMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYEQHL--GKSANFQ 567
Cdd:cd14894 567 EQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 568 KPKVVKGKAEAH---------FSLIHYAGTVDYNITGWLDKNKDPL-NETVVGLYQKSSMKTLAYLFSGAQTAEAEASSG 637
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 638 GAAKKGAKKKGSSfQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFP 717
Cdd:cd14894 721 SMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSS 799
|
.
gi 1958661053 718 S 718
Cdd:cd14894 800 S 800
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
842-1539 |
1.35e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 106.29 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 842 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMvsllkekNDLQLQVQAEAEGLADAEERCDQLIKTKIQ 921
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIER 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 922 LEAKIKEVTERAEDEEEINAELtaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTK 1001
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1002 E---KKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAkrkLEGDLklaQESIMDIEN 1078
Cdd:TIGR02168 483 ElaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1079 EKQQLDERLKKKEFEMSNLqskIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSD-LSRELeeISERL 1157
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTF---LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYlLGGVL--VVDDL 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1158 EEA-----------------------GGATSAQIEmnkKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQI 1214
Cdd:TIGR02168 632 DNAlelakklrpgyrivtldgdlvrpGGVITGGSA---KTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKEL 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1215 DNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQrlindltTQRGRLQTESGEF 1294
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE-------ERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1295 SRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSE 1374
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1375 VAQWRTKYETdAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKK-Q 1453
Cdd:TIGR02168 861 IEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiD 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1454 RNFDKILAEWK-------QKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG 1526
Cdd:TIGR02168 940 NLQERLSEEYSltleeaeALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
730
....*....|...
gi 1958661053 1527 GKRIHELEKIKKQ 1539
Cdd:TIGR02168 1020 EEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1142-1755 |
1.59e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1142 QRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHAdSVAELGEQIDNLQRVK 1221
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA-ELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1222 QKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEK 1301
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1302 EALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTK 1381
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1382 YETDA---IQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVE---------RTNAACAAL 1449
Cdd:COG1196 472 AALLEaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEaayeaaleaALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1450 DKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR 1529
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1530 IHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLD 1609
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1610 AEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkdtqlhLDDALRGQEDLKEQLAMVERRANLLQ 1689
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEEL------------------LEEEALEELPEPPDLEELERELERLE 773
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1690 AEIEEL-----RAtleqtersrkiaEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 1755
Cdd:COG1196 774 REIEALgpvnlLA------------IEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1252-1835 |
3.69e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1252 LEKMCRTLEDQVS------ELKSKEEEQQRL-----INDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIE 1320
Cdd:COG1196 198 LERQLEPLERQAEkaeryrELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1321 ELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKL 1400
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE--------LEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1401 AQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKE 1480
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1481 ARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKcelqAALEEAEASLEH 1560
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL----LLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1561 EEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHAN 1640
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1641 RMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAeiEELRATLEQTERSRKIAEQELLDASERV 1720
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA--LRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1721 QLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL 1800
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|....*
gi 1958661053 1801 QLRLDEAEQLALKGGKKQIQKLEARVRELEGEVES 1835
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1435 |
4.30e-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: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 843 IKPLLKSAETEKEMATMKEEFQKTKDELAKseAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLiktKIQL 922
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL---RLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 923 EAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE 1002
Cdd:COG1196 277 EELELELEEAQAEEYELLAEL----ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1003 KKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ 1082
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1083 LDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAeKQRSDLSRELEEISERLEEAGG 1162
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1163 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1242
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1243 E---TVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQI 1319
Cdd:COG1196 592 LargAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1320 EELKRQLEEEVKAKNALAHALQSSRHdcDLLREQYEEEQESKAELQRALSKANSEVAQwRTKYETDAIQRTEELEEAkkk 1399
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEE--- 745
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958661053 1400 LAQRLQAAEEHVEAVNAkcASLEKTKQRLQNEVEDL 1435
Cdd:COG1196 746 ELLEEEALEELPEPPDL--EELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
861-1603 |
6.91e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.07 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 861 EEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEIN 940
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 941 AELTAKKRKLED-ECSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQA 1019
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1020 EEdkvntltKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQS 1099
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1100 KIEDEQAIGIQLQKKIKELQARIEELEeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEfq 1179
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1180 KMRRDLEEATLQ-HEATAATLRKKHADSVAELGEQidnlqrvKQKLEKEKSEMKMEIDDlASNVETVSKAkgnlEKMCRT 1258
Cdd:PTZ00121 1487 EAKKKAEEAKKKaDEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADE-AKKAEEKKKA----DELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1259 LEDQVSELKSKEEEQQRlindlTTQRGRLQTESGEFSRQLDEKEaLVSQLSRGKQAFTQQIEELKRQLEEEVKAKNalAH 1338
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE--LK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1339 ALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAiQRTEEL---EEAKKKLAQRLQAAEEH---VE 1412
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEKKAAEALKKEAEEakkAE 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1413 AVNAKCASLEKTKQRLQNEVEDLMLDVERTnaacaaldKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMK 1492
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1493 NAY-EESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQA-----ALEEAEASLEHEEGKi 1565
Cdd:PTZ00121 1778 EAViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVAdsknmQLEEADAFEKHKFNK- 1856
|
730 740 750
....*....|....*....|....*....|....*...
gi 1958661053 1566 lriqlelNQVKSEIDRKIAEKDEEIDQLKRNHIRVVES 1603
Cdd:PTZ00121 1857 -------NNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1008-1831 |
1.60e-21 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 102.50 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1008 EAHQQTLDDLQAEEDKVNTL-TKAKIKLEQQVDDLEGSLEQ---EKKLRMDLERAKRKLEGDLKlaqesiMDIENEKQQL 1083
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR------NQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1084 DERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQA-----RIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1158
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1159 EAGGAT--------SAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1230
Cdd:pfam15921 235 YLKGRIfpvedqleALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1231 MKMEIDDLASnveTVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLdekEALVSQLSR 1310
Cdd:pfam15921 315 YMRQLSDLES---TVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADLHK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1311 GKQAFTQQIEELKRQLEEEVKAKNALAHalqssrhdcdllreqyeeeqeskaeLQRALSKANSEVaqwrtkyetdaiQRT 1390
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDH-------------------------LRRELDDRNMEV------------QRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1391 EELEEAKKKLAQ--------RLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLmldvertNAACAALDKKQRNFDKILAE 1462
Cdd:pfam15921 432 EALLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTVSDLTAS 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1463 WKQKyeethaeleasQKEARSLGTELFKMKNAYEESLDQLETLKREN---KNLQQEISDLTEQIAEGGKRIhelEKIKKQ 1539
Cdd:pfam15921 505 LQEK-----------ERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVI---EILRQQ 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1540 VEQ------EKCELQAALEEAEASLEHE-EGKILRIQlELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLdaei 1612
Cdd:pfam15921 571 IENmtqlvgQHGRTAGAMQVEKAQLEKEiNDRRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERL---- 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1613 RSRNDairIKKKMEGDLNEMEIQLNHANRMAAE---ALRNYRNTQGILKDTqlhlddalrgQEDLKEQLAMVerranllQ 1689
Cdd:pfam15921 646 RAVKD---IKQERDQLLNEVKTSRNELNSLSEDyevLKRNFRNKSEEMETT----------TNKLKMQLKSA-------Q 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1690 AEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDA 1769
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1770 AMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQ-KLEAR--VRELEG 1831
Cdd:pfam15921 786 NKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRlKLQHTldVKELQG 850
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
837-1442 |
3.13e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.67 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 837 MKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAeercdqlI 916
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 917 KTKIQLEAKIKEVTERAEDEEEINAELTAKKRKL-EDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEEMAGLDET 995
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 996 IAKLTKEKKALQEAHQqtlddlQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEgdlklaqesimd 1075
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAE------------ 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1076 ienEKQQLDERLKKKEFEMSNLQSKIEDEQAigiqlQKKIKELQarieeleeeieAERASRAKAEKQRSDLSRELEEISE 1155
Cdd:PTZ00121 1468 ---EAKKADEAKKKAEEAKKADEAKKKAEEA-----KKKADEAK-----------KAAEAKKKADEAKKAEEAKKADEAK 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1156 RLEEAGGATSAQIEMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNlQRVKQKLEKEKSEMKM 1233
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1234 EIDDLASNVETVSKAKgnlekmcrtledqvsELKsKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQ 1313
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAE---------------ELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1314 AFTQQIEELKRQLEEEVKAKNALAHALQSSRhDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAiQRTEEL 1393
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEA 1749
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1394 ---EEAKKKLAQRLQAAEEHVEAVNAKCASLekTKQRLQNEVEDLMLDVERT 1442
Cdd:PTZ00121 1750 kkdEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
851-1540 |
5.13e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMAtmkeefqKTKDELAKSEAKRKELEEKMVSLLKEKNDLQ--LQVQAEAEgLADAEERCDQLIktkiQLEAKIKE 928
Cdd:COG1196 176 EAERKLE-------ATEENLERLEDILGELERQLEPLERQAEKAEryRELKEELK-ELEAELLLLKLR----ELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 929 VTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQE 1008
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1009 AHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLK 1088
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1089 KKEfemsnlqskiedeqaigIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQI 1168
Cdd:COG1196 404 ELE-----------------EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1169 EmnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKsemkmEIDDLASNVETVSKA 1248
Cdd:COG1196 467 E--LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG-----AVAVLIGVEAAYEAA 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1249 KGNlekmcRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTEsgefsRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEE 1328
Cdd:COG1196 540 LEA-----ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATF-----LPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1329 EVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAE 1408
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1409 EHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTEL 1488
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1489 FKMKNAYEE-------SLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQV 1540
Cdd:COG1196 770 ERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
844-1381 |
4.83e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 94.36 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 844 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQlqvqAEAEGLADAEERCDQLIKTKIQLE 923
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 924 AKIKEVTERAEDEEEINAELTAKKRKLE------DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 997
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 998 KLTKEKKALQEahqqTLDDLQAEEDKVNTLTKAKIKLEQ--QVDDLEGSLEQEKKLRM--DLERAKRKLEGDLKLAQESI 1073
Cdd:PRK03918 339 RLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1074 MDIENEKQQLD---ERLKKKEFEMSNLQSKIEDEQAIGIqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE- 1149
Cdd:PRK03918 415 GELKKEIKELKkaiEELKKAKGKCPVCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEs 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1150 ----LEEISERLEEAGGATSA-QIEMNKKREAEFQKMRRDLEEATLQHEATaatlrKKHADSVAELGEQIDNLQRVKQKL 1224
Cdd:PRK03918 494 elikLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSL-----KKELEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1225 EKEKSEMKMEIDDLA-SNVETVSKAKGNLEKMCR---TLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDE 1300
Cdd:PRK03918 569 EEELAELLKELEELGfESVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1301 KEALVSQLSRGKQaftQQIEELKRQLEEEVKAKNALAHALQSSRH----DCDLLREQYEEEQESKAELQRaLSKANSEVA 1376
Cdd:PRK03918 649 LEELEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREeikkTLEKLKEELEEREKAKKELEK-LEKALERVE 724
|
....*
gi 1958661053 1377 QWRTK 1381
Cdd:PRK03918 725 ELREK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
850-1462 |
6.82e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 930 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDETIAKLTKE 1002
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1003 K----KALQEAHQQTLDDLQAEED--------------------------KVNTLTKAKIKLEQQVDDLEGSLEQEKKLR 1052
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1053 -------------MDLERAKR--------KLEGDL--------------KLAQESIMDIENEKQQLDERLKKKEFEMSNL 1097
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1098 QSKIEdeqaigiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAE 1177
Cdd:TIGR02169 694 QSELR-------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1178 FQKMRRDLEEATLQHEATAATLRkkhadsvaelGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCR 1257
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLS----------HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1258 TLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEevkaknala 1337
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE--------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1338 halqssrhdcdlLREQYEEEQESKAELQRALSKANSEVAQ-----WRTKYETDAIQRTEELEEAKKKLAQRLQA------ 1406
Cdd:TIGR02169 908 ------------LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnm 975
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1407 -AEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTN-----AACAALDKKQRNFDKILAE 1462
Cdd:TIGR02169 976 lAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEkkkreVFMEAFEAINENFNEIFAE 1037
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
851-1640 |
1.64e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQlEAKIKEVT 930
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 931 ERAEDEEEINAeltAKKRKLEDECSELKKDIDDLELTLA-KVEKEKHATENKV---KNLTEEMAGLDETIAKLTKEKKAL 1006
Cdd:PTZ00121 1170 RKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1007 QEAHQQTLDDLQAEEDKVNTLTKAKIKLEQ--QVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESIMDIENEKQQLD 1084
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1085 ERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAE--KQRSDLSRELEEISERLEEagg 1162
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEE--- 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1163 aTSAQIEMNKKREAEFQK---MRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKsemkmEIDDLA 1239
Cdd:PTZ00121 1403 -DKKKADELKKAAAAKKKadeAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK-----KADEAK 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1240 SNVETVSKAKgNLEKMCRTLEDQVSELKSKEEEQQRlindlttqrgrlqtesGEFSRQLDEKEAlVSQLSRGKQAftQQI 1319
Cdd:PTZ00121 1477 KKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKK----------------ADEAKKAEEAKK-ADEAKKAEEA--KKA 1536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1320 EELKRQleEEVKAKNALAHALQSSRHDcdllrEQYEEEQESKAELQRALSKANSEVAQwrtkyetdaiqrteELEEAKKK 1399
Cdd:PTZ00121 1537 DEAKKA--EEKKKADELKKAEELKKAE-----EKKKAEEAKKAEEDKNMALRKAEEAK--------------KAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1400 LAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQK 1479
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK 1675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1480 EARSLgtelfkmKNAYEESLDQLETLKREnknlqqeisdlteqiAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLE 1559
Cdd:PTZ00121 1676 KAEEA-------KKAEEDEKKAAEALKKE---------------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1560 HeegkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHA 1639
Cdd:PTZ00121 1734 E-----AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
.
gi 1958661053 1640 N 1640
Cdd:PTZ00121 1809 N 1809
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
970-1870 |
1.78e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 92.73 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 970 KVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAhqqtlDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEK 1049
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET-----ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1050 KLRmdLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEI 1129
Cdd:pfam02463 218 KLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1130 EAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAE 1209
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1210 LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQT 1289
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1290 ESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALS 1369
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1370 KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEhVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAAL 1449
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT-ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1450 DKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNA-----YEESLDQLETLKRENKNLQQEISDLTEQIA 1524
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaeKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1525 EGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNhirvVESM 1604
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK----EEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1605 QSTLDAEIRSRNDAIRIKKKMEGDLNEmeiqlnhANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERR 1684
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKE-------EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1685 ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETdisqIQGEMEDIVQEARNAEEKAKK 1764
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK----EKEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1765 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAV 1844
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890 900
....*....|....*....|....*.
gi 1958661053 1845 KGLRKHERRVKELTYQTEEDRKNILR 1870
Cdd:pfam02463 996 EKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1174-1918 |
6.79e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1174 REAEFQKMRRDLEEATLQHEATAATLRKKHADSVAElgeqidnlqrvkqklEKEKSEMKMEIDDLASNVETVSKAKG--N 1251
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAE---------------EARKAEEAKKKAEDARKAEEARKAEDarK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1252 LEKMCRTLEDQVSELKSKEEEQQRLindlTTQRGRLQTESGEFSRQLDEkealVSQLSRGKQAFTQQIEELKRQLEEEVK 1331
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKA----EEARKAEDAKKAEAARKAEE----VRKAEELRKAEDARKAEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1332 AKNALAHALQSSRHDCDLLREQYEEEQESK-AELQRAlskaNSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEH 1410
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEK 1289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1411 VEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaaLDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELfk 1490
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA-- 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1491 mkNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKilriql 1570
Cdd:PTZ00121 1360 --EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK------ 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1571 elnqvKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNY 1650
Cdd:PTZ00121 1432 -----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1651 RNTQgilKDTQLHLDDALRGQEDLKEqlAMVERRANLLQAEIEELRA-TLEQTERSRKIAEQELLDASERVQllHTQNTS 1729
Cdd:PTZ00121 1507 EAKK---KADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAE--EDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1730 LINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL-QLRLDEAE 1808
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeELKKAEEE 1658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1809 QLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQ 1888
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
730 740 750
....*....|....*....|....*....|...
gi 1958661053 1889 AEEAE---EQSNTNLSKFRKLQHELEEAEERAD 1918
Cdd:PTZ00121 1739 AEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1629-1930 |
1.18e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1629 LNEMEIQLNHANRMAAEALRnYRNTQGILKDTQLHLddALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI 1708
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1709 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1788
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1789 MKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEgEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNI 1868
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1869 LRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVK 1930
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1016-1800 |
1.32e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1016 DLQAEEDKVNTLT--KAKIKLEQQVDDLEGSLEQEKKLrmdlERAKRKLEgDLKLAQESIMdiENEKQQLDERLKKKEFE 1093
Cdd:PTZ00121 1080 DFDAKEDNRADEAteEAFGKAEEAKKTETGKAEEARKA----EEAKKKAE-DARKAEEARK--AEDARKAEEARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1094 MSNLQSKIEDEQAIGIQLQ----KKIKELQARIEELEEEIEAERASRAKAEK-QRSDLSRELEEISERLEEAGGATSAQI 1168
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKaedaKKAEAARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1169 EMNKKREAEFQKMR--RDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQR---VKQKLEKEKSEMKMEIDDLASNVE 1243
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1244 TVSKAKgNLEKMCRTLEDQVSELKSKEEEQQRLINdltTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQaftqQIEELK 1323
Cdd:PTZ00121 1313 EAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK----KADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1324 RQLEEEVKAKNALAHAlQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAiqrteelEEAKKKLAQR 1403
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-------DEAKKKAEEA 1456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1404 LQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKilAEWKQKYEETHAELEASQKEARS 1483
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEEAKKADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1484 LGTELFKMknayEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEK--IKKQVEQEKCELQAALEEAEASLEHE 1561
Cdd:PTZ00121 1535 KADEAKKA----EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1562 EGKilriQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDlnemeiqlnhanR 1641
Cdd:PTZ00121 1611 EAK----KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED------------K 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1642 MAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSrkiAEQElldaservq 1721
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEED--------- 1742
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1722 llhtqntslintKKKLEtDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmkknMEQTVKDL 1800
Cdd:PTZ00121 1743 ------------KKKAE-EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME-----VDKKIKDI 1803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
979-1637 |
2.17e-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: 88.54 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 979 ENKVKNLTEEMAGLDETIAKLTKEKKALQEahqqtlDDLQAEEDKVNTLTKAKIkLEQQVDDLEGSLEQEKKLRMDLERA 1058
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDK------NLNKDEEKINNSNNKIKI-LEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1059 KRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAK 1138
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1139 AEKQRSDLSRELEEISERLeeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQ 1218
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1219 RVKQKLEKEKSEMKMEIDDLASNVETVSkakgNLEKMCRTLEDQVSELKSkeEEQQRLINDLTTQRGRLQTESGEFSRQL 1298
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIK----ELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1299 DEKEALVSQLsrgkqafTQQIEELKRQLEEevkaknalahalqssrhdcdlLREQYEEEQESKAELQRALSKANSEVAQW 1378
Cdd:TIGR04523 331 SQNNKIISQL-------NEQISQLKKELTN---------------------SESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1379 RtkyetdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDK 1458
Cdd:TIGR04523 383 K--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1459 ILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKK 1538
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1539 QVEQEKCELQAALEEAEASLEHE--EGKILRIQLELNQVKSEID---RKIAEKDEEIDQLKRNhIRVVESMQSTLDAEIR 1613
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKslkKKQEEKQELIDQKEKE-KKDLIKEIEEKEKKIS 613
|
650 660
....*....|....*....|....
gi 1958661053 1614 SRNDAIRIKKKMEGDLNEMEIQLN 1637
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIK 637
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
851-1334 |
4.16e-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: 87.77 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQL------IKTKIQ--- 921
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQknk 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 922 -LEAKI-----------KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEM 989
Cdd:TIGR04523 215 sLESQIselkkqnnqlkDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 990 AGLDETIAKLTKEKKalQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLA 1069
Cdd:TIGR04523 291 NQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1070 QESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE 1149
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1150 LEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQheataatlrkkhadsVAELGEQIDNLQRVKQKLEKEKS 1229
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE---------------LKSKEKELKKLNEEKKELEEKVK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1230 EMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQV---------SELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDE 1300
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
490 500 510
....*....|....*....|....*....|....
gi 1958661053 1301 KEALVSQLSRGKQAFTQQIEELKRQLeEEVKAKN 1334
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
904-1541 |
1.11e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 904 GLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKhateN 980
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEV----K 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 981 KVKNLTEEMAGLDETIAKLTKEKKALQEahqqtldDLQAEEDKVNTLTKAKIKLEQQVDDLEgSLEQEKKLRMDLERAKR 1060
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1061 KLEgdlklaqesimdienekqqldERLKKKEFEMSNLQSKIEDeqaigiqLQKKIKELqarieeleeeieaerasrakae 1140
Cdd:PRK03918 304 EYL---------------------DELREIEKRLSRLEEEING-------IEERIKEL---------------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1141 kqrSDLSRELEEISERLEEAggatsaqiemnKKREAEFQKMRRDLEEAtLQHEATAATLRKKHAD-SVAELGEQIDNLQR 1219
Cdd:PRK03918 334 ---EEKEERLEELKKKLKEL-----------EKRLEELEERHELYEEA-KAKKEELERLKKRLTGlTPEKLEKELEELEK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1220 VKQKLEKE-------KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQ---------VSELKSKEEEQQRLINDLTTQ 1283
Cdd:PRK03918 399 AKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelleeyTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1284 RGRLqtesgefsRQLDEKEALVSQLSRGKQaFTQQIEELKRQLE----EEVKAKNALAHALQSS----RHDCDLLREQYE 1355
Cdd:PRK03918 479 RKEL--------RELEKVLKKESELIKLKE-LAEQLKELEEKLKkynlEELEKKAEEYEKLKEKliklKGEIKSLKKELE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1356 EEQE---SKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAqrlQAAEEHVEAVNAkcaslEKTKQRLQNEV 1432
Cdd:PRK03918 550 KLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE---PFYNEYLELKDA-----EKELEREEKEL 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1433 EDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYeethaeleaSQKEARSLGTELFKMKNAYEESLDQLETLKRENKNL 1512
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKY---------SEEEYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
650 660
....*....|....*....|....*....
gi 1958661053 1513 QQEISDLTEQIAEGGKRIHELEKIKKQVE 1541
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1080-1856 |
1.43e-16 |
|
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: 86.33 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1080 KQQLDERLKKKEFEMSNLQSKIEDEQAIG-----------IQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR 1148
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHekqkfylrqsvIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1149 ELEEISERLEEAGGATSAQIEMNKK----REAEFQKMRR---DLEEATLQHEATAATLRKKHADSvaeLGEQIDNLQRvk 1221
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSilvDFEEASGKKIYEHDSMSTMHFRS---LGSAISKILR-- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1222 qKLEKEKSEMKMEIDDLASNVETV-SKAKGNLEKMCRTLEDQVSELKSKEEEQqrlINDLTTQRGRLQTESGEFSRQLde 1300
Cdd:pfam15921 228 -ELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEVE---ITGLTEKASSARSQANSIQSQL-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1301 kEALVSQLSRGKQAFTQQIEELKRQLEEevkaknalahaLQSSrhdcdlLREQYEEEQESKAELQRALSKANSEVAQWRT 1380
Cdd:pfam15921 302 -EIIQEQARNQNSMYMRQLSDLESTVSQ-----------LRSE------LREAKRMYEDKIEELEKQLVLANSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1381 KYETDAiQRTEELEEAKKKLAQRLQAAEEHVeavnakcaSLEKTKQR---------------LQNEVEDLMLDVERTNAA 1445
Cdd:pfam15921 364 ERDQFS-QESGNLDDQLQKLLADLHKREKEL--------SLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1446 CAALDKK-QRNFDKILAEWKQKYEethaeleaSQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIA 1524
Cdd:pfam15921 435 LKAMKSEcQGQMERQMAAIQGKNE--------SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1525 EGGKRIH----ELEKIKKQVEQEKCELQaaleeaeaSLEHEEGKILRIQLELNQVKSEIdrkiAEKDEEIDQLKRNhirv 1600
Cdd:pfam15921 507 EKERAIEatnaEITKLRSRVDLKLQELQ--------HLKNEGDHLRNVQTECEALKLQM----AEKDKVIEILRQQ---- 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1601 VESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALR-GQEDLKEQLA 1679
Cdd:pfam15921 571 IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNaGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1680 MVERRANLLQaEIEELRATLEQTERSRKIAEQELLDASERVQLlhtqntslinTKKKLETDISQIQGEMEDIVQEARNAE 1759
Cdd:pfam15921 651 IKQERDQLLN-EVKTSRNELNSLSEDYEVLKRNFRNKSEEMET----------TTNKLKMQLKSAQSELEQTRNTLKSME 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1760 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrldeAEQLALKGGKKQIQKlearvrELEgEVESEQKR 1839
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAN-----KEKHFLKEEKNKLSQ------ELS-TVATEKNK 787
|
810
....*....|....*..
gi 1958661053 1840 NVEAVKGLRKHERRVKE 1856
Cdd:pfam15921 788 MAGELEVLRSQERRLKE 804
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
846-1584 |
1.59e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 86.18 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 846 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLqvqaeaeglaDAEERCDQLIKTKIQLEAK 925
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL----------CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 926 IKEVTERAEDEEEINAELTAKKRKLEDECSELKkdiddlELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1005
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ------LLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1006 LQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDlEGSLEQEKKLRMDLERAKRKLEgDLKLAQESIMDIENEKQQLDE 1085
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1086 RLKKKEFEMSNLQSKIEDEQAIGIQLQkkikELQARIEELEEEIEAERASRAKAEKQRsdlsrELEEISERLEEAGGATS 1165
Cdd:TIGR00618 380 HIHTLQQQKTTLTQKLQSLCKELDILQ----REQATIDTRTSAFRDLQGQLAHAKKQQ-----ELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1166 AQIEmnKKREAEFQKMRRDLEEATlQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLA------ 1239
Cdd:TIGR00618 451 AQCE--KLEKIHLQESAQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDnpgplt 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1240 -------SNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGK 1312
Cdd:TIGR00618 528 rrmqrgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1313 QAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLL--REQYE-----EEQESKAELQRALSKANSEVAQWRTKYETD 1385
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtaLHALQltltqERVREHALSIRVLPKELLASRQLALQKMQS 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1386 AIQRT----EELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM-----LDVERTNAACAALDKKQRNF 1456
Cdd:TIGR00618 688 EKEQLtywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNqslkeLMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1457 DKILAEWK--QKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKR-ENKNLQQEISDLTEQIAEGGKRIHEL 1533
Cdd:TIGR00618 768 EEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1534 EKIKKQVEQEKCELQAALEEaEASLEHEEGKILRIQLELNQVKSEIDRKIA 1584
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQE-QAKIIQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1077-1768 |
1.70e-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: 85.84 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1077 ENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1156
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1157 LEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEID 1236
Cdd:TIGR04523 112 IK-------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1237 DLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEqqrlINDLTTQRGRLQTESGEFSRQLDEKEALVSQLsrgkqafT 1316
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEINEKTTEISNT-------Q 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1317 QQIEELKrqlEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEvaqWRTKYETDAIQRTEELEEA 1396
Cdd:TIGR04523 253 TQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1397 KKKLAQRLQAAEEhveaVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEA 1476
Cdd:TIGR04523 327 QNQISQNNKIISQ----LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1477 SQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA 1556
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1557 SLEHEEGKILRIQ---LELNQVKSEIDRKIAEKDEEIDQLKRNhIRVVESMQSTLDAEIRSRNDAIrIKKKMEGDLNEME 1633
Cdd:TIGR04523 483 NLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1634 IQLNHANRMAAEalrnyrntqgiLKDTQLHLDDAlrgQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1713
Cdd:TIGR04523 561 KEIDEKNKEIEE-----------LKQTQKSLKKK---QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1714 LDaservqlLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITD 1768
Cdd:TIGR04523 627 EK-------LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
860-1432 |
6.69e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.94 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 860 KEEFQKTKDELAKSEAKrkELEEKMVSLLKEKNDLQlqvqaeaEGLADAEERCDQLIKTKIQLEAKIKEVTERAEdeeei 939
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEK--DLHERLNGLESELAELD-------EEIERYEEQREQARETRDEADEVLEEHEERRE----- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 940 naeltakkrkledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEkKALQEAHQQTLDDLQA 1019
Cdd:PRK02224 252 -------------ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1020 EedkvntltkakikLEQQVDDLEGSLEQEkklRMDLERAKRKLEGdlklAQESIMDIENEKQQLDERLKKKEFEMSNLQS 1099
Cdd:PRK02224 318 E-------------LEDRDEELRDRLEEC---RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEARE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1100 KIEDEQAIGIQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISERLEEAGGATsaqiemnKKREAEFQ 1179
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERF--------------GDAPVDLGNAEDFLEELREERDELRERE-------AELEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1180 KMRRDLEEA-TLQHEATAATLRKK-----HADSVAELGEQIDnlqrvkqKLEKEKSEMKMEIDDLASNVETVSKAKgNLE 1253
Cdd:PRK02224 437 TARERVEEAeALLEAGKCPECGQPvegspHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLV-EAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1254 KMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAK 1333
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1334 NALAH------ALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIqrteelEEAKkklaQRLQAA 1407
Cdd:PRK02224 589 ESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI------EEAR----EDKERA 658
|
570 580
....*....|....*....|....*
gi 1958661053 1408 EEHVEAVNAKCASLEKTKQRLQNEV 1432
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDLQAEI 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1317-1921 |
8.56e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1317 QQIEELKRQLEEEVKAKNALAHALQssrhdcdlLREQYEEEQESKAELQRALSKANSEVAQwrTKYETdAIQRTEELEEA 1396
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1397 KKKLAQRLQAAEEHVEAVNAKCASLEKtkQRLQN---EVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAE 1473
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEA--QIRGNggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1474 LEASQKEARSLGTELFKMKNAYEESLDQLETLKREnknLQQEISDLTEQIAEggkriheLEKIKKQVEQEkceLQAALEE 1553
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIAS-------LERRKSNIPAR---LLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1554 AEASLEHEEGKiLRIQLELNQVKSEID--RKIAEK-----------DEE--------IDQLKRNHIRVVESMQSTLDAEI 1612
Cdd:COG4913 449 LAEALGLDEAE-LPFVGELIEVRPEEErwRGAIERvlggfaltllvPPEhyaaalrwVNRLHLRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1613 RSRNDAIRIKKKMEGDLNEMEIQLNH--ANRMA------AEALRNYRntQGILKDTQLH-------LDDALRGQEDL--- 1674
Cdd:COG4913 528 RPRLDPDSLAGKLDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKgngtrheKDDRRRIRSRYvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1675 ---KEQLAMVERRANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQLLHTQntslintkkklETDISQIQGEMEDI 1751
Cdd:COG4913 606 fdnRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWD-----------EIDVASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1752 vqearnaeekakkaitdaammAEELKKEQDTSAHLERMkknmEQTVKDLQLRLDEAEQlALKGGKKQIQKLEARVRELEG 1831
Cdd:COG4913 674 ---------------------EAELERLDASSDDLAAL----EEQLEELEAELEELEE-ELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1832 EVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKnilRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKlQHELE 1911
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEERIDALRARLNRAEEELERAMRAFNR-EWPAE 803
|
650
....*....|
gi 1958661053 1912 EAEERADIAE 1921
Cdd:COG4913 804 TADLDADLES 813
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
851-1707 |
2.04e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 82.71 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKS-------EAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLE 923
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIidleelkLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 924 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAG-LDETIAKLTKE 1002
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEkLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1003 KKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ 1082
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1083 LDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEagg 1162
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ--- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1163 atsaqiEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDnlqRVKQKLEKEKSEMKMEIDDLASNV 1242
Cdd:pfam02463 484 ------EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR---LGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1243 ETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQ-------RGRLQTESGEFSRQLDEKEALVSQLSRGKQAF 1315
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidpiLNLAQLDKATLEADEDDKRAKVVEGILKDTEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1316 TQQIEELKRqLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEE 1395
Cdd:pfam02463 635 TKLKESAKA-KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1396 AKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaALDKKQRNFDKILAEWKQKYEETHAELE 1475
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1476 ASQKEARSLGTEL-FKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEA 1554
Cdd:pfam02463 787 KVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1555 EASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTL--DAEIRSRNDAIRIKKKMEGDLNEM 1632
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEerIKEEAEILLKYEEEPEELLLEEAD 946
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1633 EIQLNHANRMAAEaLRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1707
Cdd:pfam02463 947 EKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1033-1704 |
4.81e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.50 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1033 KLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESIMDIENEKQQLDErlkkkefemsnLQSKIEDEQAigiq 1110
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEY-----------LRAALRLWFA---- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1111 lQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIE-----MNKKRE------AEFQ 1179
Cdd:COG4913 287 -QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1180 KMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL------- 1252
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparllal 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1253 -EKMCRTLEDQVSEL---------KSKEEEQQRLIND-LTTQRGRLQTEsgefSRQLDEKEALVSQLSRGKQAFTQQIEE 1321
Cdd:COG4913 446 rDALAEALGLDEAELpfvgelievRPEEERWRGAIERvLGGFALTLLVP----PEHYAAALRWVNRLHLRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1322 LKRQLEEEVKAKNALAHALQSSRHDC-DLLREQYEEEQ-----ESKAELQRA--------LSKANSEVAQ------WRTK 1381
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1382 YET--DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQN--EVEDLMLDVERTNAACAALDKKQRNFD 1457
Cdd:COG4913 602 YVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1458 K---ILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISdlTEQIAEGGKRIHELe 1534
Cdd:COG4913 682 AssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAA- 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1535 KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQV----KSEIDRKIAE-------------------KDEEID 1591
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREwpaeTADLDADLESlpeylalldrleedglpeyEERFKE 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1592 QLKRNHIRVVESMQSTLDAEIRsrndaiRIKKKMEgDLNEM----------EIQLnHANRMAAEALRNYRNtqgilkdtq 1661
Cdd:COG4913 839 LLNENSIEFVADLLSKLRRAIR------EIKERID-PLNDSlkripfgpgrYLRL-EARPRPDPEVREFRQ--------- 901
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1958661053 1662 lHLDDALRGQEDLKEQLAmvERRANLLQAEIEELRATLEQTER 1704
Cdd:COG4913 902 -ELRAVTSGASLFDEELS--EARFAALKRLIERLRSEEEESDR 941
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1273 |
6.52e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 841 FKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKR---KELEEKMVSLLKEKNDLQLQVQAEAEGLADAEE----RCD 913
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 914 QLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATENKVKNLTEE 988
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKELLEEYTAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 989 MAGLDETIAKLTKEKKALqEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEG----SLEQEKKLRMDLERAKRKLEG 1064
Cdd:PRK03918 461 LKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1065 DLKLAQ---ESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGI-QLQKKIKELQARIEELEEEIEAERASRAKaE 1140
Cdd:PRK03918 540 EIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELKDAEKELERE-E 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1141 KQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATaaTLRKKHADSVAELGEqidnlqrv 1220
Cdd:PRK03918 619 KELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEE-------- 684
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1221 kqkLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLED------QVSELKSKEEEQ 1273
Cdd:PRK03918 685 ---LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERveelreKVKKYKALLKER 740
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
903-1840 |
1.03e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.40 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 903 EGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenk 981
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL----- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 982 vknlteemagLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRK 1061
Cdd:pfam02463 235 ----------NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1062 LEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEK 1141
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1142 QRSDLSRELEEISERLEEaggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVK 1221
Cdd:pfam02463 385 RLSSAAKLKEEELELKSE------------EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1222 QKLEKEKSEMKmeiddlasnvetvskakgnlekmCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEK 1301
Cdd:pfam02463 453 LEKQELKLLKD-----------------------ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1302 EALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALqssrhdCDLLREQYEEEQESKAELQRALSKANSEVAQWRTK 1381
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA------VIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1382 YETDaiqRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILA 1461
Cdd:pfam02463 584 IPKL---KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1462 EWKQKYEETHAELEASQKEARslgtelfkmKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVE 1541
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQEL---------QEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1542 QEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRsRNDAIRI 1621
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL-RALEEEL 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1622 KKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQ 1701
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1702 TERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAItdaamMAEELKKEQD 1781
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRL 965
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1782 TSAHLERMKKNMEQtvkDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRN 1840
Cdd:pfam02463 966 LLAKEELGKVNLMA---IEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1434 |
2.19e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.06 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 847 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQaEAEGLADAEERCDQLIKTKI-QLEAK 925
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ-DTQELLQEETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 926 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1005
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1006 LQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQ------------------------------------------------- 1036
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlaeekaisaryaeerdraeaeareketralslaraleealeakeeler 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1037 -------QVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIE-DEQAIG 1108
Cdd:pfam01576 658 tnkqlraEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARD 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1109 IQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEA 1188
Cdd:pfam01576 738 EQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEA 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1189 TLQHEATAATLR---KKHADSVAE---LGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKgnlekmcRTLEDQ 1262
Cdd:pfam01576 818 RASRDEILAQSKeseKKLKNLEAEllqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEK-------RRLEAR 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1263 VSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQL-EEEVKAKNALAHALQ 1341
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIA 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1342 SSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETD---AIQRTEELEEAK---KKLAQRLQAAEEHVEAVN 1415
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDErrhADQYKDQAEKGNsrmKQLKRQLEEAEEEASRAN 1050
|
650
....*....|....*....
gi 1958661053 1416 AkcaslekTKQRLQNEVED 1434
Cdd:pfam01576 1051 A-------ARRKLQRELDD 1062
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
850-1616 |
2.36e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.25 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 930 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEA 1009
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1010 HQ--QTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERL 1087
Cdd:pfam02463 435 EEesIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1088 KKKEFEMSNLQSKIEDEQAIGIQLQKkiKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1167
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1168 IEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQ--IDNLQRVKQKLEKEKSEMKMEIDDLASNVETV 1245
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1246 SKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQ 1325
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1326 LEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1405
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1406 AAEEHVEAVnakcaSLEKTKQRLQNEVEDLMLDVERTNAACAA---LDKKQRNFDKILAEWKQKYEETHAELEASQKEAR 1482
Cdd:pfam02463 833 EELEELALE-----LKEEQKLEKLAEEELERLEEEITKEELLQellLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1483 SLGTELFKMKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIH--ELEKIKKQVEQEKCELQAALEEAEASLEH 1560
Cdd:pfam02463 908 KLNLLEEKEN--EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNkeEEEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1561 EEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRN 1616
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLE 1041
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
842-1278 |
3.14e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 842 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQlqvqaEAEGLADAEERCDQLIKTKIQ 921
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK-----KAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 922 L----EAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDiddlELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 997
Cdd:PTZ00121 1586 AkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 998 KLTKEKKALQEAHQQTLDDLQAEEDKVntltkakiKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIE 1077
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEK--------KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1078 NEKQQLDERLKKKEfemsnlQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEI---S 1154
Cdd:PTZ00121 1734 EAKKEAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnF 1807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1155 ERLEEAGGATSAQIEMNKKRE-------AEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKE 1227
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEdsaikevADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1228 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLIN 1278
Cdd:PTZ00121 1888 DEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1024-1632 |
3.78e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1024 VNTLTKAKIKLEQQ-VDDLE--GSLEQEKK----LRMDLERAKRKLEGDLKLAQESIMDIEneKQQLDERLKKKEFEMSN 1096
Cdd:PRK02224 140 VNKLINATPSDRQDmIDDLLqlGKLEEYRErasdARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1097 LQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEA----------ERASRAKAEKQRSDLSRELEEISERLEEAGGATSA 1166
Cdd:PRK02224 218 LDEEIERYEEQREQARETRDEADEVLEEHEERREEletleaeiedLRETIAETEREREELAEEVRDLRERLEELEEERDD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1167 QIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVS 1246
Cdd:PRK02224 298 LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA-AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1247 KAkgnlekmCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEElKRQL 1326
Cdd:PRK02224 377 EA-------VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEE-AEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1327 EEEVKAKNAlAHALQSSRHDCDLlreqyEEEQESKAELQRALSKANSEVAQWRTKYET-----DAIQRTEELEEAKKKLA 1401
Cdd:PRK02224 449 LEAGKCPEC-GQPVEGSPHVETI-----EEDRERVEELEAELEDLEEEVEEVEERLERaedlvEAEDRIERLEERREDLE 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1402 QRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEdlmldvERTNAACAALDKKQRNFDKIlAEWKQKYEETHAELEASQKEA 1481
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAELEAEAE------EKREAAAEAEEEAEEAREEV-AELNSKLAELKERIESLERIR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1482 RSLgtelfkmkNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEkikKQVEQEKCE-LQAALEEAEASLEH 1560
Cdd:PRK02224 596 TLL--------AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELE---AEFDEARIEeAREDKERAEEYLEQ 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1561 EEGKILR-------IQLELNQVKSEIDRkIAEKDEEIDQLKRNHIRV---------VESMQSTLDAEIRSRNDAirikkK 1624
Cdd:PRK02224 665 VEEKLDElreerddLQAEIGAVENELEE-LEELRERREALENRVEALealydeaeeLESMYGDLRAELRQRNVE-----T 738
|
....*...
gi 1958661053 1625 MEGDLNEM 1632
Cdd:PRK02224 739 LERMLNET 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1389-1925 |
8.40e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 8.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1389 RTEELEEakKKLAQRLQAAEEHVEAVNAKCASLEKTKQRlqneVEDLmldvERTNAACAALDKKQRNFDKilaewkQKYE 1468
Cdd:COG4913 214 REYMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQ----IELL----EPIRELAERYAAARERLAE------LEYL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1469 ETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE-GGKRIHELEKIKKQVEQEKCE- 1546
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEEr 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1547 ------LQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNH-------------IRVVESMQST 1607
Cdd:COG4913 358 errrarLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALrdlrrelreleaeIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1608 LDAEIRSRNDAIRIK-KKMEGDL----NEMEIQLNHAN-RMAAE-ALRNYRNTqgILKDTQlHLDDALR--GQEDLKEQL 1678
Cdd:COG4913 438 IPARLLALRDALAEAlGLDEAELpfvgELIEVRPEEERwRGAIErVLGGFALT--LLVPPE-HYAAALRwvNRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1679 amverranllqaeieelratleQTERSRKIAEQELLDASERVQLLHtqntslintkkKLETDISQIQGEMEDIVQE---- 1754
Cdd:COG4913 515 ----------------------VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrfdy 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1755 --ARNAEE--KAKKAITDAAMMAeelkkeQDTSAHlermKKNMEQTVK-DLQLRLDEAEQLALKggKKQIQKLEARVREL 1829
Cdd:COG4913 562 vcVDSPEElrRHPRAITRAGQVK------GNGTRH----EKDDRRRIRsRYVLGFDNRAKLAAL--EAELAELEEELAEA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1830 EGEVEsEQKRNVEAVKGLRKHERRVKELTY-------------QTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQS 1896
Cdd:COG4913 630 EERLE-ALEAELDALQERREALQRLAEYSWdeidvasaereiaELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
570 580
....*....|....*....|....*....
gi 1958661053 1897 NTNLSKFRKLQHELEEAEERADIAESQVN 1925
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1215-1938 |
1.05e-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: 76.93 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1215 DNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLiNDLTTQRGRLQTESGEF 1294
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1295 SRQLDEKEALVSQLSRgkqafTQQIEELKRQLEEEVKAKNALAHALQSSRhdcdllrEQYEEEQESKAELQRALSKANSE 1374
Cdd:TIGR00618 266 RARIEELRAQEAVLEE-----TQERINRARKAAPLAAHIKAVTQIEQQAQ-------RIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1375 VAQwrtkyetdaiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTK-------QRLQNEVEDLMLDVERTNAACA 1447
Cdd:TIGR00618 334 VKQ-------------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtltQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1448 ALDKKQRNFDKILAE------WKQKYEETHAELEASQKEARSLgtelfkmKNAYEESLDQLETLKRENKNLQQEISDLTE 1521
Cdd:TIGR00618 401 ELDILQREQATIDTRtsafrdLQGQLAHAKKQQELQQRYAELC-------AAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1522 QIAEGgKRIHELEKIKKQVEQEKCELQAALE-EAEASLEHEEGK-------------ILRIQLELNQVKSEIDRKIAEKD 1587
Cdd:TIGR00618 474 QLQTK-EQIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1588 EEIDQLKRNHIRVVESMQSTLDAEI---RSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHL 1664
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1665 DDALRGQEDLKEQLAMVERRANLLQAEIEE-LRATLEQTERSRKIAEQELLDASERVQLLhTQNTSLINTKKKLETDISQ 1743
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKEQL-TYWKEMLAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1744 IQGEMEDIVQEARNAEEKAKKAItdaammaeelkkEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkqiQKLE 1823
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLGSDL------------AAREDALNQSLKELMHQARTVLKARTEAHFN----------NNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1824 ARVRELEGEVESEQKRNVEAVKglRKHERRVKELTYQTEEDRknilrlQDLVDKLQAKVKSYKRQAEEaEEQSNTNLSKF 1903
Cdd:TIGR00618 770 VTAALQTGAELSHLAAEIQFFN--RLREEDTHLLKTLEAEIG------QEIPSDEDILNLQCETLVQE-EEQFLSRLEEK 840
|
730 740 750
....*....|....*....|....*....|....*
gi 1958661053 1904 RKLQHELEEAEERADIAESQVNKLRVKSREVHTKV 1938
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1280-1843 |
1.42e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1280 LTTQRGRLqtesGEFSRQLDEKEA--LVSQLSRGKQAFTQQIEELKRQLEEEVKAKnalahalqSSRHDCDLLREQYEEE 1357
Cdd:PRK02224 182 LSDQRGSL----DQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1358 QESKAELQRALSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1431
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1432 VEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARS-------LGTELFKMKNAYEESLDQLET 1504
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreeieeLEEEIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1505 LKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQ--------------EKCELQAALEEAEASLEHEEGKILRIQL 1570
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1571 ELNQVKSEIDR--KIAEKDEEIDQLKRNHIRVVESMqSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALR 1648
Cdd:PRK02224 490 EVEEVEERLERaeDLVEAEDRIERLEERREDLEELI-AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1649 NYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERranlLQAEIEELRatleqtERSRKIAEQElldaSERVQLLHTQNT 1728
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIAD----AEDEIERLR------EKREALAELN----DERRERLAEKRE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1729 SlintKKKLETDISqiqgemEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLD--E 1806
Cdd:PRK02224 635 R----KRELEAEFD------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREalE 704
|
570 580 590
....*....|....*....|....*....|....*..
gi 1958661053 1807 AEQLALKGGKKQIQKLEARVRELEGEVeseQKRNVEA 1843
Cdd:PRK02224 705 NRVEALEALYDEAEELESMYGDLRAEL---RQRNVET 738
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
851-1453 |
1.65e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELaksEAKRKELEEKMVSLLKEKNDLQLQVQAEAE-GLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 930 TERAEDE---------------EEINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEMAGL 992
Cdd:pfam15921 305 QEQARNQnsmymrqlsdlestvSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 993 DETIAKLTKEKKALQEAHQQTLDdlqaeEDKVNTLTKAkiKLEQQVDDLEGSLEQEKKLrmdLERAKRKLEGDLKLAQES 1072
Cdd:pfam15921 383 LADLHKREKELSLEKEQNKRLWD-----RDTGNSITID--HLRRELDDRNMEVQRLEAL---LKAMKSECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1073 ImdienekQQLDERLKKkefeMSNLQSKIEDEQAIgiqLQKKIKELqarieeleeeiEAERASRAKAEKQRSDLSRELEE 1152
Cdd:pfam15921 453 I-------QGKNESLEK----VSSLTAQLESTKEM---LRKVVEEL-----------TAKKMTLESSERTVSDLTASLQE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1153 ISERLEeaggATSAQIEMNKKRE----AEFQKMRRDLEE-ATLQHEATAATLRKKHADSVAE-LGEQIDNLQ-------R 1219
Cdd:pfam15921 508 KERAIE----ATNAEITKLRSRVdlklQELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEiLRQQIENMTqlvgqhgR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1220 VKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELkskEEEQQRLINDLTTQRGRLQTESGEFSRQLD 1299
Cdd:pfam15921 584 TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL---ELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1300 EKEALVSQLSrgkqAFTQQIEELKRQL----EEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAE-------LQRAL 1368
Cdd:pfam15921 661 EVKTSRNELN----SLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQI 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1369 SKANSEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERT 1442
Cdd:pfam15921 737 TAKRGQIDALQSKIQfleeamTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
650
....*....|....
gi 1958661053 1443 N---AACAALDKKQ 1453
Cdd:pfam15921 817 SlqfAECQDIIQRQ 830
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1248-1912 |
2.00e-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: 75.93 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1248 AKGNLEKMCRTLEDQVSELKSKEEEQQRLINdltTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE 1327
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHE---KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1328 EEVK----AKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALskANSEVAQWRTKYETDAIQRT------------- 1390
Cdd:pfam15921 149 NTVHeleaAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMhfrslgsaiskil 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1391 EELEEAKKKLAQRLQAAEEHVEAVNAKCAS-LEKTKQRLQNEVEDLMLD--------VERTNAACAALDKKQRNFDKILA 1461
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEheveitglTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1462 EWKQK---YEETHAELEASQKEARSlgtELFKMKNAYEESLDQLEtlkrenKNLQQEISDLTEQIAEGGKRIHELEKIKK 1538
Cdd:pfam15921 307 QARNQnsmYMRQLSDLESTVSQLRS---ELREAKRMYEDKIEELE------KQLVLANSELTEARTERDQFSQESGNLDD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1539 QVEQEKCELQAalEEAEASLEHEEGKILRIQLELNQVK-SEIDRKIAEKDEEIDQLKRnhirVVESMQSTLDAEIRSRND 1617
Cdd:pfam15921 378 QLQKLLADLHK--REKELSLEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLEA----LLKAMKSECQGQMERQMA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1618 AIRIKKKMEGDLNEMEIQLNHANRMAAEALRNyrntqgiLKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRA 1697
Cdd:pfam15921 452 AIQGKNESLEKVSSLTAQLESTKEMLRKVVEE-------LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1698 TLE---QTERSRKIAEQELLDASERVQLLHTQntsLINTKKKLETDISQIQGEMEDIVQEARNAeekakkaitdAAMMAE 1774
Cdd:pfam15921 525 RVDlklQELQHLKNEGDHLRNVQTECEALKLQ---MAEKDKVIEILRQQIENMTQLVGQHGRTA----------GAMQVE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1775 elkkeqdtsahlermKKNMEQTVKDLQLRLDEAEQLAlkggkkqiQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRV 1854
Cdd:pfam15921 592 ---------------KAQLEKEINDRRLELQEFKILK--------DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV 648
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1855 KELTYQTE----EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEE 1912
Cdd:pfam15921 649 KDIKQERDqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1262-1928 |
3.02e-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: 75.60 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1262 QVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQ-----------------LSRGKQAFTQQIEELKR 1324
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQlqaetelcaeaeemrarLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1325 QLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTeELEEAKKKLAQRL 1404
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS-KLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1405 QAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSL 1484
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1485 GTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGK 1564
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1565 ILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAA 1644
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1645 EALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMverranlLQAEIEELRATLEQTE----RSRK---IAEQELLDAS 1717
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAEgkniKLSKdvsSLESQLQDTQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1718 ERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTV 1797
Cdd:pfam01576 475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1798 KDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVES---EQKRNVEAVKGLRKHERRVKELtyqTEEDRKNILRLQDL 1874
Cdd:pfam01576 555 EALTQQLEEKAA--------AYDKLEKTKNRLQQELDDllvDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEE 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1875 VDKLQAkvksykrqaeEAEEQSNTNLSkfrkLQHELEEAEERADIAESQVNKLR 1928
Cdd:pfam01576 624 RDRAEA----------EAREKETRALS----LARALEEALEAKEELERTNKQLR 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1044-1941 |
3.53e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 75.47 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1044 SLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKiEDEQAIGIQLQKKIKELQARIE 1123
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1124 ELEeeieAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREA-EFQKMRRDLEEATLQHEATAATLRKK 1202
Cdd:TIGR00606 266 KLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1203 HADSVAELGE-----QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQ-------VSELKSKE 1270
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktaaqlCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1271 EEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLL 1350
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1351 REQYeeEQESKAELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQAAE-EHVEAVNAKCA------SLEK 1423
Cdd:TIGR00606 502 EVKS--LQNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKsRHSDELTSLLGyfpnkkQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1424 TKQRLQNEVEDLMLDVERTNAACAALDKKQ---RNFDKILAEWKQKYEETHAELEASQKEARSLGtelfKMKNAYEESLD 1500
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQDEESDLE----RLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1501 QLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQV----- 1575
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglap 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1576 --KSEIDRKIAEKDEEIDQLK---------RNHIRVVESMQSTLDAEIRSRND-----AIRIKKKMEGDLNEMEIQLNHA 1639
Cdd:TIGR00606 734 grQSIIDLKEKEIPELRNKLQkvnrdiqrlKNDIEEQETLLGTIMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1640 NRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEEL---RATLEQTERSRKIAEQELLDA 1716
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQFEEQLVEL 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1717 SERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQearNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLER 1788
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDD 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1789 MKKNMEQTVKDLQLRLDEAEQlalkgGKKQIQKlEARVRELEGEVESEQKRNVEAVKGLRKHERRVKEL-----TYQTEE 1863
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEM 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1864 DRKNILRLQDLVDKLQAKVKSYKR-------QAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1936
Cdd:TIGR00606 1045 GQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYY 1124
|
....*
gi 1958661053 1937 KVISE 1941
Cdd:TIGR00606 1125 KTLDQ 1129
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1317-1916 |
4.08e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1317 QQIEELKRQLE--EEVKAKNALAHALQSSRHDCDLLRE--QYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEE 1392
Cdd:COG4913 242 EALEDAREQIEllEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1393 LEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldvERTNAACAALDKKQRNFDKILAEWKQKYEETHA 1472
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1473 ELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG-GKRIHEL----EKIkkQVEQEKCEL 1547
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLDEAELpfvgELI--EVRPEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1548 QAALEEAeasleheegkilriqleLNQVKSEI---DRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKK 1624
Cdd:COG4913 477 RGAIERV-----------------LGGFALTLlvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1625 MEGDLNEMEIQLNH--ANRMA------AEALRNYRntQGILKDTQLH-------LDDALRGQEDL------KEQLAMVER 1683
Cdd:COG4913 540 LDFKPHPFRAWLEAelGRRFDyvcvdsPEELRRHP--RAITRAGQVKgngtrheKDDRRRIRSRYvlgfdnRAKLAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1684 RANLLQAEIEELRATLEQTERSRKiAEQELLDASERVQllhTQNTSLINTkKKLETDISQIQGEMEDIvqearnaeEKAK 1763
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELD-ALQERREALQRLA---EYSWDEIDV-ASAEREIAELEAELERL--------DASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1764 KAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNVEA 1843
Cdd:COG4913 685 DDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAEDLARLELRALLEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1844 VKGLRKHERRVKELTYQTEEDRKNIL-RLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLS-------KFRKLQHE-LEEAE 1914
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRaRLNRAEEELERAMRAFNREWPAETADLDADLEslpeylaLLDRLEEDgLPEYE 833
|
..
gi 1958661053 1915 ER 1916
Cdd:COG4913 834 ER 835
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
4.61e-13 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 65.14 E-value: 4.61e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1958661053 33 DAKTSVFVAEPKESFVKGTIQSKDAGKVTVKTEAGATLTVKEDQI 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
917-1633 |
5.07e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 74.37 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 917 KTKIQLEAKIKEVTERAEDEEEINAELTAkkRKLEDECSELKKDIddleltlakveKEKHATENKVKNLTEEMAGLDETI 996
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELQFENEKVS--LKLEEEIQENKDLI-----------KENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 997 AKLTKEKkalqEAHQQTLDDLQAEEDKVNTLTKakiklEQQVDDLEGSLEQEKKLRMDLERAKRkLEGDLklaQESIMDI 1076
Cdd:pfam05483 172 KKYEYER----EETRQVYMDLNNNIEKMILAFE-----ELRVQAENARLEMHFKLKEDHEKIQH-LEEEY---KKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1077 ENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKelqarieeleeeieAERASRAKAEKQRSDLSRELEEISER 1156
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK--------------LQDENLKELIEKKDHLTKELEDIKMS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1157 LEEAggatsaqIEMNKKREAEFQKMRRDLEEATLQHEATAATLRK---KHADSVAELGEQIDNLQRV----KQKLEKEKS 1229
Cdd:pfam05483 305 LQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKakaAHSFVVTEFEATTCSLEELlrteQQRLEKNED 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1230 EMK---MEIDDLASNVETVSKAKGNLEKMCRTLEDQVSE---LKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEA 1303
Cdd:pfam05483 378 QLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEdekLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1304 LVSQLSRGKQAFTQQIEELKRQLEEEvKAKNALAHAlqssrhDCDLLREQYEEEQESKAELQRALSKANSEVAQWRtKYE 1383
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------HCDKLLLENKELTQEASDMTLELKKHQEDIINCK-KQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1384 TDAIQRTEELEEAKKKLAQRLQAAEEHV----EAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNfdki 1459
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN---- 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1460 laewKQKYEEthaELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEgGKRIHElEKIKKQ 1539
Cdd:pfam05483 606 ----KNKNIE---ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIE-DKKISE-EKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1540 VEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDqLKRNHIRVVESMQSTLDAEIRS-RNDA 1618
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG-LYKNKEQEQSSAKAALEIELSNiKAEL 755
|
730
....*....|....*
gi 1958661053 1619 IRIKKKMEGDLNEME 1633
Cdd:pfam05483 756 LSLKKQLEIEKEEKE 770
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
853-1766 |
5.29e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 74.70 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 853 EKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKekndlqlqvqaeaegladaeercdqliktkiqLEAKIKEVTER 932
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK--------------------------------LDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 933 AEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAH-- 1010
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKte 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1011 ---QQTLDDLQAEEDKVNTLTKAKIKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQL 1083
Cdd:TIGR00606 345 llvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1084 DERLKKKEFEMSNLQSKIEDEQAIgiqLQKKIKELQARIEELEeeieaerasraKAEKQRSDLSRELEEISERLEEAGGA 1163
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1164 -TSAQIEMNKKREAEFQKMRRDLEEaTLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1242
Cdd:TIGR00606 491 eKNSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1243 ETVskakgnlekmcRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSR------GKQAFT 1316
Cdd:TIGR00606 570 PNK-----------KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1317 QQIEELKRQLEEEVKAKNALAHALQssrhdcdlLREQYEEEQESKaelqralSKANSEVAQwrtkyetDAIQRTEELEEA 1396
Cdd:TIGR00606 639 SDLERLKEEIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEF 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1397 KKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELE- 1475
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGt 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1476 --ASQKEARSLGTELFKMKNAYEEsldqletLKRENKNLQQEISDLteQIAEGGKRIHELEKIKKQVEQEKCELQAALEE 1553
Cdd:TIGR00606 777 imPEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1554 AEASLEHEEGKILRIQLELNQVKSEiDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEME 1633
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1634 IQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKE-QLAMVERRANLLQAEIEELRATLEQTERSRKIAEQE 1712
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD 1006
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661053 1713 LLDASERVQLLHTQNTSLI--NTKKKLETDISQIQGEM-EDIVQEARNAEEKAKKAI 1766
Cdd:TIGR00606 1007 IDTQKIQERWLQDNLTLRKreNELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
919-1591 |
7.36e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 919 KIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK 998
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 999 LtkekkalqeahQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKlrmdlerAKRKLEGDLKLAQESIMDIEN 1078
Cdd:TIGR04523 199 L-----------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ-------EINEKTTEISNTQTQLNQLKD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1079 EKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARieeleeeieaerasraKAEKQRSDLSRELEEISERLE 1158
Cdd:TIGR04523 261 EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ----------------KEQDWNKELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1159 EaggaTSAQIEMNKKreaefqkmrrdleeatlqheataatlrkkhadSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDL 1238
Cdd:TIGR04523 325 E----IQNQISQNNK--------------------------------IISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1239 ASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTesgefsrqldEKEALVSQLSRGKQAFTQQ 1318
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ----------EKELLEKEIERLKETIIKN 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1319 IEELKRqLEEEVKAKNALAHALQSSRhdcdllreqyeEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1398
Cdd:TIGR04523 439 NSEIKD-LTNQDSVKELIIKNLDNTR-----------ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1399 KLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVErtnaacaaldkkqrnfdkilaewKQKYEETHAELEasq 1478
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN-----------------------KDDFELKKENLE--- 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1479 KEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASL 1558
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1958661053 1559 EHEEGKILRIQLELNQVK---SEIDRKIAEKDEEID 1591
Cdd:TIGR04523 641 NKLKQEVKQIKETIKEIRnkwPEIIKKIKESKTKID 676
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1276 |
1.34e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 843 IKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQL 922
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 923 EAKIKEVTERAEDEEEINaELTAKKRKLEDECSELK-KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTK 1001
Cdd:PRK03918 348 KELEKRLEELEERHELYE-EAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1002 EKKALQEAHQQ--TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQ-----ESIM 1074
Cdd:PRK03918 427 AIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkelaEQLK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1075 DIENEKQQLD-ERLKKKEFEMSNLQSK---IEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRE- 1149
Cdd:PRK03918 507 ELEEKLKKYNlEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEs 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1150 LEEISERLEEAGGATSAQIEM-NKKREAEFQKMRRDLEEATLqhEATAATLRKKHADsVAELGEQIDNLQRV-----KQK 1223
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELkDAEKELEREEKELKKLEEEL--DKAFEELAETEKR-LEELRKELEELEKKyseeeYEE 663
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1224 LEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRL 1276
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1241-1778 |
1.46e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1241 NVETVSKAKGNLEKMCRTLEDQVSELK---SKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQ---A 1314
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKeleE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1315 FTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQ--RALSKANSEVAQWRTKYEtdaiQRTEE 1392
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYL----DELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1393 LEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQR---LQNEVEDLMLDVERTNAACAALDKKQRNFDKI----LAEWKQ 1465
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKlkeLEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1466 KYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQ-----IAEGGKRIHELEKIKKQV 1540
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1541 EQEKCELQAALEEAEASLEHEEgKILRIQLELNQVKS------EIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRS 1614
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKEleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1615 RNDAIRIKKKMEGDLNEMEIQLNHANRMAAE--------------ALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAM 1680
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerlkELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1681 VERRANLLQAEIEELRATLEQTERS-----RKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIvQEA 1755
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-EKA 709
|
570 580
....*....|....*....|...
gi 1958661053 1756 RNAEEKAKKAITDAAMMAEELKK 1778
Cdd:PRK03918 710 KKELEKLEKALERVEELREKVKK 732
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1391-1930 |
2.31e-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: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1391 EELEEAKKKLAQRLQAAEE-HveavnakcaslEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEE 1469
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNElH-----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1470 THAELEAsqkeARSLGTELFKMKNAyeeSLDQLETLKRENKNLQQEISDLTEQIAEG-GKRIHELEKIKK-QVEQEKCEL 1547
Cdd:pfam15921 150 TVHELEA----AKCLKEDMLEDSNT---QIEQLRKMMLSHEGVLQEIRSILVDFEEAsGKKIYEHDSMSTmHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1548 QAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIaekdeeiDQLKRNHirvvesmqstldaeirsrndairiKKKMEG 1627
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSESQNKI-------ELLLQQH------------------------QDRIEQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1628 DLNEMEIQLNHANRMAAEALRNYRNTQgilkdTQLHLDdalrgQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRK 1707
Cdd:pfam15921 272 LISEHEVEITGLTEKASSARSQANSIQ-----SQLEII-----QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1708 IAEQELldaservqllhTQNTSLINTkkkletDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1787
Cdd:pfam15921 342 DKIEEL-----------EKQLVLANS------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1788 RMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKn 1867
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE- 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1868 ilRLQDLVDKLQAkvksyKRQAEEAEEQSNTNLSKfrklqhELEEAEERADIAESQVNKLRVK 1930
Cdd:pfam15921 476 --MLRKVVEELTA-----KKMTLESSERTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1379-1892 |
2.33e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1379 RTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVN-------AKCASLEKTKQRLQ---NEVEDLMLDVERTNAACAA 1448
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselpelrEELEKLEKEVKELEelkEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1449 LDKKQRNFDKILAEWKQKYEETHaELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK 1528
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1529 RIHELEKIKKQVEqekcELQAALEEAEASLEHEEgKILRIQLELNQVKSEI-DRKIAEKDEEIDQLKR------NHIRVV 1601
Cdd:PRK03918 336 KEERLEELKKKLK----ELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGLTPEKLEKELEELEKakeeieEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1602 ESMQSTLDAEIRSRNDAIRIKKKMEG-----------------------DLNEMEIQLNHANRMAAEALRNYRNTQGILK 1658
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1659 DtqlhlDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQT--ERSRKIAEQ--ELLDASERVQLLHTQNTSLINTK 1734
Cdd:PRK03918 491 K-----ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKlkEKLIKLKGEikSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1735 KKLETDISQIQGEMEDI-----------VQEARNAEEK---AKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDL 1800
Cdd:PRK03918 566 DELEEELAELLKELEELgfesveeleerLKELEPFYNEyleLKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1801 QLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDL------ 1874
Cdd:PRK03918 643 EELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLekaler 722
|
570
....*....|....*...
gi 1958661053 1875 VDKLQAKVKSYKRQAEEA 1892
Cdd:PRK03918 723 VEELREKVKKYKALLKER 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
842-1334 |
3.16e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 842 KIKPLLKSAETEKEMATMKEEFQKTKDElaksEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLiKTKIQ 921
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA-KKKAE 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 922 LEAKIKEVTERAedEEEINAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAGLDETIAKLTK 1001
Cdd:PTZ00121 1429 EKKKADEAKKKA--EEAKKADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1002 EKKALQEAHQQTLDDLQAEEDKvntltkaKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQEsiMDIENEKQ 1081
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--LKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1082 QLDErlKKKEFEMSNLQSKIEDEQAigiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAg 1161
Cdd:PTZ00121 1565 KAEE--AKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL- 1638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1162 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS--VAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLA 1239
Cdd:PTZ00121 1639 ----------KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1240 SNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGrlqtESGEFSRQLDEKEALVSQLSRGKQAFTQQ- 1318
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEe 1784
|
490
....*....|....*...
gi 1958661053 1319 --IEELKRQLEEEVKAKN 1334
Cdd:PTZ00121 1785 ldEEDEKRRMEVDKKIKD 1802
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1382 |
3.28e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 848 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLiktkiqleakik 927
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL------------ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 928 eVTERAEDEEEINAeltakkrkLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQ 1007
Cdd:PRK02224 299 -LAEAGLDDADAEA--------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1008 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDD----LEGSLEQEKKLRMDLERAKRK---LEGDLKLAQESImdieNEK 1080
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREReaeLEATLRTARERV----EEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1081 QQLDERLK----KKEFEMSNLQSKIEDEQAIGIQLQKKIKELQaRIEELEEEIEAERASRAKAEKQRSDLSRELEEISER 1156
Cdd:PRK02224 446 EALLEAGKcpecGQPVEGSPHVETIEEDRERVEELEAELEDLE-EEVEEVEERLERAEDLVEAEDRIERLEERREDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1157 LEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhadsvaelgEQIDNLQRVKQKLEKEKSEMKMEID 1236
Cdd:PRK02224 525 IAER----RETIEEKRERAEELRERAAELEAEAEEKREAAAEAE-----------EEAEEAREEVAELNSKLAELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1237 DLAsNVETVSKAKGNlekmcrtLEDQVSELKSKEEEQQRLiNDLttQRGRLQTESgEFSRQLDEK--EALVSQLSRGKQA 1314
Cdd:PRK02224 590 SLE-RIRTLLAAIAD-------AEDEIERLREKREALAEL-NDE--RRERLAEKR-ERKRELEAEfdEARIEEAREDKER 657
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1315 FTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREqYEEEQESKAELQRALSKANSEVAQWRTKY 1382
Cdd:PRK02224 658 AEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE-LRERREALENRVEALEALYDEAEELESMY 724
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1187-1764 |
2.92e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1187 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNVETVSKAKGNLEKMCRTLEDQVSEL 1266
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKEDHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1267 KSKEEEQQRLINDLTTqrgrLQTESGEFSRQLDEKEALVS----QLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQ- 1341
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQi 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1342 SSRHDCDLLRE---QYEEEQESKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVEavnakc 1418
Cdd:pfam05483 322 ATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQKKSSELE------ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1419 aslEKTKQRLQNEVEdlMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEES 1498
Cdd:pfam05483 395 ---EMTKFKNNKEVE--LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1499 LDQLETLKR---------------------ENKNLQQEISDLT-------EQIAEGGKRIHELEKIKKQVEQEKCELQAA 1550
Cdd:pfam05483 470 LKEVEDLKTelekeklknieltahcdklllENKELTQEASDMTlelkkhqEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1551 LEEAEASL--EHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEG- 1627
Cdd:pfam05483 550 LESVREEFiqKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENk 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1628 -------DLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANL-LQAEIEELRATL 1699
Cdd:pfam05483 630 qlnayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKrCQHKIAEMVALM 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1700 EQTERS-RKIAEQElldaSERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKK 1764
Cdd:pfam05483 710 EKHKHQyDKIIEER----DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1525 |
3.10e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 859 MKEEFQKTKDELAKSEAKRKELEEKMVSLlkeKNDLQLQVQAEAEGLADAEercdqliKTKIQLEAKIKEVTERAED-EE 937
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 938 EINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTL 1014
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1015 DDLQAEEDKVNTLTKAKIKL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKK 1090
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1091 EFEMSNLqSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEM 1170
Cdd:pfam05483 390 SSELEEM-TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEH 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1171 NKKreaEFQKMRRDLEEATLQHeataatlrkkhadsvAELGEQIDNLQRVKQKLEKEKSEMKMEiddLASNVETVSKAKG 1250
Cdd:pfam05483 469 YLK---EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKK 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1251 NLEKMCRTLEdqvselkSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEalvsqlsrgkqaftqqieELKRQLEEEV 1330
Cdd:pfam05483 528 QEERMLKQIE-------NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE------------------ENARSIEYEV 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1331 KAKNALAHALQSSrhdCDLLREQYEEEQESKAELQ---RALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAA 1407
Cdd:pfam05483 583 LKKEKQMKILENK---CNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1408 EEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAC--------AALDKKQRNFDKILAEWKQKYEETHAELEASQK 1479
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCqhkiaemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSS 739
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1958661053 1480 EARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1525
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1208-1713 |
5.31e-11 |
|
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: 67.84 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1208 AELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRL 1287
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1288 QTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRA 1367
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1368 LSKANSEVAQWRT------KYETDAiqrtEELEEAKKKLAQ--RLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDV 1439
Cdd:pfam05557 162 QSSLAEAEQRIKElefeiqSQEQDS----EIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1440 ERTNAACAALdkkqrnfdkilAEWKQKYEETHAELEASQKEARSLGTELFKMknayeesldqlETLKRENKNLQQEISDL 1519
Cdd:pfam05557 238 EREEKYREEA-----------ATLELEKEKLEQELQSWVKLAQDTGLNLRSP-----------EDLSRRIEQLQQREIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1520 TEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQlelnqvkseidRKIAEKDEEIDQLKRNhir 1599
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAI--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1600 vVESMQSTLDAEIRSRNDAIRIK------KKMEGDLNEMEIQLNHANRmaaealrnyrnTQGILKDTQLHLD---DALRG 1670
Cdd:pfam05557 362 -LESYDKELTMSNYSPQLLERIEeaedmtQKMQAHNEEMEAQLSVAEE-----------ELGGYKQQAQTLErelQALRQ 429
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958661053 1671 QEDLKEQLAMVERRANLLQaEIEELRATLEQTERSRKIAEQEL 1713
Cdd:pfam05557 430 QESLADPSYSKEEVDSLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
898-1631 |
6.87e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.94 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 898 VQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHA 977
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 978 TENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLT------KAKIKlEQQVDD 1040
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTakynrrRSKIK-EQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1041 LEGSLEQEKKLRMDLERAKRKLEGDLKlAQESIMDIENEKQQLDERLKKKEFE--MSNLQSKIEDEQAIGIQL------Q 1112
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLNQATATPELLlqlenfD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1113 KKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRR----DLEEA 1188
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQS 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1189 TLQHEATAATLRKK-HADSVAELGEQIDNLQRVKQKLEK-EKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSEL 1266
Cdd:pfam12128 551 IGKVISPELLHRTDlDPEVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1267 KSKEEEQQRlinDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEvkaKNALAHALQssrhd 1346
Cdd:pfam12128 631 NGELEKASR---EETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ---LKQLDKKHQ----- 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1347 cDLLREQYEEEQESKAELQRALSKANSEvaqwrTKYETDAIQrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQ 1426
Cdd:pfam12128 700 -AWLEEQKEQKREARTEKQAYWQVVEGA-----LDAQLALLK--AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIA 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1427 RLQNEVEDLMLDVERTnaacaaldkkqRNFDKILAEWKQKYEETHaeleASQKEARSLgtelfkmknayeesldQLETLK 1506
Cdd:pfam12128 772 KLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQETW----LQRRPRLAT----------------QLSNIE 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1507 RENKNLQQeisDLTEQIAEGGKRIHELEKIKKQVEqekcELQAALEEAEASLEHEEGKILRiqLELNQVKSEIDRKIAEK 1586
Cdd:pfam12128 821 RAISELQQ---QLARLIADTKLRRAKLEMERKASE----KQQVRLSENLRGLRCEMSKLAT--LKEDANSEQAQGSIGER 891
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1958661053 1587 DEEIDQLKRNHIRVVESMQSTLDaeirsrNDAIRIKKKMEGDLNE 1631
Cdd:pfam12128 892 LAQLEDLKLKRDYLSESVKKYVE------HFKNVIADHSGSGLAE 930
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
854-1262 |
7.05e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 7.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 854 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEA--EGLADAEERCDQLIKTKIQLEAKIKEVTE 931
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 932 RAEDEEEINAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1001 KEKKALQE-----------AHQQTLDDLQAEEDKV---------------NTLTKAKIKLEQQVDDLEGSLEQEKKLRMD 1054
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1055 LERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEfemsnlqskiedEQAIGIQLQKKIKELQARIEELEEEIEAERA 1134
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAE------------ELEEELQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1135 SRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKR--EAEFQKMRRDLEEATLQHEAtaatLRKKHADSVAELG- 1211
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELEE----LREELAELEAELEq 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1212 -EQIDNLQRVKQKLEKEKSEMKMEIDDLASNvetvSKAKGNLEKMCRTLEDQ 1262
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREE 512
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1250-1857 |
7.98e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 67.47 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1250 GNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQL-------DEKEALVSQLSrGKQAFTQQIEEL 1322
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAvaekagqAEAEGLRAALA-GAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1323 KRQLEEEVKA--KNALAHALQSSRHDCDLLREQYE--EEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1398
Cdd:pfam07111 138 SQRELEEIQRlhQEQLSSLTQAHEEALSSLTSKAEglEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1399 KLAQRLQ--AAEEHVEAVNAKCASLEKtkQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILA----EWKQKYEETHA 1472
Cdd:pfam07111 218 TLVESLRkyVGEQVPPEVHSQTWELER--QELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlqeeELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1473 ELEASQKEARSLgtelfkMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkrihELEKIKKQvEQEKCELQAALE 1552
Cdd:pfam07111 296 LEPEFPKKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE------LQEQVTSQ-SQEQAILQRALQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1553 EAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKrnhiRVVESMQSTldaeirsrndAIRIKKKMeGDLNEM 1632
Cdd:pfam07111 363 DKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSST----------QIWLETTM-TRVEQA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1633 EIQLNHANRMAAEALRNYRNTQGILKD----TQLHLDD------ALRGQEDLKEQLAMVERRANLLQAEIeELRATLEQT 1702
Cdd:pfam07111 428 VARIPSLSNRLSYAVRKVHTIKGLMARkvalAQLRQEScpppppAPPVDADLSLELEQLREERNRLDAEL-QLSAHLIQQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1703 ERSRKIAEQElldaSERVQllhtqntsLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDT 1782
Cdd:pfam07111 507 EVGRAREQGE----AERQQ--------LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEI 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1783 SAH-----LERMKKNMEQTVKDLQLRLDEA--EQLALKGGKKQIQKLEARVRELEGEVE--SEQKRNVEAvkglRKHERR 1853
Cdd:pfam07111 575 YGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHRATQEKERNQELRrlQDEARKEEG----QRLARR 650
|
....
gi 1958661053 1854 VKEL 1857
Cdd:pfam07111 651 VQEL 654
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1577-1924 |
8.13e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1577 SEIDRKIAEKDEEIDQLKRNHIR---VVESMQSTLDAEIRSRNDAIR------IKKKMEG-----DLNEMEIQLNHANRM 1642
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqallkEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1643 AAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQL-AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQ 1721
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1722 LLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSA----HLERMKKNMEQTV 1797
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1798 KDLQLRLDEAEQLALKGG--KKQIQKLEARVRELEGEVESEQKRnveavkgLRKHERRVKELTYQTEEDRKNILRLQDLV 1875
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1958661053 1876 DKLQakvksykrqaeeaeeqsntnlSKFRKLQHELEEAEERADIAESQV 1924
Cdd:TIGR02169 479 DRVE---------------------KELSKLQRELAEAEAQARASEERV 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1213-1934 |
1.06e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1213 QIDNLQRVKQKLEKEKSEMKMEIDDLASNV--ETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRlindlttqrgrlqte 1290
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRadEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK--------------- 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1291 sGEFSRQLDE--KEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRAL 1368
Cdd:PTZ00121 1124 -AEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1369 SKAnsevaqwRTKYETDAIQRTEELEEAKKKLAQRlQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAA 1448
Cdd:PTZ00121 1203 EAA-------RKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1449 LDKKQrnfdkilAEWKQKYEETHAELEASQKEARSLGTELfkmKNAYEEsldqletlKRENKNLQQEISDLTEQIAEGGK 1528
Cdd:PTZ00121 1275 EEARK-------ADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEE--------AKKADEAKKKAEEAKKKADAAKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1529 RIhelEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLElnQVKSEIDRKIAEKDEEIDQLKRNhirvvesmqstl 1608
Cdd:PTZ00121 1337 KA---EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKADEAKKK------------ 1399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1609 dAEiRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEqlAMVERRANLL 1688
Cdd:PTZ00121 1400 -AE-EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--AEEAKKADEA 1475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1689 QAEIEELRATLE---QTERSRKIAEqELLDASErvqllhtqntslinTKKKLEtdiSQIQGEMEDIVQEARNAEEKAKka 1765
Cdd:PTZ00121 1476 KKKAEEAKKADEakkKAEEAKKKAD-EAKKAAE--------------AKKKAD---EAKKAEEAKKADEAKKAEEAKK-- 1535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1766 iTDAAMMAEELKKEQDTSaHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVK 1845
Cdd:PTZ00121 1536 -ADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1846 glRKHERRVK-ELTYQTEEDRKNILRLQDLVDKLQAKVKSYkRQAEEAE----EQSNTNLSKFRKLQHELEEAEERADIA 1920
Cdd:PTZ00121 1614 --KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENkikaAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
730
....*....|....
gi 1958661053 1921 ESQVNKLRVKSREV 1934
Cdd:PTZ00121 1691 AEALKKEAEEAKKA 1704
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1218-1903 |
1.07e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.97 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1218 QRVKQKLEKEKSEMK---MEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEF 1294
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1295 SRQLDEKEALVSQLSRgkqaftqQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSE 1374
Cdd:TIGR04523 116 KEQKNKLEVELNKLEK-------QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1375 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQR 1454
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1455 NFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLD-----QLETLKRENKNLQQEISDLTEQIAEGGKR 1529
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1530 IHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEI---DRKIaEKDEEIDQLKRNHIRVVESMQS 1606
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndlESKI-QNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1607 TLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNhanrMAAEALRNYRntqgilkdtqlhlddalrgqEDLKEQLAMVERRAN 1686
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKE----LIIKNLDNTR--------------------ESLETQLKVLSRSIN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1687 LLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIvqearnaEEKAKKai 1766
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-------EDELNK-- 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1767 tdaamMAEELKKEQdtsahLERMKKNMEQTVKDLqlrldeaeqlalkggKKQIQKLEARVRELEGEVESEQKRNVEAVKG 1846
Cdd:TIGR04523 550 -----DDFELKKEN-----LEKEIDEKNKEIEEL---------------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661053 1847 LRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKF 1903
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1496-1937 |
1.62e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1496 EESLDQLETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEheegkilriqleln 1573
Cdd:PRK02224 186 RGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1574 qvkseidrKIAEKDEEIDQLkRNHIRVVESMQSTLDAEIRSRndairikkkmegdlnemeiqlnhanRMAAEALRNYRNt 1653
Cdd:PRK02224 252 --------ELETLEAEIEDL-RETIAETEREREELAEEVRDL-------------------------RERLEELEEERD- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1654 qGILKDTQLhlDDAlrGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINT 1733
Cdd:PRK02224 297 -DLLAEAGL--DDA--DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1734 KKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLaLK 1813
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1814 GGK---------------------KQIQKLEARVRELEGEVESEQKRnVEAVKGLRKHERRVKELtyqtEEDRKNilrLQ 1872
Cdd:PRK02224 451 AGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERRED---LE 522
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1873 DLVDKLQAKVKSYKRQAEEAEEQSNtnlskfrKLQHELEEAEERADIAESQVNKLRVKSREVHTK 1937
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAA-------ELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1494-1921 |
1.96e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1494 AYEESLDQLETLK-RENKNLQQEISDLTEQIAEGGK---RIHELEKIKKQVEQEKCELQAALEEAEASLEHEEgkILRIQ 1569
Cdd:COG4717 50 RLEKEADELFKPQgRKPELNLKELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLE--KLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1570 LELNQVKSEIDRKIAEKDEEIDQLKRnhirvvesmqstldaEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRN 1649
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1650 YrntqgiLKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTS 1729
Cdd:COG4717 193 E------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1730 LINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTVKDLQLRLDEA 1807
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1808 EQLALKGGKKQIQKLEARVRELEGE---------VESEQK--RNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVD 1876
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEiaallaeagVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958661053 1877 K--LQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAE 1921
Cdd:COG4717 427 EeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
921-1121 |
3.73e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 921 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1001 KEKK----ALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDI 1076
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958661053 1077 ENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQAR 1121
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1204-1420 |
4.11e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1204 ADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELkskEEEQQRLINDLTTQ 1283
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1284 RGRLQTESGEFSRQL---------DEKEALVS-----QLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDL 1349
Cdd:COG4942 96 RAELEAQKEELAELLralyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1350 LREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCAS 1420
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1257-1706 |
5.47e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1257 RTLEDQVSELKSKEEEQQRLINDLTTQRGRLQtesgEFSRQLDEKEALVSQLSRGKQAFT--QQIEELKRQLEEEVKAKN 1334
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1335 ALAHALQSSRHdcdlLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAV 1414
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1415 NAKCASLEKTKQRLQ--NEVEDLMLDVERTNAACAALDKKQRNFDKILAEWK----------QKYEETHAELEASQKEAR 1482
Cdd:COG4717 226 EEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllaLLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1483 SLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEE 1562
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1563 GkiLRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQ-STLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANR 1641
Cdd:COG4717 386 E--LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1642 MAAEALRnyrntqgilkdtqlhLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSR 1706
Cdd:COG4717 464 QLEEDGE---------------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1672-1938 |
6.94e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1672 EDLKEQLAMVERRANLLQAEIEELRATLE--QTERSRKIAEQELLDASERVQLlhtqnTSLINTKKKLETDISQIQGEME 1749
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1750 DIVQEARNAEEKAkkaitdaammaEELKKEqdtSAHLERMKKNMEQTVKDLqlrlDEAEQLALKGG----KKQIQKLEAR 1825
Cdd:TIGR02169 248 SLEEELEKLTEEI-----------SELEKR---LEEIEQLLEELNKKIKDL----GEEEQLRVKEKigelEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1826 VRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRK 1905
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270
....*....|....*....|....*....|...
gi 1958661053 1906 LQHELEEAEERADIAESQVNKLRVKSREVHTKV 1938
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1201-1778 |
7.18e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.15 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1201 KKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDdlasnvetvskakgNLEKMCRTLEDQVSELKSKEEEQQRLINDL 1280
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYN--------------NAMDDYNNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1281 TTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEEL---------KRQLEEEVKAKNALAHALQSSRHDCDLLR 1351
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1352 EQYEEEQESKAELQRALSKANSevaqwrtkYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1431
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEG--------YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1432 VEDLMLDVERTNAACAALDKKQRNfdkiLAEWKQKYEETHAELEASQKE---ARSLGTE-LFKMKNAYEESLDQLETLKR 1507
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRA----LRENLDELSRNMEMLNGQSVCpvcGTTLGEEkSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1508 EnknLQQEISDLTEQIAEGGKRIHELEKikKQVEQEKCELQAaLEEAEASLEHEEGKILRIQlELNQVKSEIDRKIAEKD 1587
Cdd:PRK01156 487 E---IEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNK-IESARADLEDIKIKINELK-DKHDKYEEIKNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1588 EEIDQLKRNHIRVVESMQSTLDAE-IRSRNDAIRIK-KKMEGDLNEMEIQLNHAN-------RMAAEALRNYRNTQGILK 1658
Cdd:PRK01156 560 LEDLDSKRTSWLNALAVISLIDIEtNRSRSNEIKKQlNDLESRLQEIEIGFPDDKsyidksiREIENEANNLNNKYNEIQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1659 DTQLHLDDALRGQEDLKEQLAMVERRanllQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLE 1738
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIAEIDSI----IPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELS 715
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1958661053 1739 TDISQIQGEMEDIvqearnaeEKAKKAITDAAMMAEELKK 1778
Cdd:PRK01156 716 DRINDINETLESM--------KKIKKAIGDLKRLREAFDK 747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
947-1571 |
7.56e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 947 KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDETIAKLTKEKKALQ-EAHQQTLDDLQAEEDK 1023
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1024 vntLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD-LKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIE 1102
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1103 DEQAIGIQLQKKIKELQARIEELEEEIEAErasRAKAEKQRSDLSRELEEISERLeeaggatsAQIEMNKKR-EAEFQKM 1181
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEAEI--------ASLERRKSNiPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1182 RRDLEEATLQHEA---------------------------TAAT---LRKKHADSVAELGEQID-----NLQRVKQKLEK 1226
Cdd:COG4913 446 RDALAEALGLDEAelpfvgelievrpeeerwrgaiervlgGFALtllVPPEHYAAALRWVNRLHlrgrlVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1227 EKSeMKMEIDDLASNVET-VSKAKGNLEKM---------CRTLED------------QVSELKSKEEEQ----------- 1273
Cdd:COG4913 526 PER-PRLDPDSLAGKLDFkPHPFRAWLEAElgrrfdyvcVDSPEElrrhpraitragQVKGNGTRHEKDdrrrirsryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1274 ----QRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFtQQIEELK------RQLEEEVKAKNALAHALQSS 1343
Cdd:COG4913 605 gfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSwdeidvASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1344 RHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHV------------ 1411
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE----QAEEELDELQDRLEAAEDLARLELralleerfaaal 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1412 --EAVNAKCASLEKTKQRLQNEVEDLMLDVERtnaacaaldkkqrnfdkILAEWKQKYEETHAELEASQKEARSlgtelf 1489
Cdd:COG4913 760 gdAVERELRENLEERIDALRARLNRAEEELER-----------------AMRAFNREWPAETADLDADLESLPE------ 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1490 kmknaYEESLDQLET----------LKRENKNLQQEISDLTEQIAEggkrihELEKIKKQVEqekcELQAALEEaeasLE 1559
Cdd:COG4913 817 -----YLALLDRLEEdglpeyeerfKELLNENSIEFVADLLSKLRR------AIREIKERID----PLNDSLKR----IP 877
|
730
....*....|..
gi 1958661053 1560 HEEGKILRIQLE 1571
Cdd:COG4913 878 FGPGRYLRLEAR 889
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
838-1511 |
8.79e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.30 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 838 KLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSE--AKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAE------ 909
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 910 ERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 982
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 983 KNLTEEMAGLDETIAKLTKekkalQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEGSLEQEKKLRMDLERA 1058
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1059 KRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELqarieeleeeieaerasRAK 1138
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL-----------------RNK 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1139 AEKQRSDLSRELEEISERlEEAGGATSAQIEMNKKREAEFQKMRRdLEEATLQHEataatlrKKHADSVAELgeQIDNLQ 1218
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMER-FQMELKDVE-------RKIAQQAAKL--QGSDLD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1219 RVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKS---------------------KEEEQQRLI 1277
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqigtnlqrrqqfeeqlveLSTEVQSLI 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1278 NDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLRE-QYEE 1356
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKEtELNT 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1357 EQESKAELQRALSKANSEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQAAEEhveavnAKCASLEKT 1424
Cdd:TIGR00606 982 VNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQE 1055
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1425 KQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWK-QKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLE 1503
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH 1135
|
....*...
gi 1958661053 1504 TLKRENKN 1511
Cdd:TIGR00606 1136 SMKMEEIN 1143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1227-1809 |
1.10e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1227 EKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEdQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQ-LDEKEALV 1305
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1306 SQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHD-CDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYET 1384
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1385 DAiqrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVertnaacAALDKKQRNFD----KIL 1460
Cdd:COG4913 378 SA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI-------ASLERRKSNIParllALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1461 AEWKQkyeethaELEASQKEARSLGtELFKMKNAYEESLDQLETLKR--------ENKNLQQeISDLTEQIAEGGK-RIH 1531
Cdd:COG4913 447 DALAE-------ALGLDEAELPFVG-ELIEVRPEEERWRGAIERVLGgfaltllvPPEHYAA-ALRWVNRLHLRGRlVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1532 ELEKIKKQVEQEKCELQAALEEaeasLEHEEGKILR-IQLELNQvkseidRKIAEKDEEIDQLKRNHIRVVESMQSTLDA 1610
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLAGK----LDFKPHPFRAwLEAELGR------RFDYVCVDSPEELRRHPRAITRAGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1611 E---------IRSRN----DAIRIKKKMEGDLNEMEIQLNHANRmAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQ 1677
Cdd:COG4913 588 TrhekddrrrIRSRYvlgfDNRAKLAALEAELAELEEELAEAEE-RLEALEAELDALQERREALQRLAEYSWDEIDVASA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1678 LAMVERranlLQAEIEELRAT---LEQTERSRKIAEQELLDASERVQLLHTQntslintKKKLETDISQIQgemEDIVQE 1754
Cdd:COG4913 667 EREIAE----LEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGE-------IGRLEKELEQAE---EELDEL 732
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1755 ARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQ 1809
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
836-1912 |
1.25e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 63.92 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 836 WMKLFFKIKPLL-----KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLlKEKNDLQLQVQAEAEGLADAEE 910
Cdd:TIGR01612 556 WKKLIHEIKKELeeeneDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNI-SDKNEYIKKAIDLKKIIENNNA 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 911 RCDQLIKTKIQleakikEVTERAEDEEEINAELTAKKRKLEDEcselkkDIDDLELTLAKVEKEkhateNKVKNlTEEMA 990
Cdd:TIGR01612 635 YIDELAKISPY------QVPEHLKNKDKIYSTIKSELSKIYED------DIDALYNELSSIVKE-----NAIDN-TEDKA 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 991 GLDETIAKLTKEKKALQEAHQQTLD-DLQAEEDKVNTLTKAKIKLEQQVDDlegslEQEKKLRMDLERAKRKLegdlKLA 1069
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVElHLSNIENKKNELLDIIVEIKKHIHG-----EINKDLNKILEDFKNKE----KEL 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1070 QESIMDIENEKQQLDerlkKKEFEMSNLQSKIEDEQAIgiqlqKKIKElqarieeleeeieaerasraKAEKQRSDLSRE 1149
Cdd:TIGR01612 768 SNKINDYAKEKDELN----KYKSKISEIKNHYNDQINI-----DNIKD--------------------EDAKQNYDKSKE 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1150 -LEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI--DNLQRVKQKLEK 1226
Cdd:TIGR01612 819 yIKTISIKEDE----IFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFND 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1227 EKS---EMKMEIDDLASNVETVSKAKGNLeKMCRTLEDQVSELKSKeeeqQRLINDLTTQRGRLQTESGEFSRQLDEK-- 1301
Cdd:TIGR01612 895 SKSlinEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfd 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1302 EALVSQLSRGKQAFTQ-QIEELKRQLEEEVKAKNALAHALQSSRHDcdLLREQYEEEQESKAELQRALSKANSEVAQWRT 1380
Cdd:TIGR01612 970 NTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKEN--MLYHQFDEKEKATNDIEQKIEDANKNIPNIEI 1047
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1381 KYETDAIQRTEELEEAKKKLAQRLQaaEEHVEAVNAKCASLEKTKQRLqnevedlmldvertnaacaaldkKQRNFDKIL 1460
Cdd:TIGR01612 1048 AIHTSIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKL-----------------------KHYNFDDFG 1102
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1461 AEWKQKYEEthaELEASQKEARSLGTELFKMKNAYEESLDQLETLKREnknLQQEISDLtEQIAEGGKRIHELEKIKKQV 1540
Cdd:TIGR01612 1103 KEENIKYAD---EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDE---IKAQINDL-EDVADKAISNDDPEEIEKKI 1175
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1541 EQ--EKCELQAALEEAEASLEHEEGKILRIQLELNQVKSeIDRKIAEKD-----EEIDQLKRNHIRVVESMQSTLDaeir 1613
Cdd:TIGR01612 1176 ENivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKG-INLSYGKNLgklflEKIDEEKKKSEHMIKAMEAYIE---- 1250
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1614 srnDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNtqgilKDTQLHLDDALRGQEDLKEQ-LAMVErrANLLQAEI 1692
Cdd:TIGR01612 1251 ---DLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDD-----KDHHIISKKHDENISDIREKsLKIIE--DFSEESDI 1320
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1693 EELRATLEQTersrkiaeqeLLDASER---VQLLHTQNTSLINTKKkletdISQIQgEMEDIVQEARNAEEKAKKAITDA 1769
Cdd:TIGR01612 1321 NDIKKELQKN----------LLDAQKHnsdINLYLNEIANIYNILK-----LNKIK-KIIDEVKEYTKEIEENNKNIKDE 1384
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1770 AMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQK------RNVEA 1843
Cdd:TIGR01612 1385 LDKSEKLIKKIKDDINLEECKSKIESTLDDKD--IDECIK-KIKELKNHILSEESNIDTYFKNADENNEnvlllfKNIEM 1461
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1844 VKGLRKHERRVKELTYQTEEDRkNILRLQDLVDklqaKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEE 1912
Cdd:TIGR01612 1462 ADNKSQHILKIKKDNATNDHDF-NINELKEHID----KSKGCKDEADKNAKAIEKNKELFEQYKKDVTE 1525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
897-1216 |
1.42e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 897 QVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAE--------DEEEINAeltakkRKLEDECSELKKDIDDLELT- 967
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDV------ASAEREIAELEAELERLDASs 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 968 --LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKikLEQQVDDLEGSl 1045
Cdd:COG4913 685 ddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGD- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1046 EQEKKLRMDLERAKRKLEGDLKLAQESIMDIenekqqLDERLKKKEFEMSNLQSKIEDE----------QAIGI-QLQKK 1114
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESLpeylalldrlEEDGLpEYEER 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1115 IKELqarieeleeeieaerasRAKAEKQ-----RSDLSRELEEISERLEEA---------GGATSAQIEMNKKREAEFQK 1180
Cdd:COG4913 836 FKEL-----------------LNENSIEfvadlLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVRE 898
|
330 340 350
....*....|....*....|....*....|....*.
gi 1958661053 1181 MRRDLEEATLQHEATAATLRKKHADSVAELGEQIDN 1216
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1055-1595 |
1.59e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.38 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1055 LERAKRKLEGDLKLAQESIMDIENekqqLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERA 1134
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1135 SR-----------------AKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1197
Cdd:PRK01156 240 ALnelssledmknryeseiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1198 TLRKKHADSVAELGEQIDNLQRVKQKleKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLI 1277
Cdd:PRK01156 320 EINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1278 NDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE----EEVKAKNALAHALQSSRHdcdlLREQ 1353
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngQSVCPVCGTTLGEEKSNH----IINH 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1354 YEEE----QESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ-------------RLQAAEEHVEAVNA 1416
Cdd:PRK01156 474 YNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1417 KCASLEKTKQRLQNEvEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYE 1496
Cdd:PRK01156 554 RYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1497 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVk 1576
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI- 711
|
570
....*....|....*....
gi 1958661053 1577 SEIDRKIAEKDEEIDQLKR 1595
Cdd:PRK01156 712 NELSDRINDINETLESMKK 730
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1487-1933 |
2.18e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.89 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1487 ELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKIL 1566
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1567 RIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVesmqsTLDAEIRSRNDAIRI-----------KKKMEGDLNEMEIQ 1635
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKV-----TTEAKIKKLEEDILLledqnsklskeRKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1636 LNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLD 1715
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1716 ASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDiVQEARNAEEKAKKaitdaammaeelkkeqDTSAHLERMKKNMEQ 1795
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLES-ERAARNKAEKQRR----------------DLGEELEALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1796 TVKDlqlrldEAEQLALKGgkkqiqKLEARVRELEGEVESEQKRNVEAVKGLR-KHERRVKELTYQTEEDRKNilrlqdl 1874
Cdd:pfam01576 311 TLDT------TAAQQELRS------KREQEVTELKKALEEETRSHEAQLQEMRqKHTQALEELTEQLEQAKRN------- 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1875 vdklqakvKSYKRQAEEAEEQSNTNLSK-FRKLQHELEEAEERADIAESQVNKLRVKSRE 1933
Cdd:pfam01576 372 --------KANLEKAKQALESENAELQAeLRTLQQAKQDSEHKRKKLEGQLQELQARLSE 423
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
887-1721 |
2.87e-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: 62.55 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 887 LLKEKNDLQLQVQAEAEGLADAEERC---DQLIKTKIQLEAKIKEV----TERAEDEEEINAELTAKKrkleDECSELKK 959
Cdd:pfam12128 153 TLLGRERVELRSLARQFALCDSESPLrhiDKIAKAMHSKEGKFRDVksmiVAILEDDGVVPPKSRLNR----QQVEHWIR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 960 DIDdlelTLAKVEKEKHatenkvknlteEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVD 1039
Cdd:pfam12128 229 DIQ----AIAGIMKIRP-----------EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLR 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1040 DLEgslEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ-LDERLKKKEFEMSNL---QSKIEDEQAIGIQLQKKI 1115
Cdd:pfam12128 294 TLD---DQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQLpswQSELENLEERLKALTGKH 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1116 KELQARIEeleeeieaerasrAKAEKQRSDLSRELEEISERLEeaggatsaqiemnkkreaefqKMRrdlEEATLQHEAT 1195
Cdd:pfam12128 371 QDVTAKYN-------------RRRSKIKEQNNRDIAGIKDKLA---------------------KIR---EARDRQLAVA 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1196 AATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEeeqqr 1275
Cdd:pfam12128 414 EDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVE----- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1276 linDLTTQRGRLQTESGEFSRQLDEKEALVSQLSrgkqaftQQIEELKRQLeeeVKAKNALAHALQSSRHDCdllrEQYE 1355
Cdd:pfam12128 489 ---RLQSELRQARKRRDQASEALRQASRRLEERQ-------SALDELELQL---FPQAGTLLHFLRKEAPDW----EQSI 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1356 EEQESKAELQRA---LSKANSEVAQWRTKY----ETDAIQRTEELEeAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRL 1428
Cdd:pfam12128 552 GKVISPELLHRTdldPEVWDGSVGGELNLYgvklDLKRIDVPEWAA-SEEELRERLDKAEEALQSAREKQAAAEEQLVQA 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1429 QNEVEDLMLDVERTNAACA-ALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKR 1507
Cdd:pfam12128 631 NGELEKASREETFARTALKnARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1508 ENKNLQQE-----ISDLTEQIAeggkrihelekikkQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRK 1582
Cdd:pfam12128 711 EARTEKQAywqvvEGALDAQLA--------------LLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKRE 776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1583 IAEKDEEIDQLKRNHIRVVES---MQSTLDaeirSRNDAIRIKK-KMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILK 1658
Cdd:pfam12128 777 IRTLERKIERIAVRRQEVLRYfdwYQETWL----QRRPRLATQLsNIERAISELQQQLARLIADTKLRRAKLEMERKASE 852
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1659 DTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIeELRATLEQTERSRKIAEQELLDASERVQ 1721
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG-SIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1395-1595 |
2.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1395 EAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAEL 1474
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1475 EASQKEARSLGTELFKMKNA-----------YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQe 1543
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1544 kceLQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKR 1595
Cdd:COG4942 179 ---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
846-1309 |
3.60e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 61.76 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 846 LLKSAETEKEMATMK-----EEFQKTKDELAKSEAKRKE-----LEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQL 915
Cdd:pfam10174 264 LLHTEDREEEIKQMEvykshSKFMKNKIDQLKQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 916 iktkiqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDET 995
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 996 IAKLTKEKKALQEAHQQ------TLDDLQAEEDKVNTLTKAKIKLEQQVDDLEgsLEQEKKLRMDLERAKRKLEGDLKLA 1069
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNtdtaltTLEEALSEKERIIERLKEQREREDRERLEE--LESLKKENKDLKEKVSALQPELTEK 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1070 QESIMDIENEKQQLDERLKKKEFEMSNLQskiedeqaigIQLQKKIKELQARIEELEEEIEAERASRAKAEkqRSDLSRE 1149
Cdd:pfam10174 495 ESSLIDLKEHASSLASSGLKKDSKLKSLE----------IAVEQKKEECSKLENQLKKAHNAEEAVRTNPE--INDRIRL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1150 LEEISERLEEAGGATSAQIE--MNKKREAEFQKMRRDLEEATLqhEATAATLRKKHADSVAELgeqidnlqRVKQKLEKE 1227
Cdd:pfam10174 563 LEQEVARYKEESGKAQAEVErlLGILREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKVANI--------KHGQQEMKK 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1228 KSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDE-----KE 1302
Cdd:pfam10174 633 KGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEilemkQE 712
|
....*..
gi 1958661053 1303 ALVSQLS 1309
Cdd:pfam10174 713 ALLAAIS 719
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
854-1651 |
4.65e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 854 KEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKiQLEAKIKEVTERA 933
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 934 EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKV-----EKEKHATE-NKVKNLTEEMAGLDEtIAKLTKEKkaLQ 1007
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyQQAVQALERAKQLCG-LPDLTADN--AE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1008 EAHQQtlddLQAEEDkvnTLTKAKIKLEQQVDDLEGSLEQ-EKKLR--------MDLERAKRKlegdlklAQESIMDIEN 1078
Cdd:PRK04863 442 DWLEE----FQAKEQ---EATEELLSLEQKLSVAQAAHSQfEQAYQlvrkiageVSRSEAWDV-------ARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1079 EKQQlDERLKKKEFEMSNLQSKIEDEQaigiQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1158
Cdd:PRK04863 508 QRHL-AEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1159 EaggaTSAQIEMNKKREAEFQKmrrdLEEATLQHEATAATLRKKHADSVA---ELGEQIDNLQRVKQKLEKEKSEMKMEI 1235
Cdd:PRK04863 583 A----LRQQLEQLQARIQRLAA----RAPAWLAAQDALARLREQSGEEFEdsqDVTEYMQQLLERERELTVERDELAARK 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1236 DDLASNVETVSKAKGNLEKMCRTLEDQ-----VSELKSKEEEQQR--------------LINDLTTQRGRLQTE------ 1290
Cdd:PRK04863 655 QALDEEIERLSQPGGSEDPRLNALAERfggvlLSEIYDDVSLEDApyfsalygparhaiVVPDLSDAAEQLAGLedcped 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1291 ------------SGEFSRQLDEKEALV------SQLSR-------GKQAFTQQIEELKRQLEEEVkaknalahalqssrh 1345
Cdd:PRK04863 735 lyliegdpdsfdDSVFSVEELEKAVVVkiadrqWRYSRfpevplfGRAAREKRIEQLRAEREELA--------------- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1346 dcdllrEQYEEEQESKAELQRALSKANSEVA-------QWRTKYETDAIQRT--------EELEEAKKKLAQRLQAAEEH 1410
Cdd:PRK04863 800 ------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRrveleralADHESQEQQQRSQLEQAKEG 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1411 VEAVNaKCASLEKTKQR--LQNEVEDLMLDVERTNAACAALDKKQRNFDKI-------------LAEWKQKYEETHAELE 1475
Cdd:PRK04863 874 LSALN-RLLPRLNLLADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQDYQQAQQTQR 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1476 ASQKEARSLgTELFKMKN--AYEESLDQLEtlkrenknlqqEISDLTEQIAEggkRIhelekikKQVEQEKCELQAALEE 1553
Cdd:PRK04863 953 DAKQQAFAL-TEVVQRRAhfSYEDAAEMLA-----------KNSDLNEKLRQ---RL-------EQAEQERTRAREQLRQ 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1554 AEAslEHEEGKILRIQLelnqvKSEIDRKIAEKDEEIDQLKRNHIRVVESM-------QSTLDAEI---RSRNDAIrikk 1623
Cdd:PRK04863 1011 AQA--QLAQYNQVLASL-----KSSYDAKRQMLQELKQELQDLGVPADSGAeerararRDELHARLsanRSRRNQL---- 1079
|
890 900
....*....|....*....|....*...
gi 1958661053 1624 kmEGDLNEMEIQLNHANRMAAEALRNYR 1651
Cdd:PRK04863 1080 --EKQLTFCEAEMDNLTKKLRKLERDYH 1105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1589 |
6.86e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1352 EQYEEEQESKAELQRALSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNE 1431
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1432 vedlmldvertnaacaaLDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKN 1511
Cdd:COG4942 99 -----------------LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1512 LQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEE 1589
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1179-1923 |
7.08e-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: 61.39 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1179 QKMRRDLEEATLQHEATAATLRKKHadSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRT 1258
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRP--EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1259 LEDQVSELKSkeeeqqRLINDLTTQRGRLQTESGEFsrqldekEALVSQLSRGKQAftqQIEELKRQLEEEVKAKNALah 1338
Cdd:pfam12128 295 LDDQWKEKRD------ELNGELSAADAAVAKDRSEL-------EALEDQHGAFLDA---DIETAAADQEQLPSWQSEL-- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1339 ALQSSRHDCdLLREQYEEEQESKAELQRALSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAqrLQAAEEHV-EAVNAK 1417
Cdd:pfam12128 357 ENLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDRQLAVAEDD--LQALESELrEQLEAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1418 CASLEKTKQRLQNEVEDLMLdveRTNAACAALDKK--QRNFDKILaewkqkyEETHAELEASQKEARSLGTELFKMKNAY 1495
Cdd:pfam12128 432 KLEFNEEEYRLKSRLGELKL---RLNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRR 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1496 EESLDQLETLKRENKNLQQEISDLTEQ-IAEGGKRIHEL--------EKIKKQVEQE---KCELQAALEEAEASlehEEG 1563
Cdd:pfam12128 502 DQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLrkeapdweQSIGKVISPEllhRTDLDPEVWDGSVG---GEL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1564 KILRIQLELNQVkseidrKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEiqlnhanrMA 1643
Cdd:pfam12128 579 NLYGVKLDLKRI------DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET--------FA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1644 AEALRNYRNTQGILKDTQLHLDDALrgQEDLKEQLAMVERRANLLQaeieelratleqtersrkiAEQELLDASERVQLL 1723
Cdd:pfam12128 645 RTALKNARLDLRRLFDEKQSEKDKK--NKALAERKDSANERLNSLE-------------------AQLKQLDKKHQAWLE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1724 HTQNTSLINTKKKLETdISQIQGEM---EDIVQEARNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNMEQ 1795
Cdd:pfam12128 704 EQKEQKREARTEKQAY-WQVVEGALdaqLALLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLER 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1796 TVKDLQLRLDEAeqlalkggkkqiqkleARVRELEGEVESEQKRNVEAVkgLRKHERRVKELtyqteedRKNILRLQDLV 1875
Cdd:pfam12128 783 KIERIAVRRQEV----------------LRYFDWYQETWLQRRPRLATQ--LSNIERAISEL-------QQQLARLIADT 837
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1958661053 1876 DKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQ 1923
Cdd:pfam12128 838 KLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQ 885
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1667-1898 |
8.48e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1667 ALRGQEDLKEQLamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQG 1746
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1747 EMEDIVQEARNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTVKDLQLRLDE--AEQLALKGGKKQIQ 1820
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1821 KLEARVRELEGEVESEQKRNVEAVKglrKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNT 1898
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1196-1593 |
1.22e-08 |
|
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: 60.35 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1196 AATLRKKHADSVAELGEQIDNLQRVKQKL-EKEKSEMKMEIDDLASN--VETVSKAKGNLEKMCRTLEDqVSELKSKEEE 1272
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELeELSARESDLEQDYQAASdhLNLVQTALRQQEKIERYQED-LEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1273 QQRLINDLTTQRGRLQTEsgeFSRQLDEKEALVSQLSRGKQAF-TQQIEELKRQleeevKAKNALAHALQSSRHDcDLLR 1351
Cdd:COG3096 366 QEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLADYQQALdVQQTRAIQYQ-----QAVQALEKARALCGLP-DLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1352 EQYEEEQE-SKAELQralskansevaqwrtkyetdaiQRTEELEEAKKKLAQRLQAAEEHVEAVNAkcaslektkqrlqn 1430
Cdd:COG3096 437 ENAEDYLAaFRAKEQ----------------------QATEEVLELEQKLSVADAARRQFEKAYEL-------------- 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1431 eVEDLMLDVERTNAACAA--LDKKQRNFdKILAEWKQKYEETHAELE---ASQKEARSLGTELFKMKNAYEESLDQLETL 1505
Cdd:COG3096 481 -VCKIAGEVERSQAWQTAreLLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1506 KREnknLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCEL----------QAAL----EEAEASLEHEEG------KI 1565
Cdd:COG3096 559 LAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALerlrEQSGEALADSQEvtaamqQL 635
|
410 420
....*....|....*....|....*...
gi 1958661053 1566 LRIQLELNQVKSEIDRKIAEKDEEIDQL 1593
Cdd:COG3096 636 LEREREATVERDELAARKQALESQIERL 663
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1493-1936 |
1.75e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.84 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1493 NAYEESLDQL-ETL--KRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALE-EAEASLEHEEGKILRI 1568
Cdd:pfam10174 154 GARDESIKKLlEMLqsKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1569 QLELNQVK-SEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKME---GDLNEMEIQLnHANRMAA 1644
Cdd:pfam10174 234 VIEMKDTKiSSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-LALQTKL 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1645 EALRNYRNtqgilkDTQLHLddalrgqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLH 1724
Cdd:pfam10174 313 ETLTNQNS------DCKQHI-------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1725 TQNTSLINTKKKLETDISQIQGEMEDIVQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQT 1796
Cdd:pfam10174 380 GEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1797 VKDLQLRLDEAEQL--ALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDL 1874
Cdd:pfam10174 460 EREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1875 VDKLQakvksykrQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHT 1936
Cdd:pfam10174 540 LKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1008-1456 |
1.85e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1008 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQesimdIENEKQQLDERL 1087
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1088 KKKEFEMSNLQSKIEDEQaigiQLQKKIKELQARIEELEEEieaeraSRAKAEKQRSDLSRELEEISERLEEAGGATsaq 1167
Cdd:COG4717 149 EELEERLEELRELEEELE----ELEAELAELQEELEELLEQ------LSLATEEELQDLAEELEELQQRLAELEEEL--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1168 iemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSK 1247
Cdd:COG4717 216 ----EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1248 AKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE 1327
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1328 EEVKAKNALAHALQSSRHDCDLLREqYEEEQESKAELQRALSKANSEVAQWRTKYETDAI-QRTEELEEAKKKLAQRLQA 1406
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELeEELEELEEELEELEEELEE 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1407 AEEHVEAVNAKCASLEKT---------KQRLQNEVEDLMLDVERTNAACAALDKKQRNF 1456
Cdd:COG4717 451 LREELAELEAELEQLEEDgelaellqeLEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1410 |
2.00e-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: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQK---TKDELAKSEAKRK---ELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-QLE 923
Cdd:COG4913 222 DTFEAADALVEHFDDlerAHEALEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 924 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELK-KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE 1002
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1003 KKALQEAHQQTLDDLQAEEDKVNT----LTKAKIKLEQQVDDLEG---SLEQEK--------KLRMDLERAKRKLEGDLK 1067
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLERRKsniparllALRDALAEALGLDEAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1068 LAQESI-MDIENEKQQL----------------DERLKKkefemsnLQSKIEDEQAIG-IQLQKKIKELQARIEELEEEI 1129
Cdd:COG4913 462 FVGELIeVRPEEERWRGaiervlggfaltllvpPEHYAA-------ALRWVNRLHLRGrLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1130 EAERASRAKAEKQRSDLSRELEEIS-----ERLEEAGGATSA-----QIEMNKKReaeFQK-MRRDLEE----------- 1187
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAitragQVKGNGTR---HEKdDRRRIRSryvlgfdnrak 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1188 -ATLQHEATAATLRKKHADS-VAELGEQIDNLQRVKQKLEKeKSEMKMEIDDLASNVETVSKAKGNLEKM------CRTL 1259
Cdd:COG4913 612 lAALEAELAELEEELAEAEErLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREIAELEAELERLdassddLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1260 EDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAftQQIEELKRQLEEEVKAK--NALA 1337
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAveRELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1338 HALQSSRHDCDLLREQYEEEQESKaeLQRALSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQAAEEH 1410
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
976-1206 |
2.39e-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: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 976 HATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL----EQEKKL 1051
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1052 RMDLERAKRKLEGDLKLAQESimdieNEKQQLDERLKKKEFE-----MSNLQSKIEDEQAIGIQLQKKIKELQARIEELE 1126
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1127 EEIEAERASRAKAEKQRSDLSRELEEISERLEEAggatSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADS 1206
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARL----EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1388-1834 |
2.77e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 58.55 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1388 QRTEELE-------EAKKKLAQ---RLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFD 1457
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1458 KILAEWKQKYEEthaeLEASQKEARSLGTELFKMKNA-------------YEESLDQLETLKRENKNLQQEISDLTEQIA 1524
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1525 EGGKRIHELEKIKKQVEQEKCELQaaleEAEASLEHEEGKILRIQLELNQ-------VKSEIDRKIAEKD---EEIDQLK 1594
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1595 RNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQgiLKDTQLHLDDALRGQEDL 1674
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRER--LTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1675 KEQLAMVERRANLLQAEIEELRATLeqtersrkiaeqelldaservQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQE 1754
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1755 ARNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TVKDLQLRLDEAEQLALKGGKKQIQKLEARV 1826
Cdd:pfam05622 383 KEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKKI 462
|
....*...
gi 1958661053 1827 RELEGEVE 1834
Cdd:pfam05622 463 EHLERDFE 470
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
921-1249 |
2.98e-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: 58.37 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 921 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT 1000
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1001 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEK 1080
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1081 QQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSR------------ 1148
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1149 -----ELEEISERLEEA------GGATSAQ--------IEMNKKR----EAEFQKMRRDLEEATLQHEATAATL------ 1199
Cdd:pfam07888 275 hqarlQAAQLTLQLADAslalreGRARWAQeretlqqsAEADKDRieklSAELQRLEERLQEERMEREKLEVELgrekdc 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1200 -RKKHADSVAELGEQIDNL---QRVKQKLEKEKSEMKMEIDDLASNVETVSKAK 1249
Cdd:pfam07888 355 nRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1323 |
3.19e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.96 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKSEAKRKELE---EKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIK 927
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITmelQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 928 EVTERaedEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETiakLTKEKKALQ 1007
Cdd:pfam05483 433 ELKGK---EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL---LLENKELTQ 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1008 EAHQQTLDdLQAEEDKVNTLTKAKIKLEQQVDDLEgslEQEKKLRMDLERAKRKL--EGD-----LKLAQESIMDIENEK 1080
Cdd:pfam05483 507 EASDMTLE-LKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFiqKGDevkckLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1081 QQLDERLKKKEFEMSNLQSKIEDEQaigiqlqKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1160
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKN-------KNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1161 GGATSAQIEMNKKREaefQKMRRDLEEAtlqheataatlrKKHADSVAELGEQIDnlQRVKQKLekeksemkmeiddlAS 1240
Cdd:pfam05483 656 IDNYQKEIEDKKISE---EKLLEEVEKA------------KAIADEAVKLQKEID--KRCQHKI--------------AE 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1241 NVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIE 1320
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
...
gi 1958661053 1321 ELK 1323
Cdd:pfam05483 785 DKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1069-1284 |
3.68e-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: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1069 AQESIMDIENEKQQLDERLKKKEFEMSNLQSKIED--------EQAIgIQLQKKIKELQARIEELEEEIEAERASRAKAE 1140
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaalERRI-AALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1141 KQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKhadsVAELGEQIDNLQRV 1220
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1221 KQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQR 1284
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
987-1838 |
4.19e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 987 EEMAGLDETIAKLTKEK---KALQEAHQQTLDDLQAEEDkvnTLTKAKIKLEQQVDDLEGSL----------EQEKKLRM 1053
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1054 DLERAKRKLEGDL---KLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQarieeleeeie 1130
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE----------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1131 aerasRAKAEKQRSDLsrELEEISERLEEAggATSAQIEMNKKREAEfQKMRrDLEEATLQHEATAATLRKkhadsvaeL 1210
Cdd:PRK04863 425 -----RAKQLCGLPDL--TADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHSQFEQAYQLVRK--------I 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1211 GEQID--NLQRVKQKLEKEKSEMKMEIDDLASnvetvskakgnlekmcrtLEDQVSELKSKEEEQQ---RLINDLTTQRG 1285
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQRHLAEQLQQ------------------LRMRLSELEQRLRQQQraeRLLAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1286 RLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEE---EVKAKNALAHALQSSRHDCDLLREQYEEEQESK- 1361
Cdd:PRK04863 548 KNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqaRIQRLAARAPAWLAAQDALARLREQSGEEFEDSq 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1362 ---------AELQRALSKANSEVAQwrtkyetdaiqRTEELEEAKKKLAQ-------RLQAAEEHVEAV----------- 1414
Cdd:PRK04863 628 dvteymqqlLERERELTVERDELAA-----------RKQALDEEIERLSQpggsedpRLNALAERFGGVllseiyddvsl 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1415 -----------NAKCA----SLEKTKQRLQNEvEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEEthAELEASQ- 1478
Cdd:PRK04863 697 edapyfsalygPARHAivvpDLSDAAEQLAGL-EDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQWRYSRf 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1479 KEARSLGtelfkmKNAYEESLDQLetlkrenknlQQEISDLTEQIAEGGKRIHELEKIKKQV----------------EQ 1542
Cdd:PRK04863 774 PEVPLFG------RAAREKRIEQL----------RAEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEA 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1543 EKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEID--RKIAEkdeEIDQLKRNHI--RVVEsmqstLDAEIRSRNDA 1618
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalNRLLP---RLNLLADETLadRVEE-----IREQLDEAEEA 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1619 IRIKKKMEGDLNEMEIQLN--HANRMAAEALR-NYRNTQGILKDTQLHLDDalrgqedLKEqlaMVERRA--------NL 1687
Cdd:PRK04863 910 KRFVQQHGNALAQLEPIVSvlQSDPEQFEQLKqDYQQAQQTQRDAKQQAFA-------LTE---VVQRRAhfsyedaaEM 979
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1688 LQAE---IEELRATLEQTERSRKIAEQELLDASERvqllHTQNT-------SLINTKKKLETDISQiqgEMEDI-VQEAR 1756
Cdd:PRK04863 980 LAKNsdlNEKLRQRLEQAEQERTRAREQLRQAQAQ----LAQYNqvlaslkSSYDAKRQMLQELKQ---ELQDLgVPADS 1052
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1757 NAEEKAkkaitdaammaeelkkeqdtSAHLERMKKNMEQTvkdlQLRLDEAEqlalkggkKQIQKLEARVRELEGEVESE 1836
Cdd:PRK04863 1053 GAEERA--------------------RARRDELHARLSAN----RSRRNQLE--------KQLTFCEAEMDNLTKKLRKL 1100
|
..
gi 1958661053 1837 QK 1838
Cdd:PRK04863 1101 ER 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1257-1498 |
4.46e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1257 RTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNAL 1336
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1337 AHALQssrhdcDLLREQYEEEQESKAELqrALSKANSEVAQWRTKYETDAIQ----RTEELEEAKKKLAQRLQAAEEHVE 1412
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1413 AVNAKCASLEKTKQRLQNEvedlmldvertnaacaaldKKQRNfdKILAEWKQKYEETHAELEASQKEARSLGTELFKMK 1492
Cdd:COG4942 175 ELEALLAELEEERAALEAL-------------------KAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*.
gi 1958661053 1493 NAYEES 1498
Cdd:COG4942 234 AEAAAA 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
981-1942 |
4.70e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.52 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 981 KVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtlddLQAEEDKVntltkakIKLEQQVDDLegsleQEKKLRMDLERAK- 1059
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKE----LEEENEDS-------IHLEKEIKDL-----FDKYLEIDDEIIYi 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1060 RKLEGDLKlaqESIMDIENEkqqlDERLKKKefemSNLQSKIEDEQAIgIQLQKKIKELQARIEELEEEIEAERASRAKA 1139
Cdd:TIGR01612 599 NKLKLELK---EKIKNISDK----NEYIKKA----IDLKKIIENNNAY-IDELAKISPYQVPEHLKNKDKIYSTIKSELS 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1140 EKQRSDLSRELEEISERLEEA---GGATSAQIE-MNKKREAEFQKMRrDLEEATLQ-HEATAATLRKKHADSVAEL---- 1210
Cdd:TIGR01612 667 KIYEDDIDALYNELSSIVKENaidNTEDKAKLDdLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhi 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1211 -GEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINdlttqrgrlqt 1289
Cdd:TIGR01612 746 hGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD----------- 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1290 ESGEFSRQLDEKEALVSQLsrgkqaftqqIEELKRQLEEEVKAKNALAHAlqssRHDCdllREQYEEEQESKAELqraLS 1369
Cdd:TIGR01612 815 KSKEYIKTISIKEDEIFKI----------INEMKFMKDDFLNKVDKFINF----ENNC---KEKIDSEHEQFAEL---TN 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1370 KANSEVAQWR-TKYETDAIQRTEELEEAKKKLAQR------LQAAEEHVEAVNAKCASLEK--TKQRLQNEVEDLMLDV- 1439
Cdd:TIGR01612 875 KIKAEISDDKlNDYEKKFNDSKSLINEINKSIEEEyqnintLKKVDEYIKICENTKESIEKfhNKQNILKEILNKNIDTi 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1440 ERTNaacaALDKKQRN-FDKILAEWKQKYEETHAELEASQKEARSlgTELFKMKNAYEESL---------DQLETLKREN 1509
Cdd:TIGR01612 955 KESN----LIEKSYKDkFDNTLIDKINELDKAFKDASLNDYEAKN--NELIKYFNDLKANLgknkenmlyHQFDEKEKAT 1028
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1510 KNLQQEISDLTEQIAEGGKRIH--------ELEK-IKKQVEQEKCELqaaLEEAEASLEHEEGkiLRIQLELNQVKSEID 1580
Cdd:TIGR01612 1029 NDIEQKIEDANKNIPNIEIAIHtsiyniidEIEKeIGKNIELLNKEI---LEEAEINITNFNE--IKEKLKHYNFDDFGK 1103
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1581 RKIAEKDEEIDQLKRNhirvVESMQSTLDAEIrsrNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNyRNTQGILKDT 1660
Cdd:TIGR01612 1104 EENIKYADEINKIKDD----IKNLDQKIDHHI---KALEEIKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKI 1175
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1661 QlhlddalrgqedlkEQLAMVERRANLLQaEIEELRATLEQTERsrkiaEQELLDASERVQLLHTQNTSLI------NTK 1734
Cdd:TIGR01612 1176 E--------------NIVTKIDKKKNIYD-EIKKLLNEIAEIEK-----DKTSLEEVKGINLSYGKNLGKLflekidEEK 1235
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1735 KKLETDISQIQGEMEDI--VQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrldeAEQLAL 1812
Cdd:TIGR01612 1236 KKSEHMIKAMEAYIEDLdeIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR-----EKSLKI 1310
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1813 KGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKherrvkeltyqtEEDRKNILRLQDlVDKLQAKVKSYKRQAEEA 1892
Cdd:TIGR01612 1311 IEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNE------------IANIYNILKLNK-IKKIIDEVKEYTKEIEEN 1377
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1893 EEQSNTNLSKFRKL------QHELEEAEERAD--IAESQVNKLRVKSREVHTKVISEE 1942
Cdd:TIGR01612 1378 NKNIKDELDKSEKLikkikdDINLEECKSKIEstLDDKDIDECIKKIKELKNHILSEE 1435
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
905-1881 |
5.47e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.52 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 905 LADAEERCDQLIKTKIqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE-------KHA 977
Cdd:TIGR01612 527 GFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 978 TENKVKNLTEE-----------------MAGLDEtIAKLTKE----------------KKALQEAHQQTLDDLQ------ 1018
Cdd:TIGR01612 605 LKEKIKNISDKneyikkaidlkkiiennNAYIDE-LAKISPYqvpehlknkdkiystiKSELSKIYEDDIDALYnelssi 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1019 -AEEDKVNTLTKAKI-----KLEQQVDDLEGSLEQEKKLRM-DLERAKRKLEGDLKLAQESIM-DIENEKQQLDERLKKK 1090
Cdd:TIGR01612 684 vKENAIDNTEDKAKLddlksKIDKEYDKIQNMETATVELHLsNIENKKNELLDIIVEIKKHIHgEINKDLNKILEDFKNK 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1091 EFEMSNlqsKIEDEQAIGIQLQK---KIKELQarieELEEEIEAERASRAKAEKQRSDLSRE-LEEISERLEEaggaTSA 1166
Cdd:TIGR01612 764 EKELSN---KINDYAKEKDELNKyksKISEIK----NHYNDQINIDNIKDEDAKQNYDKSKEyIKTISIKEDE----IFK 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1167 QIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI--DNLQRVKQKLEKEKS---EMKMEIDDLASN 1241
Cdd:TIGR01612 833 IINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSlinEINKSIEEEYQN 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1242 VETVSKAKGNLeKMCRTLEDQVSELKSKeeeqQRLINDLTTQRGRLQTESGEFSRQLDEK--EALVSQLSRGKQAFTQ-Q 1318
Cdd:TIGR01612 913 INTLKKVDEYI-KICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKINELDKAFKDaS 987
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1319 IEELKRQLEEEVKAKNALAHALQSSRHdcDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1398
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIG 1065
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1399 KLAQRLQaaEEHVEAVNAKCASLEKTKQRLqnevedlmldvertnaacaaldkKQRNFDKILAEWKQKYEEthaELEASQ 1478
Cdd:TIGR01612 1066 KNIELLN--KEILEEAEINITNFNEIKEKL-----------------------KHYNFDDFGKEENIKYAD---EINKIK 1117
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1479 KEARSLGTELFKMKNAYEESLDQLETLKREnknLQQEISDLtEQIAEGGKRIHELEKIKKQVEQ--EKCELQAALEEAEA 1556
Cdd:TIGR01612 1118 DDIKNLDQKIDHHIKALEEIKKKSENYIDE---IKAQINDL-EDVADKAISNDDPEEIEKKIENivTKIDKKKNIYDEIK 1193
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1557 SLEHEEGKILRIQLELNQVKS-------EIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDaEIRSRNDAIRIKKKMEGDL 1629
Cdd:TIGR01612 1194 KLLNEIAEIEKDKTSLEEVKGinlsygkNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMDI 1272
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1630 N-EME--------------IQLNHANRMAAEALRNYRNTQG---------ILKDTQLHLDDALRGQEDLKEQLAMVERRA 1685
Cdd:TIGR01612 1273 KaEMEtfnishdddkdhhiISKKHDENISDIREKSLKIIEDfseesdindIKKELQKNLLDAQKHNSDINLYLNEIANIY 1352
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1686 NLLQAE-----IEELRATLEQTERSRKIAEQElLDASERVQLLHTQNTSLINTKKKLETDI----------------SQI 1744
Cdd:TIGR01612 1353 NILKLNkikkiIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKKIKDDINLEECKSKIESTLddkdidecikkikelkNHI 1431
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1745 QGEMEDIVQEARNAEE-------------------------KAKKAITDAAMMAEELKKEQDTS-----------AHLER 1788
Cdd:TIGR01612 1432 LSEESNIDTYFKNADEnnenvlllfkniemadnksqhilkiKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEK 1511
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1789 MKKNMEQTVKDLQLRLDEAEQLALKGG----KKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEED 1864
Cdd:TIGR01612 1512 NKELFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKS 1591
|
1130
....*....|....*..
gi 1958661053 1865 RKNILRLQDLVDKLQAK 1881
Cdd:TIGR01612 1592 NKAAIDIQLSLENFENK 1608
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
851-1248 |
5.83e-08 |
|
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: 57.84 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEgladaEERCDQLIKTKIQLEAKIKEVT 930
Cdd:pfam09731 53 EDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE-----KEATKDAAEAKAQLPKSEQEKE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 931 ERAEDEEEINAELTAKKRKLEdecselkkdiddLELTLAKVEKEKHATEN-KVKNLTEEMAGLDETIAKLTKEKKALQEA 1009
Cdd:pfam09731 128 KALEEVLKEAISKAESATAVA------------KEAKDDAIQAVKAHTDSlKEASDTAEISREKATDSALQKAEALAEKL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1010 HQQTLDDLQAEEDKVN-TLTKAKIKLEQQVDDL---EGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEkqqLDE 1085
Cdd:pfam09731 196 KEVINLAKQSEEEAAPpLLDAAPETPPKLPEHLdnvEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPD---IIP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1086 RLKKKE-FEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEaerasrakaEKQRSDLSRELEEISERLEEAGGAT 1164
Cdd:pfam09731 273 VLKEDNlLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERAL---------EKQKEELDKLAEELSARLEEVRAAD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1165 SAQIEmnKKREAEFQKMRRDLEE---ATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASN 1241
Cdd:pfam09731 344 EAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLAN 421
|
....*..
gi 1958661053 1242 VETVSKA 1248
Cdd:pfam09731 422 LKGLEKA 428
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1363-1782 |
7.90e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1363 ELQRALSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQAAEEHVEAvnakcASLEKTKQRLQNEVEDLMLDVE 1440
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1441 RTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSlgtELFKMKNAYEESLDQLETLKRENKNLQQEISDLT 1520
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1521 EQIaEGGKRIHELEKIKKQVEQEK---------CELQAALEEAEASLEHEEGK------ILRIQLELNQVKSEIDRKIAE 1585
Cdd:COG4717 227 EEL-EQLENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1586 KDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRmAAEALRNYRNTQGILKDTQLHLD 1665
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1666 DALRG-------QEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIA--EQELLDASERVQLLHTQNTSLINTKKK 1736
Cdd:COG4717 385 EELRAaleqaeeYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEelEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958661053 1737 LETD--ISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDT 1782
Cdd:COG4717 465 LEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1135-1337 |
1.52e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1135 SRAKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkrEAEFQKMRRDLEEATLQHEATAATLRKKHADsVAELGEQI 1214
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1215 DNLQrvkQKLEKEKSEMKM----------------------EIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEE 1272
Cdd:COG3883 75 AEAE---AEIEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1273 QQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALA 1337
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
658-682 |
1.57e-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: 1.57e-07
10 20
....*....|....*....|....*
gi 1958661053 658 FRENLNKLMTNLRSTHPHFVRCIIP 682
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1079 |
1.88e-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: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 868 DELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKK 947
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 948 RKLEDECSEL------KKDIDDLELTL-----AKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDD 1016
Cdd:COG4942 100 EAQKEELAELlralyrLGRQPPLALLLspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1017 LQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENE 1079
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1319-1894 |
1.99e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.45 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1319 IEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYE--TDAIQRTEELEEA 1396
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1397 KKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLqNEVEDLMLDVERTNAACAALDKKQ-RNFDKILAEWK---QKYEETHA 1472
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1473 ELEASQKEArslgtelfkmknayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALE 1552
Cdd:PRK01156 330 KLSVLQKDY------------------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1553 EAEASLEHEEGKILRIQLELNQVKSEIDR---KIAEKDEEIDQLKRNHIRVVESMQ-----------STLDAEIRSRnda 1618
Cdd:PRK01156 392 FISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSN--- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1619 iRIKKKMEGDLNEMEIQLNHANRMAAEalrnyrntqgilkdtqlhLDDALRGQEDLKEQLAMVE-RRANLLQAEIEELRA 1697
Cdd:PRK01156 469 -HIINHYNEKKSRLEEKIREIEIEVKD------------------IDEKIVDLKKRKEYLESEEiNKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1698 TLEQTersrKIAEQELLDASERVQLLHTQNTSL-INTKKKLETDISQIQGEMEDIVQEA-RNAEEKAKKAITDAAMMAEE 1775
Cdd:PRK01156 530 DLEDI----KIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETnRSRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1776 LKKE-QDTSAHLERMKKNMEQTVKDLQLRLDEAEQLalkggKKQIQKLEARVRELE---GEVESEQKRNVEAVKGLRKHE 1851
Cdd:PRK01156 606 IEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQEN-----KILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIE 680
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1958661053 1852 RRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEE 1894
Cdd:PRK01156 681 DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
848-1461 |
2.16e-07 |
|
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: 56.39 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 848 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGL---------------------- 905
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLeerlkaltgkhqdvtakynrrr 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 906 ADAEERCDQLIKTKIQLEAKIKEVTER----AED-----EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH 976
Cdd:pfam12128 382 SKIKEQNNRDIAGIKDKLAKIREARDRqlavAEDdlqalESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 977 ATENKvKNLTEEMAGLDETIAKLTKEKKALQE-------AHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSL-EQE 1048
Cdd:pfam12128 462 LLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1049 KKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDE------RLKKKEFEMSnlqSKIEDEQAIGIQLQKKIKELQARI 1122
Cdd:pfam12128 541 RKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDVP---EWAASEEELRERLDKAEEALQSAR 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1123 EeleeeieaeraSRAKAEKQRSDLSRELEEISERLEEAGGAtsaqiemnkkreaeFQKMRRDLEEATLQHEATAATLRKK 1202
Cdd:pfam12128 618 E-----------KQAAAEEQLVQANGELEKASREETFARTA--------------LKNARLDLRRLFDEKQSEKDKKNKA 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1203 HADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGN-LEKMCRTLEDQVSELKSKEEEQqrlindLT 1281
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvVEGALDAQLALLKAAIAARRSG------AK 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1282 TQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRhdcDLLREQYEEEQESK 1361
Cdd:pfam12128 747 AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRR---PRLATQLSNIERAI 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1362 AELQRALSKANSEVAQWRTKYET--DAIQRTE-ELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQneVEDLMLD 1438
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMerKASEKQQvRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ--LEDLKLK 901
|
650 660
....*....|....*....|...
gi 1958661053 1439 VERtnaACAALDKKQRNFDKILA 1461
Cdd:pfam12128 902 RDY---LSESVKKYVEHFKNVIA 921
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
925-1415 |
2.43e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 925 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLT---K 1001
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1002 EKKALQEAHQQTLDDLQAEEDKVNTLTKAK---------------------IKLEQQVDDLEGSLEQEKKLRMDLERAKR 1060
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYKELEerhmkiindpvyknrnyindyFKYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1061 KLEgDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAE 1140
Cdd:PRK01156 330 KLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1141 KQRSDLSRELEEISERLeeagGATSAQIEMNKKREAEFQKMRRDLEE-------ATLQHEATAATLRKKHADSVAELGEQ 1213
Cdd:PRK01156 409 KELNEINVKLQDISSKV----SSLNQRIRALRENLDELSRNMEMLNGqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1214 IDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRT----LEDQVSELKSKEEEQQRLIN--------DLT 1281
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAdledIKIKINELKDKHDKYEEIKNrykslkleDLD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1282 TQRGR---------------LQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHD 1346
Cdd:PRK01156 565 SKRTSwlnalavislidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKIL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1347 CDLLREQYEEEQESKAE------------------------LQRALSKANSEVAQWRTKYETDaIQRTEELEEAKKKLAQ 1402
Cdd:PRK01156 645 IEKLRGKIDNYKKQIAEidsiipdlkeitsrindiednlkkSRKALDDAKANRARLESTIEIL-RTRINELSDRINDINE 723
|
570
....*....|...
gi 1958661053 1403 RLQAAEEHVEAVN 1415
Cdd:PRK01156 724 TLESMKKIKKAIG 736
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1671-1919 |
2.72e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1671 QEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI--AEQELLDASERVQLLHTQNTSLintkkklETDISQIQGEM 1748
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSEL-------ESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1749 edivQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtvkdLQLRLDEAEQLALKGGK-KQIQKLEARVR 1827
Cdd:COG3206 236 ----AEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQL----------AELEAELAELSARYTPNhPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1828 ELEGEVESEQKRNVEAVKG-LRKHERRVKELTYQTEEDRKNILRLQdlvdKLQAKVKSYKRQAEEAEEQSNTNLSKFRKL 1906
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
250
....*....|...
gi 1958661053 1907 QheLEEAEERADI 1919
Cdd:COG3206 378 R--LAEALTVGNV 388
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1196-1557 |
3.04e-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: 55.29 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1196 AATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQR 1275
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1276 LINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELK-------RQLEEEVKAKNALAHALQSSRHDCD 1348
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKerakkagAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1349 LLREQYEEEQESKAELQRALSKANSEVAQWRTKYETdAIQRTEELEEAKKKLA---QRLQAAEEHVEAVNAKCASLEKTK 1425
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT-AHRKEAENEALLEELRslqERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1426 QRLQNEVEDLMLDVERTNAACAALDKKQRNFDkilAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEE-------- 1497
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGR---ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEermerekl 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661053 1498 ----------SLDQLETLKRENKNL-------QQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEAS 1557
Cdd:pfam07888 345 evelgrekdcNRVQLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPD 421
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1253-1525 |
4.30e-07 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 55.24 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1253 EKMCRtLEDQVSELKSK-------EEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQ 1325
Cdd:pfam09726 395 DALVR-LEQDIKKLKAElqasrqtEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1326 LEEEVKAKNALAHALQSSRhdcdllreQYEEEQESKAELQRALSKANSevaqwrtKYETDAI-QRTEELEEAKKKLAQRL 1404
Cdd:pfam09726 474 LKAEQEARASAEKQLAEEK--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDI 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1405 QAAEEHVEAVNAKCASLEKTKQRlQNEVEDLMldvertnAACAALDKKQRNFDKILAewkqkyEETHAELeasqkearsl 1484
Cdd:pfam09726 539 KLKEEQIRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQDKNQHLENSLS------AETRIKL---------- 594
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958661053 1485 gtELFkmkNAYEESLDQLETLKRENKNLQQEISDLTEQIAE 1525
Cdd:pfam09726 595 --DLF---SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1394-1615 |
5.14e-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: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1394 EEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAAcaaLDKKQRNFDKILAEWKQKYEETHAE 1473
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1474 LEASQKEARSLGT-ELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkriheLEKIKKQVEQEKCELQAALE 1552
Cdd:COG3883 92 ARALYRSGGSVSYlDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1553 EAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSR 1615
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1537-1775 |
5.32e-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: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1537 KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQvkseIDRKIAEKDEEIDQLkrnhirvvESMQSTLDAEIRSRN 1616
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRAL--------EQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1617 DAIrikKKMEGDLNEMEIQLNhanRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELR 1696
Cdd:COG4942 90 KEI---AELRAELEAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1697 ATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEE 1775
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
869-1024 |
6.26e-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: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 869 ELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER-AEDEEEINAELTAKK 947
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 948 RK-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKV 1024
Cdd:COG1579 91 YEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1579-1933 |
8.39e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.14 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1579 IDRKIAEKDEEIDQLKRNHIRVVESM--QSTLDAEIRSRNDAIRIKKKMEGDLNEMEiqlnhaNRMAAEALRNYR--NTQ 1654
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDNEQQT------NSKDGEQLSDFQleDLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1655 GILKDTQ---LHLDDA-LRGQEDLKEQLAmvERRAnlLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSL 1730
Cdd:PLN02939 135 GMIQNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNEL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1731 INTKKKLETDISQIQGEMEDIVQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQLRLDEA 1807
Cdd:PLN02939 211 LIRGATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1808 EQLALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKH---ERRVKELTYQTEEdrKNILRLQ-DLVDKLQAKVK 1883
Cdd:PLN02939 284 QEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLK 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1884 SYKRQAEEAEEQSNtnlSKFRKLQHELEEAEeraDIAESQVNKLRVKSRE 1933
Cdd:PLN02939 362 LLEERLQASDHEIH---SYIQLYQESIKEFQ---DTLSKLKEESKKRSLE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1457-1620 |
8.60e-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: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1457 DKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE----------- 1525
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1526 ----GG------------------KRIHELEKI----KKQVEQEKcELQAALEEAEASLEHEEGKILRIQLELNQVKSEI 1579
Cdd:COG3883 95 lyrsGGsvsyldvllgsesfsdflDRLSALSKIadadADLLEELK-ADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958661053 1580 DRKIAEKDEEIDQLKRNHIRVVESMQStLDAEIRSRNDAIR 1620
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAA 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1439-1916 |
8.88e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1439 VERTNAACAALDKKQRNFDKILAEwKQKYEETHAELEASQKEARSLGTELFKMKNAYEEsLDQLETLKRENKNLQQEISD 1518
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1519 LTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHI 1598
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1599 RVVESMQSTLDAEIRSRNDAIRIkkkmegDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQL 1678
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1679 AMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLEtdISQIQGEMEDIVQEARNA 1758
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1759 EEkakKAITDAAMMAEELKKEQDTSAHLERmkknmeqtvkDLQLRLDEAEQLALKGGKKQiqkLEARVRELEGEVESEQK 1838
Cdd:COG4717 383 DE---EELRAALEQAEEYQELKEELEELEE----------QLEELLGELEELLEALDEEE---LEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1839 RnveavkgLRKHERRVKELTYQTEEdrkniLRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEER 1916
Cdd:COG4717 447 E-------LEELREELAELEAELEQ-----LEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1465-1717 |
1.02e-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: 53.23 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1465 QKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEK 1544
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1545 CELQAALEEAEASLeHEEGKILRIQLELNQVKSEidrKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKK 1624
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1625 MEGDLNEMEIQlnhanRMAAEALRNYRNTQgilkdtqlhlddalrgQEDLKEQLAMVERRANLLQAEIEELRATLEQTER 1704
Cdd:COG4942 176 LEALLAELEEE-----RAALEALKAERQKL----------------LARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|...
gi 1958661053 1705 SRKIAEQELLDAS 1717
Cdd:COG4942 235 EAAAAAERTPAAG 247
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
824-1616 |
1.06e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 824 NIRAFMNVKHWPWMKLFFKIKPLLKSAETEKemaTMKEEFQKT----KDELAK--SEAKRKELEEKMVSLLKEKNDLQLQ 897
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESNLIEK---SYKDKFDNTlidkINELDKafKDASLNDYEAKNNELIKYFNDLKAN 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 898 VQAEAEGLA----DAEERCDQLIKTKIQ------------LEAKIKEVTERAEDEEEINAELTAKK--RKLEDECSELKK 959
Cdd:TIGR01612 1009 LGKNKENMLyhqfDEKEKATNDIEQKIEdanknipnieiaIHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNE 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 960 DIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIkl 1034
Cdd:TIGR01612 1089 IKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAI-- 1163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1035 eqQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEsIMDIENEK----------------------QQLDERLKKKEF 1092
Cdd:TIGR01612 1164 --SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKtsleevkginlsygknlgklflEKIDEEKKKSEH 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1093 EMSNLQSKIEDEQAIGIQLQKKIKELqARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatSAQIEMNK 1172
Cdd:TIGR01612 1241 MIKAMEAYIEDLDEIKEKSPEIENEM-GIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDF 1314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1173 KREAEFQKMRRDLEEATLQHEataatlrkKHADSVAELGEQIDNLQRVKQ--KLEKEKSEMKMEIDDLASNVETVSKAKG 1250
Cdd:TIGR01612 1315 SEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDELD 1386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1251 NLEKMCRTLEDQVS--ELKSKEEEQ------QRLINDLTTQRGRLQTESGE---FSRQLDEKEALVSQLSRgkqafTQQI 1319
Cdd:TIGR01612 1387 KSEKLIKKIKDDINleECKSKIESTlddkdiDECIKKIKELKNHILSEESNidtYFKNADENNENVLLLFK-----NIEM 1461
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1320 EELKRQLEEEVKAKNAlahalqSSRHDCDL--LREQYEEEQESKAELQRalskansevaqwrtkyETDAIQRTEELEEAK 1397
Cdd:TIGR01612 1462 ADNKSQHILKIKKDNA------TNDHDFNIneLKEHIDKSKGCKDEADK----------------NAKAIEKNKELFEQY 1519
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1398 KKLAQRLQAAEEHVEAVNaKCASLEKTKQRLQNEVEDL----MLDVERTNAACAALDKKQRNFDKILAewkqKYEETHAE 1473
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKN-KFAKTKKDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIEDDAA----KNDKSNKA 1594
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1474 LEASQKEARSLGTELFKMKNAYEESLDQLetlkRENKNLQQEISDLT-----EQIAEGGKRIHELEKIKKQVEQEKcelq 1548
Cdd:TIGR01612 1595 AIDIQLSLENFENKFLKISDIKKKINDCL----KETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQK---- 1666
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1549 AALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVV-ESMQSTLDAEIRSRN 1616
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIkELIEPTIENLISSFN 1735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1050 |
1.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 860 KEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEI 939
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 940 NAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDE 994
Cdd:COG4942 106 LAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 995 TIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1050
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
844-1093 |
1.31e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 844 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKnDLQLQVQAEAEGLADAEER------------ 911
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEM-DRQAAIYAEQERMAMERERelerirqeerkr 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 912 -CDQLIKTKIQLE-AKIKEV----TERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKhATENKVKN 984
Cdd:pfam17380 361 eLERIRQEEIAMEiSRMRELerlqMERQQKNERVRQELeAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-ARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 985 LTEEMAGLDETIAKLTKEKKALQEAHQQtlddlQAEEDKVNTLTKAKIKLEQQVDD------LEGSLEQEKKLRMDLERA 1058
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLELEKEKRDRKRAEeqrrkiLEKELEERKQAMIEEERK 514
|
250 260 270
....*....|....*....|....*....|....*
gi 1958661053 1059 KRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFE 1093
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
921-1431 |
1.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 921 QLEAKIKEVTErAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK--HATENKVKNLTEEMAGLDETIAK 998
Cdd:COG4717 72 ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 999 LTKEKKALQEAHQQtlddlqaeedkvntltkaKIKLEQQVDDLEGSLEQEkklrmdLERAKRKLEGDLKLAQESIMDIEN 1078
Cdd:COG4717 151 LEERLEELRELEEE------------------LEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1079 EKQQLDERLKkkefemsnlqskiedeqaigiQLQKKIKELQARIEeleeeieaerasRAKAEKQRSDLSRELEEISERLe 1158
Cdd:COG4717 207 RLAELEEELE---------------------EAQEELEELEEELE------------QLENELEAAALEERLKEARLLL- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1159 eAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRvKQKLEKEKSEMKMEIDDL 1238
Cdd:COG4717 253 -LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA-LEELEEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1239 ASNVETvskakgnleKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAftQQ 1318
Cdd:COG4717 331 PPDLSP---------EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY--QE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1319 IEELKRQLEEEVKAKNALAHALqSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAqwRTKYETDAIQRTEELEEAKK 1398
Cdd:COG4717 400 LKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQ 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958661053 1399 KLAQRLQAAEEHVEAVNAKCAS---LEKTKQRLQNE 1431
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLAlelLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
941-1238 |
1.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 941 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAtENKVKNLTEE---MAGLDETIAKLTKEKKALQEAHQQtLDDL 1017
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELERLDASSDD-LAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1018 QAEEDKvntltkakikLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ-----LDERLKKKEF 1092
Cdd:COG4913 691 EEQLEE----------LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1093 EmsnlqskiEDEQAIGIQLQKKIKELqarieeleeeieaerasRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEmnk 1172
Cdd:COG4913 761 D--------AVERELRENLEERIDAL-----------------RARLNRAEEELERAMRAFNREWPAETADLDADLE--- 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661053 1173 kREAEFQKMRRDLEEATL-QHEATAATLRKKHAdsvaelGEQIDNLQrvkQKLEKEKSEMKMEIDDL 1238
Cdd:COG4913 813 -SLPEYLALLDRLEEDGLpEYEERFKELLNENS------IEFVADLL---SKLRRAIREIKERIDPL 869
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
853-1842 |
1.47e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.90 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 853 EKEMATMKEEFQKTKDELAKSEAKRKELeekmvsllkeKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTER 932
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEI----------KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 933 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVekekhatENKVKNlteEMAglDETIAKLTKEKKALQEAHQQ 1012
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAEL-------TNKIKA---EIS--DDKLNDYEKKFNDSKSLINE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1013 TLDDLQAEEDKVNTLTkakiKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERL--KKK 1090
Cdd:TIGR01612 902 INKSIEEEYQNINTLK----KVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLidKIN 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1091 EFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASraKAEKQRSDLSRELEE------------------ 1152
Cdd:TIGR01612 978 ELDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFD--EKEKATNDIEQKIEDanknipnieiaihtsiyn 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1153 ISERLEEAGGATSAQIEMNKKREAE-----FQKMRRDLEEATLQHEATAATLR-----KKHADSVAELGEQIDN----LQ 1218
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEILEEAEinitnFNEIKEKLKHYNFDDFGKEENIKyadeiNKIKDDIKNLDQKIDHhikaLE 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1219 RVKQKLEKEKSEMKMEIDDLaSNVETVSKAKGNLEKMCRTLEDQVSELKSKE---EEQQRLINDLTtqrgrlQTESGEFS 1295
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTKIDKKKniyDEIKKLLNEIA------EIEKDKTS 1208
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1296 rqLDEKEALvsQLSRGK---QAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQrALSKAN 1372
Cdd:TIGR01612 1209 --LEEVKGI--NLSYGKnlgKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEME-TFNISH 1283
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1373 SEvaqwRTKYETDAIQRTEELEEAKKKLAQRLQAaeehveavNAKCASLEKTKQRLQNEVedlmLDVERTNAACAALDKK 1452
Cdd:TIGR01612 1284 DD----DKDHHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNE 1347
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1453 QRNFDKILaewkqkyeethaeleasqkearslgtELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIaeggkrihe 1532
Cdd:TIGR01612 1348 IANIYNIL--------------------------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI--------- 1392
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1533 lEKIKKQVEQEKCElqaalEEAEASLEHEE--GKILRIQLELNQVKSE---IDR--KIAEKDEEIDQLKRNHIRVVESmQ 1605
Cdd:TIGR01612 1393 -KKIKDDINLEECK-----SKIESTLDDKDidECIKKIKELKNHILSEesnIDTyfKNADENNENVLLLFKNIEMADN-K 1465
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1606 STLDAEIRSRNDAirikKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQG---ILKDTQLHLDDALR--GQEDLKEQLAM 1680
Cdd:TIGR01612 1466 SQHILKIKKDNAT----NDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFEQYKKDVTELLNkySALAIKNKFAK 1541
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1681 VERRANLLQAEIEELRA--TLEQTERSRKIAE--QELLDASERVQLLHTQNTSLINTKKKLET------DISQIQGEMED 1750
Cdd:TIGR01612 1542 TKKDSEIIIKEIKDAHKkfILEAEKSEQKIKEikKEKFRIEDDAAKNDKSNKAAIDIQLSLENfenkflKISDIKKKIND 1621
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1751 IVQEARNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRldeaeqlalkggKKQIQKLEARVRELE 1830
Cdd:TIGR01612 1622 CLKETESIEKKISSFSIDS--QDTELKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIE 1687
|
1050
....*....|..
gi 1958661053 1831 GEVEsEQKRNVE 1842
Cdd:TIGR01612 1688 IDVD-QHKKNYE 1698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1680-1942 |
1.48e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1680 MVERranLLQAEIEELRATLEQ-------TERsRKIAEQELLDASE---RVQLLHTQntslinTKKKLETdiSQIQGEME 1749
Cdd:TIGR02168 145 KISE---IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--LERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1750 DIVQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVREL 1829
Cdd:TIGR02168 213 ERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1830 EGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHE 1909
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270
....*....|....*....|....*....|...
gi 1958661053 1910 LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1942
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
987-1869 |
1.51e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 987 EEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEED---KVNTLTKAKIKLEQQVDDLEgsleqekklrmDLERAKRKLE 1063
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnLVQTALRQQEKIERYQEDLE-----------ELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1064 GDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQarieeleeeieaerasRAKAEKQR 1143
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALE----------------KARALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1144 SDLSreLEEISERLEEAGGATSAQIEmnKKREAEfQKMRrDLEEATLQHEATAATLRK-------KHADSVA-ELGEQID 1215
Cdd:COG3096 432 PDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1216 NLQRVKQKLEkeksEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLindlTTQRGRLQTESGEFS 1295
Cdd:COG3096 506 SQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL----EAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1296 RQLdekealvSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHalqssrhdcdlLREQYEEEQESKAELQRALSK-ANSE 1374
Cdd:COG3096 578 EQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALER-----------LREQSGEALADSQEVTAAMQQlLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1375 VAQWRTKYEtdAIQRTEELEEAKKKLAQ-------RLQAAEEHVEAV------------NAKCAS--------------L 1421
Cdd:COG3096 640 REATVERDE--LAARKQALESQIERLSQpggaedpRLLALAERLGGVllseiyddvtleDAPYFSalygparhaivvpdL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1422 EKTKQRLQNeVEDLMLDV------------------ERTNAACAALDKKQRNFDKI-------LAEWKQKYEETHAELEA 1476
Cdd:COG3096 718 SAVKEQLAG-LEDCPEDLyliegdpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFpevplfgRAAREKRLEELRAERDE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1477 SQKEARSLGTELFKMKNAYEeSLDQLETLKRE---NKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEE 1553
Cdd:COG3096 797 LAEQYAKASFDVQKLQRLHQ-AFSQFVGGHLAvafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1554 -----AEASLEHEEGKILRIQlelnQVKSEIDrkIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSrNDAIRIkkkmegD 1628
Cdd:COG3096 876 lnkllPQANLLADETLADRLE----ELREELD--AAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQ-FEQLQA------D 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1629 LNEMEIQLNHAnRMAAEALrnyrnTQGILKDTQLHLDDAlrgQEDLKEQLAMVERranllqaeieeLRATLEQTERSRKI 1708
Cdd:COG3096 943 YLQAKEQQRRL-KQQIFAL-----SEVVQRRPHFSYEDA---VGLLGENSDLNEK-----------LRARLEQAEEARRE 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1709 AEQELLDASERVQLLHTQNTSLINTKK-KLETdISQIQGEMEDI-VQEARNAEEKAKkaitdaammaeELKKEQDTSAHL 1786
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQVLASLKSSRDaKQQT-LQELEQELEELgVQADAEAEERAR-----------IRRDELHEELSQ 1070
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1787 ERMKKNmeQTVKDLQLRldEAEqlalkggkkqIQKLEARVRELEGEVESEQKRNVEAVKG------LRKH---ERRV--K 1855
Cdd:COG3096 1071 NRSRRS--QLEKQLTRC--EAE----------MDSLQKRLRKAERDYKQEREQVVQAKAGwcavlrLARDndvERRLhrR 1136
|
970
....*....|....
gi 1958661053 1856 ELTYQTEEDRKNIL 1869
Cdd:COG3096 1137 ELAYLSADELRSMS 1150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1098-1343 |
1.53e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1098 QSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggaTSAQIEMNKKREAE 1177
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1178 FQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETvskakgnlekmcr 1257
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1258 tLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALA 1337
Cdd:COG4942 162 -LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*.
gi 1958661053 1338 HALQSS 1343
Cdd:COG4942 241 ERTPAA 246
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1566-1916 |
1.69e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1566 LRIQLELNQVKSEIDRKIAEKDE-------EIDQLKRNhirvvesmQSTLDAEIRSRND-------AIRIKKKME---GD 1628
Cdd:PRK04863 285 LEEALELRRELYTSRRQLAAEQYrlvemarELAELNEA--------ESDLEQDYQAASDhlnlvqtALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1629 LNEMEIQLNHANRMAAEAlrnyrntQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQaeieelratleqterSRKI 1708
Cdd:PRK04863 357 LEELEERLEEQNEVVEEA-------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ---------------TRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1709 AEQELLDASERVQLLhTQNTSLinTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1788
Cdd:PRK04863 415 QYQQAVQALERAKQL-CGLPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1789 mkKNMEQTVKDLQLRLDEAEQLAlkggkKQIQKLEARVRELEGEVESEQkrnvEAVKGLRKHERRVkELTYQTEEDrkni 1868
Cdd:PRK04863 492 --SEAWDVARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRL-GKNLDDEDE---- 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958661053 1869 lrLQDLVDKLQAKVKSYKRQAEEAEEQSNTnlskfrkLQHELEEAEER 1916
Cdd:PRK04863 556 --LEQLQEELEARLESLSESVSEARERRMA-------LRQQLEQLQAR 594
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1006-1562 |
1.85e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 53.27 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1006 LQEAHQQTLDD-LQAEEDKVNTLTKAKIKLEQQVDdlegSLEQEKKLRMDLERAKRKLegdlklaQESIMDIENEKQQLD 1084
Cdd:PRK10246 213 LTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSLN----WLTRLDELQQEASRRQQAL-------QQALAAEEKAQPQLA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1085 E-RLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAErasRAKAEKQRSDLSRELEEISERLEEAGGA 1163
Cdd:PRK10246 282 AlSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARI---RHHAAKQSAELQAQQQSLNTWLAEHDRF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1164 TSAQIEMNKKReAEFQKMRRDLEEATLQHEATAATLRKKHA----------DSVAELGEQIDNLQRVKQKLEKEKSEMKM 1233
Cdd:PRK10246 359 RQWNNELAGWR-AQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1234 EIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEE---------EQQRLINDLTTQRGRLQT--------------- 1289
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpav 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1290 ------ESGEFSRQLDEKEALVSQLS------RGK-QAFTQQI----EELKRQLEEE---VKAKNALAHALQSSRHDCD- 1348
Cdd:PRK10246 518 eayqalEPGVNQSRLDALEKEVKKLGeegaalRGQlDALTKQLqrdeSEAQSLRQEEqalTQQWQAVCASLNITLQPQDd 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1349 ---LLREQYEEEQE-----SKAELQRALSKANSEVAQWRTKYETDAIQRTEELEE----------------AKKKLAQRL 1404
Cdd:PRK10246 598 iqpWLDAQEEHERQlrllsQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqedeeaswlaTRQQEAQSW 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1405 QAAEEHVEAVNAKCASLEKTKQRL------QNEVEDLMLDVER-TNAACAALDKKQRNFDKILAEWKQKYEETHAELEAS 1477
Cdd:PRK10246 678 QQRQNELTALQNRIQQLTPLLETLpqsddlPHSEETVALDNWRqVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1478 QKEARSLGTELFKMKNAYEESLDQLETLKRENKN-----------------------------------LQQEISDLTEQ 1522
Cdd:PRK10246 758 LQASVFDDQQAFLAALLDEETLTQLEQLKQNLENqrqqaqtlvtqtaqalaqhqqhrpdgldltvtveqIQQELAQLAQQ 837
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1958661053 1523 IAEGGKRIHELEKIKKQVEQEKCELQAALEE-AEASLEHEE 1562
Cdd:PRK10246 838 LRENTTRQGEIRQQLKQDADNRQQQQALMQQiAQATQQVED 878
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1496-1694 |
2.27e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1496 EESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKikkqveqEKCELQAALEEAEASLEHEEGKILRIQLELNQv 1575
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1576 KSEIDRKIAEKDEEIDQLKrnhiRVVESMQSTLDaEIRSRNDaiRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQG 1655
Cdd:COG2433 460 EIRKDREISRLDREIERLE----RELEEERERIE-ELKRKLE--RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190
....*....|....*....|....*....|....*....
gi 1958661053 1656 ILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEE 1694
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSE 571
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
958-1540 |
2.54e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 958 KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----------ETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTL 1027
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDyleeklkssnLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1028 TKAKIKLEQQVDDLEGSLEQEKKLRMDLerakRKLEGDLklaqESIMDIENEKQQLDERLKKKEfemSNLQSKIEDEQAI 1107
Cdd:PRK01156 231 MDDYNNLKSALNELSSLEDMKNRYESEI----KTAESDL----SMELEKNNYYKELEERHMKII---NDPVYKNRNYIND 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1108 GIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSrELEEISERLEEaggaTSAQIEMNKKREAEFQKMRRDLEE 1187
Cdd:PRK01156 300 YFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYN-DYIKKKSRYDD----LNNQILELEGYEMDYNSYLKSIES 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1188 ATLQHEataaTLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELK 1267
Cdd:PRK01156 375 LKKKIE----EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1268 SK-----------EEEQQRLINDLTTQRGRLQTEsgefsrqLDEKEALVSQLSRGKQaftQQIEELKRQLEEEVKAKNAL 1336
Cdd:PRK01156 451 GQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEK-------IREIEIEVKDIDEKIV---DLKKRKEYLESEEINKSINE 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1337 AHALQSSRHDCDLLREQYEEEQESKAELQRALSKANS-EVAQWRTKYET-------------DAIQ-RTEELEEAKKKLA 1401
Cdd:PRK01156 521 YNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSwlnalavislidiETNRsRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1402 QRLQAAEEHVEAVNakcASLEKTKQRLQNEVEDL---MLDVERTNAACAALDKKQRNFDKILAEwKQKYEETHAELEAsq 1478
Cdd:PRK01156 601 SRLQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITS-- 674
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1479 kEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQV 1540
Cdd:PRK01156 675 -RINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1093-1335 |
3.12e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1093 EMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEaggatsaqiemnk 1172
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1173 kREAEFQKMRRDLEEATLQHEATAATLrkkHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNL 1252
Cdd:COG3883 84 -RREELGERARALYRSGGSVSYLDVLL---GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1253 EKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKA 1332
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
...
gi 1958661053 1333 KNA 1335
Cdd:COG3883 240 AAA 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
856-1720 |
3.21e-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: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 856 MATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLAdaeercdqLIKTKIQLEAKIK-------E 928
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKIEryqedleE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 929 VTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhatenkvknlteemaGLDE--TIA-KLTKEKKA 1005
Cdd:COG3096 359 LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ-----------------ALDVqqTRAiQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1006 LQEAHQQT-LDDLqAEEDKVNTLTKAKIKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKLAQEsiMDIENEKQQLD 1084
Cdd:COG3096 422 LEKARALCgLPDL-TPENAEDYLAAFRAKEQQATEEV---LELEQKLSVA-DAARRQFEKAYELVCK--IAGEVERSQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1085 ERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQarieeleeeieaeraSRAKAEKQRSDLSR----------ELEEIS 1154
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQLAELEQRLR---------------QQQNAERLLEEFCQrigqqldaaeELEELL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1155 ERLEeaggatsAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKK-----HADSVAE-----LGEQIDNLQRV---- 1220
Cdd:COG3096 560 AELE-------AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALErlreqSGEALADSQEVtaam 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1221 KQKLEKEKsEMKMEIDDLA-------SNVETVSKAKGNLEKMCRTLEDQVS-ELKSKEEE------------------QQ 1274
Cdd:COG3096 633 QQLLERER-EATVERDELAarkqaleSQIERLSQPGGAEDPRLLALAERLGgVLLSEIYDdvtledapyfsalygparHA 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1275 RLINDLTTQRGRLQTES----------------GEFSRQLDEKE-ALVSQLSR--------------GKQAFTQQIEELK 1323
Cdd:COG3096 712 IVVPDLSAVKEQLAGLEdcpedlyliegdpdsfDDSVFDAEELEdAVVVKLSDrqwrysrfpevplfGRAAREKRLEELR 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1324 RQLEEEVK--AKNA--------LAHALQS--SRHDCDLLREQYEEE----QESKAELQRALSKANSEVAQWRTKY----- 1382
Cdd:COG3096 792 AERDELAEqyAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLdqlke 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1383 ----------------ETDAIQRTEELEEAkkklAQRLQAAEEHVEAVNAKCASLEKTKQRLQN---EVEDLMLDVERTN 1443
Cdd:COG3096 872 qlqllnkllpqanllaDETLADRLEELREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAK 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1444 AACAALdkKQRNFdkILAEWKQK-----YEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISD 1518
Cdd:COG3096 948 EQQRRL--KQQIF--ALSEVVQRrphfsYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAS 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1519 LT-------EQIAEGGKRIHELE-----KIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLE---LNQVKSEIDRKI 1583
Cdd:COG3096 1024 LKssrdakqQTLQELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEmdsLQKRLRKAERDY 1103
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1584 AEKDEEIDQLKRNHIRVVEsmqstldaeiRSRNDAirikkkMEGDLNEMEIQLNHANR---MAAEALRNYRNTQGILKdt 1660
Cdd:COG3096 1104 KQEREQVVQAKAGWCAVLR----------LARDND------VERRLHRRELAYLSADElrsMSDKALGALRLAVADNE-- 1165
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1661 qlHLDDALRGQEDLKEQLAMV-----------ER-----------RANLLQAEIEELRATLEQTERsrkiaEQELLDASE 1718
Cdd:COG3096 1166 --HLRDALRLSEDPRRPERKVqfyiavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSR-----EQKLAISSE 1238
|
..
gi 1958661053 1719 RV 1720
Cdd:COG3096 1239 SV 1240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1765 |
4.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1476 ASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAE 1555
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1556 ASLEheegkilriqlelnqvkseidrkiaekdeeidQLKRNHIRVVESMQstldaeirsrndairikkkMEGDLNEMEIQ 1635
Cdd:COG4942 97 AELE--------------------------------AQKEELAELLRALY-------------------RLGRQPPLALL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1636 LNHANrmAAEALRNYRNTQGILKDTQLHLddalrgqEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLD 1715
Cdd:COG4942 126 LSPED--FLDAVRRLQYLKYLAPARREQA-------EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1716 ASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKA 1765
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1078-1570 |
5.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1078 NEKQQLDERLKKKEFEMSNLQSKIEDEQaigiQLQKKIKELQARIEE--LEEEIEAERASRAKAEKQRSDLSRELEEISE 1155
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1156 RLEEAggatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1235
Cdd:COG4717 147 RLEEL-----------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1236 DDLASNVETVSKAKGNLEKmcrtlEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEAL----------V 1305
Cdd:COG4717 216 EEAQEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1306 SQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTkyetd 1385
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL----- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1386 aiqrtEELEEAKKKLAQRLQAAEEhvEAVNAKCASLEKtkqrlqnevedlmldvertnaacaaldkkqrnfdkiLAEWKQ 1465
Cdd:COG4717 366 -----EELEQEIAALLAEAGVEDE--EELRAALEQAEE------------------------------------YQELKE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1466 KYEETHAELEASQKEARSLGTELfkmknayeesldQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKC 1545
Cdd:COG4717 403 ELEELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
490 500
....*....|....*....|....*..
gi 1958661053 1546 --ELQAALEEAEASLEHEEGKILRIQL 1570
Cdd:COG4717 471 laELLQELEELKAELRELAEEWAALKL 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1045-1555 |
5.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1045 LEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQaigiqLQKKIKELQARIEE 1124
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1125 LEeeieaerasraKAEKQRSDLSRELEEISERLEEAggatsaqiemnkkreaefqkmRRDLEEATLQHEATAATLRKKHA 1204
Cdd:COG4717 151 LE-----------ERLEELRELEEELEELEAELAEL---------------------QEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1205 DSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKgNLEKMCRTLEdQVSELKSKEEEQQRLINDLTTQR 1284
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLL-IAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1285 GRLQTESGEFSrqldekeALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAEL 1364
Cdd:COG4717 277 GVLFLVLGLLA-------LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1365 QRALSKANSEVAQWRTKYETDAIQrtEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNA 1444
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIA--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1445 acAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTElfkmkNAYEESLDQLETLKRENKNLQQEIS--DLTEQ 1522
Cdd:COG4717 428 --EELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAalKLALE 500
|
490 500 510
....*....|....*....|....*....|...
gi 1958661053 1523 IaeggkriheLEKIKKQVEQEKceLQAALEEAE 1555
Cdd:COG4717 501 L---------LEEAREEYREER--LPPVLERAS 522
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1358-1541 |
6.26e-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: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1358 QESKAELQRALSKANSEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLM 1436
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1437 ldverTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLD-QLETLKRENKNLQQE 1515
Cdd:COG3206 261 -----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQAREASLQAQ 335
|
170 180
....*....|....*....|....*.
gi 1958661053 1516 ISDLTEQIAEGGKRIHELEKIKKQVE 1541
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVE 361
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1447-1624 |
6.57e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1447 AALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNL--QQEISDLTEQIA 1524
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1525 EGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGkilriqlELNQVKSEIDRKIAEKDEEIDQLKRNhirvVESM 1604
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEAE----REEL 168
|
170 180
....*....|....*....|
gi 1958661053 1605 QSTLDAEIRSRNDAIRIKKK 1624
Cdd:COG1579 169 AAKIPPELLALYERIRKRKN 188
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
846-1119 |
7.36e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 846 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLiktkiqleak 925
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL---------- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 926 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlteeMAGLDETIAKLTKEKKA 1005
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1006 LQEAHQQTLDDLQAeedKVNTLTKAKIKLEQQVDDLEgslEQEKKLRMDLERA---KRKLEGDLKLAQESIMDIENEKQQ 1082
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKVAN 808
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1958661053 1083 LDERLKKKEFEMSNLQSKI--EDEQAIGIQLQKK--IKELQ 1119
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIqrQEQESVRLKLQHTldVKELQ 849
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
898-1106 |
8.65e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 898 VQAEAEgLADAEERCDQLIKTKIQLEAKIKEVTERAEdeeeinaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHA 977
Cdd:COG3883 12 AFADPQ-IQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 978 TENKVKNLTEEM--AGLDETIAKLTKEKKALQEA--HQQTLDDL-QAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLR 1052
Cdd:COG3883 84 RREELGERARALyrSGGSVSYLDVLLGSESFSDFldRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1053 MDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQA 1106
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1351-1712 |
9.06e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 50.53 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1351 REQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQA-AEEHVEAVNAKCASLEKTKQRLQ 1429
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1430 NEVEDLMLDVERTNAACAALDKKQRNFDKILAE-WKQKYEETHAELEASQKE-ARSLGTELFKMKNAYEESLDQLETLKR 1507
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAEISREKATDSALQKAEaLAEKLKEVINLAKQSEEEaAPPLLDAAPETPPKLPEHLDNVEEKVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1508 ENKNLQQEISDLTEQIAEG-GKRIHELEKIKKQVEQEKCELQAAL-EEAEASLEHEEGKILRIQLELN----QVKSEIDR 1581
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASErIVFQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAelkkREEKHIER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1582 KIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIR--IKKKMEgdlNEMEIQLNHANRMAAEALRNYRNTQGILKD 1659
Cdd:pfam09731 317 ALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREReeIRESYE---EKLRTELERQAEAHEEHLKDVLVEQEIELQ 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1660 tqlhlddaLRGQEDLKEQlamVERRANLLQAEIEELRATLEQTER---SRKIAEQE 1712
Cdd:pfam09731 394 --------REFLQDIKEK---VEEERAGRLLKLNELLANLKGLEKatsSHSEVEDE 438
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1460-1941 |
9.70e-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: 50.88 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1460 LAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQ 1539
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1540 VEQEKCELQAALEEAEASLEHeegkiLRIQLElnQVKSEIDRKIAEKDEEIDQLKRNHIRVV---ESMQSTLDAEIRSRN 1616
Cdd:pfam05483 181 TRQVYMDLNNNIEKMILAFEE-----LRVQAE--NARLEMHFKLKEDHEKIQHLEEEYKKEIndkEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1617 DAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQ----GILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEI 1692
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1693 EELRATLEQTERSRKIAEQELLDASERVQ-LLHTQNTSLINTKKKLETDISQIQ---GEMEDIVQEARNAE---EKAKKA 1765
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEeLLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEvelEELKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1766 ITDAAMMAEELKKEQDTSahlERMKKNMEQTVKDLQLRLDEAEQLALK--GGKKQIQKLEARVRELEGEVESEQKRNVE- 1842
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIA---EELKGKEQELIFLLQAREKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1843 --------------------AVKGLRKHERRVKELTYQTEEDRKNILRLQD----LVDKLQAKVKSYKRQAEEAEEQSNT 1898
Cdd:pfam05483 491 tahcdklllenkeltqeasdMTLELKKHQEDIINCKKQEERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDK 570
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1958661053 1899 NLSKFRKLQHELEEAEERADIAESQVNKLRvKSREVHTKVISE 1941
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLK-KQIENKNKNIEE 612
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1684-1942 |
1.03e-05 |
|
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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1684 RANLLQAE--IEELRATLEQTERSRKIAE--QELLDASERVQ--LLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARN 1757
Cdd:TIGR02168 185 RENLDRLEdiLNELERQLKSLERQAEKAEryKELKAELRELElaLLVLRLEELREELEELQEELKEAEEELEELTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1758 AEEKAkkaitdaammaEELKKEqdtsahlermKKNMEQTVKDLQLRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQ 1837
Cdd:TIGR02168 265 LEEKL-----------EELRLE----------VSELEEEIEELQKELYALANE-ISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1838 KRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHE-------- 1909
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnnei 402
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958661053 1910 ------LEEAEERADIAESQVNKLRVKSREVHTKVISEE 1942
Cdd:TIGR02168 403 erlearLERLEDRRERLQQEIEELLKKLEEAELKELQAE 441
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1265-1843 |
1.11e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1265 ELKSKEEEQQRLINDLTTQRGRLQTESGEFSRqldEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSsr 1344
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKLRETEEVEFSL---KAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQ-- 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1345 hdcdllreQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAvnakcaSLEKT 1424
Cdd:COG5022 886 --------ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGP------SIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1425 KQRLQNEVedlmldvertNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLgTELFKMKNAYEESLDQLET 1504
Cdd:COG5022 952 KLPELNKL----------HEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL-AELSKQYGALQESTKQLKE 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1505 LKRENKNLQQEISDLTEQIAEGgKRIHELEKIKKQVEQEKCELQAALEEAeaSLEHEEGKILRIQLELNQVKSEIDRKIA 1584
Cdd:COG5022 1021 LPVEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNQLQARYKAL--KLRRENSLLDDKQLYQLESTENLLKTIN 1097
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1585 EKDEEIdqLKRNHIRVVESMQSTLDAEIRSRNdAIRIKKKMEGDLN--EMEIQLNHANRMAAEALRNYRNTQgilkdtQL 1662
Cdd:COG5022 1098 VKDLEV--TNRNLVKPANVLQFIVAQMIKLNL-LQEISKFLSQLVNtlEPVFQKLSVLQLELDGLFWEANLE------AL 1168
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1663 HLDDALRGQ-EDLKEQLAMVERRANLLQAEIEELRA---TLEQTERSRKIAEQELLDASERVQLLHTQNTSL-------- 1730
Cdd:COG5022 1169 PSPPPFAALsEKRLYQSALYDEKSKLSSSEVNDLKNeliALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLkgfnnlnk 1248
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1731 ------INTKKKLETDISQIQGEMEDIVQEA------------RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK- 1791
Cdd:COG5022 1249 kfdtpaSMSNEKLLSLLNSIDNLLSSYKLEEevlpatinsllqYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCr 1328
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1792 ------------NMEQTVKDLQLRLDEAEQLALKGGKK------QIQKLEAR--VRELEGEVESEQKRNVEA 1843
Cdd:COG5022 1329 efeisdvdeeleELIQAVKVLQLLKDDLNKLDELLDACyslnpaEIQNLKSRydPADKENNLPKEILKKIEA 1400
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1355-1484 |
1.36e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1355 EEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqaaeehVEAVNAKCASLEKTKQRLQNEVED 1434
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1435 lmldvertnaacaaLDKKQRNFDKILAEWKQKYEETHAELEA----SQKEARSL 1484
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEI 158
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1008-1169 |
1.39e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1008 EAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQekklrmdLERAKRKLEGDLKLAQESIMDIENEKQQLDERL 1087
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1088 KKKEF---------EMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1158
Cdd:COG1579 76 KKYEEqlgnvrnnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|.
gi 1958661053 1159 EAGGATSAQIE 1169
Cdd:COG1579 156 AELEELEAERE 166
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1018-1248 |
1.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1018 QAEEDKVNTLTKAKIKLEQQVDDLEGSLEQ-EKKlrmdLERAKRK-----LEGDLKLAQESIMDIENEKQQLDERLKKKE 1091
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1092 FEMSNLQSKIEDEQAIG---------IQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEagg 1162
Cdd:COG3206 240 ARLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA--- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1163 ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRkkhadsvaELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNV 1242
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
....*.
gi 1958661053 1243 ETVSKA 1248
Cdd:COG3206 389 RVIDPA 394
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1488-1890 |
1.55e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.85 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1488 LFKMKNAYEEsLDQLETLKRE--NKNLQQEISDLtEQIAEGGKRIHELEKIKKQ----VEQEKCELQAALEEAEASLEhe 1561
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1562 EGKILRIQLELNQVKS---EIDRKIAEKDEEIDQLK------RNHIRVVESMQSTLDAEIRSRN----DAIrikKKMEGD 1628
Cdd:pfam06160 78 KYRFKKAKKALDEIEElldDIEEDIKQILEELDELLeseeknREEVEELKDKYRELRKTLLANRfsygPAI---DELEKQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1629 LNEMEIQLNHANRMAAEAlrNYRNTQGILKDTQLHLDDAlrgQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKI 1708
Cdd:pfam06160 155 LAEIEEEFSQFEELTESG--DYLEAREVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1709 AEQelLDASERVQLLHTQNTSLINTKKKLETD-----ISQIQGEMEDIvQEARNAEEKAKKaitdaammaeELKKEQDT- 1782
Cdd:pfam06160 230 LEH--LNVDKEIQQLEEQLEENLALLENLELDeaeeaLEEIEERIDQL-YDLLEKEVDAKK----------YVEKNLPEi 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1783 SAHLERMKKNMEQTVKDLQL-----RLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNV-------EAVKGLRKH 1850
Cdd:pfam06160 297 EDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSelqeeleEILEQLEEI 376
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1958661053 1851 ERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAE 1890
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
867-1095 |
1.76e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 867 KDELAKSEAKRKELEEkMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-------QLEAKIKEVTERAEDEEEI 939
Cdd:PLN02939 142 KNILLLNQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 940 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQtLDDLQA 1019
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1020 EE--DKVNTLT-----------KAKIKLEQ------QVDDLEGSLEQE-----------------KKLRMDLERAKRKLE 1063
Cdd:PLN02939 296 DCwwEKVENLQdlldratnqveKAALVLDQnqdlrdKVDKLEASLKEAnvskfssykvellqqklKLLEERLQASDHEIH 375
|
250 260 270
....*....|....*....|....*....|..
gi 1958661053 1064 GDLKLAQESIMDIENEKQQLDERLKKKEFEMS 1095
Cdd:PLN02939 376 SYIQLYQESIKEFQDTLSKLKEESKKRSLEHP 407
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
940-1543 |
2.95e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 940 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQA 1019
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1020 E---EDKVNTLTKAKIKLEQQVDDLEGSLEQE-KKLRMDLERAKRKLEgdlklaqesimDIENEKQQLDERLKKKEFEMS 1095
Cdd:pfam05557 81 KkkyLEALNKKLNEKESQLADAREVISCLKNElSELRRQIQRAELELQ-----------STNSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1096 NLQSKIEDEQAIGIQL---QKKIKELQARIEELEEEIEAERASRAKAEkQRSDLSRELeeisERLEEAGGATSAQIEMNK 1172
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPELEKEL----ERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1173 KREAEFQKMRRDLEEatlqheataatlRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI---DDLASNVETVSKAK 1249
Cdd:pfam05557 225 LLKEEVEDLKRKLER------------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQRE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1250 GNLEKMCRTLEdqvSELKSKEEEQQRLINDLTTQRGRLQtesgEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLE-- 1327
Cdd:pfam05557 293 IVLKEENSSLT---SSARQLEKARRELEQELAQYLKKIE----DLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILEsy 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1328 -EEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRT-KYETDAIQRTEELEEAkkklaqrlQ 1405
Cdd:pfam05557 366 dKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTlERELQALRQQESLADP--------S 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1406 AAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLG 1485
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLK 517
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1486 TELFKMknayEESLDQLETLKRENKNLQ-QEISDLTEQIAEGGKRIHELEKIKKQVEQE 1543
Cdd:pfam05557 518 RLLKKL----EDDLEQVLRLPETTSTMNfKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
861-1091 |
3.04e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 49.00 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 861 EEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEErCDQLIKTKIQLEAKIKEVTERAEDeeeIN 940
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDE-IFALINKEANRDARAIAYTQNLKG---IK 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 941 AELTAKKRKLEDECSELKKDIDDLE----LTLAKVEKEKHATENKVKNLteemaGLD-ETIAKLTKEKKALQEAHQQTLD 1015
Cdd:pfam18971 686 RELSDKLEKISKDLKDFSKSFDEFKngknKDFSKAEETLKALKGSVKDL-----GINpEWISKVENLNAALNEFKNGKNK 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1016 DL----QAEEDKVNTLTKAKI--KLEQQVDDLEGSLEQEKKLrmdlerakrkleGDLKLAQESIMDIEN-EKQQLDERLK 1088
Cdd:pfam18971 761 DFskvtQAKSDLENSVKDVIInqKVTDKVDNLNQAVSVAKAM------------GDFSRVEQVLADLKNfSKEQLAQQAQ 828
|
...
gi 1958661053 1089 KKE 1091
Cdd:pfam18971 829 KNE 831
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1672-1938 |
3.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1672 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKiaeqELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDI 1751
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1752 VQEARNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQtvkdlqlrldeaeqlalkgGKKQIQKLEARVRELEG 1831
Cdd:PRK03918 272 KKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD-------------------ELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1832 EVEseqkrnvEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQaKVKSYKRQAEEAEEQSnTNLSKfRKLQHELE 1911
Cdd:PRK03918 325 GIE-------ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL-TGLTP-EKLEKELE 394
|
250 260
....*....|....*....|....*..
gi 1958661053 1912 EAEERADIAESQVNKLRVKSREVHTKV 1938
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEI 421
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
932-1078 |
3.08e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 48.13 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 932 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETI-AKLTKEKKALQEAH 1010
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKE 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1011 qqtLDDLQAEEDKVNT----LTKAKI-KLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIEN 1078
Cdd:cd22656 181 ---IKDLQKELEKLNEeyaaKLKAKIdELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
847-1084 |
3.12e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 847 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKE---------LEEKMVSLLKEKNDLQLQ-VQAEAEgLADAEERCDQLi 916
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQlAEARAE-LAEAEARLAAL- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 917 ktKIQLEAKIKEVTERAEDEEEinaeltakkrkledecSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLde 994
Cdd:COG3206 246 --RAQLGSGPDALPELLQSPVI----------------QQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL-- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 995 tiakltkeKKALQEAHQQTLDDLQAEedkVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRklegDLKLAQESIM 1074
Cdd:COG3206 304 --------RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYE 368
|
250
....*....|
gi 1958661053 1075 DIENEKQQLD 1084
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1109-1431 |
3.38e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1109 IQLQKKIKELQARIEELEEEIEaerasRAKAEKQrsDLSRELEEiSERLEEAGGATSAQIEMNKKREAEFQK--MRRDLE 1186
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-----RLRQEKE--EKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERmaMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1187 EATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIddlasnvETVSKAKGNLEKMCRTLEDQVSEL 1266
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQEL-------EAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1267 ----KSKEEEQQRLINDLTTQRGRlqtesgEFSRQLDEKEALVSQLSRgkqaFTQQIEELKRQLEEEVKAKNALAHALQS 1342
Cdd:pfam17380 423 eqirAEQEEARQREVRRLEEERAR------EMERVRLEEQERQQQVER----LRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1343 SR----HDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKC 1418
Cdd:pfam17380 493 RRkileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAME 572
|
330
....*....|...
gi 1958661053 1419 ASLEKTKQRLQNE 1431
Cdd:pfam17380 573 REREMMRQIVESE 585
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1309-1585 |
4.09e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1309 SRGKQAFTQQIEELKRQLEEEVKAknalahalqssrhdcdllreqyeeeqesKAELQRALSKANSEVAQWRTKYETDAIQ 1388
Cdd:pfam00038 46 SRLYSLYEKEIEDLRRQLDTLTVE----------------------------RARLQLELDNLRLAAEDFRQKYEDELNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1389 RTeELEEAKKKLAQRLQAA-------EEHVEAVNAKCASLEKTKQR----LQNEVEDLMLDVERTNAACAALdkkqrnfD 1457
Cdd:pfam00038 98 RT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELAFLKKNHEEevreLQAQVSDTQVNVEMDAARKLDL-------T 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1458 KILAEWKQKYEEtHAELeaSQKEARslgtELFKMKnaYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIK 1537
Cdd:pfam00038 170 SALAEIRAQYEE-IAAK--NREEAE----EWYQSK--LEELQQAAARNGDALRSAKEEITELRRTIQS---LEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1538 KQveqeKCELQAALEEAEASLEHE----EGKILRIQLELNQVKSEIDRKIAE 1585
Cdd:pfam00038 238 KQ----KASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1258-1416 |
4.52e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1258 TLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAK--NA 1335
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1336 LAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVN 1415
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 1958661053 1416 A 1416
Cdd:COG1579 174 P 174
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
859-1106 |
4.87e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 48.31 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 859 MKEEFQKTKDELAKSEAKRKELEEkmvslLKEKNDLqLQVQAEAEGLADAEERCDQLiktKIQLEAKIKEVTERAEDEEE 938
Cdd:PLN03229 509 LMEKIEKLKDEFNKRLSRAPNYLS-----LKYKLDM-LNEFSRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEK 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 939 INAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDETIAKltkeKKALQEAHQQTLDDLQ 1018
Cdd:PLN03229 580 MEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT----KKNKDTAEQTPPPNLQ 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1019 AEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAQEsimdIENEKQQLDERLKKKeFEMSNLQ 1098
Cdd:PLN03229 649 EKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSELK 718
|
....*...
gi 1958661053 1099 SKIEDEQA 1106
Cdd:PLN03229 719 EKFEELEA 726
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
850-1119 |
5.82e-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: 47.97 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 930 TERAE-------DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAK---L 999
Cdd:pfam07888 156 KERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1000 TKEKKALQE---AHQQT-------LDDLQAEEDKVNT-LTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKL 1068
Cdd:pfam07888 236 LEELRSLQErlnASERKveglgeeLSSMAAQRDRTQAeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1069 AQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIG-IQLQKKIKELQ 1119
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNrVQLSESRRELQ 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-1933 |
6.14e-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: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1740 DISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQI 1819
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1820 QKLEARVRELEGEVESEQKRNVEAV----KGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ 1895
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958661053 1896 SNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSRE 1933
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1259-1482 |
6.15e-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: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1259 LEDQVSELKSKEEEQQRLINDLTTQRG--RLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNAL 1336
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1337 AHALQSSRhdcdlLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNA 1416
Cdd:COG3206 260 LQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1417 KcasLEKTKQRLQ--NEVEDLMLDVERTnaacaaLDKKQRNFDKILaewkQKYEETHAELEASQKEAR 1482
Cdd:COG3206 335 Q---LAQLEARLAelPELEAELRRLERE------VEVARELYESLL----QRLEEARLAEALTVGNVR 389
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
863-1202 |
6.67e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 863 FQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKI-----------QLEAKIKEVTE 931
Cdd:PRK04778 100 FRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLanrfsfgpaldELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 932 RAEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----LTEEMAGLDETiaKLTKE 1002
Cdd:PRK04778 180 EFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHLDHL--DIEKE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1003 KKALQEAHQQTLDDLQAEE-DKVNTLTKakiKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQ 1081
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDlDEAEEKNE---EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1082 QLDERlkkkeFEMSnlqskiEDEQAIGIQLQKKIKELQARIEELEEEIeaerasrAKAEKQRSDLSRELEEISERLEEAg 1161
Cdd:PRK04778 335 RVKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYSELQEELEEILKQLEEI- 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1958661053 1162 gatsaqiemnKKREAEFQKMRRDLEEATLQHEATAATLRKK 1202
Cdd:PRK04778 396 ----------EKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1353-1557 |
7.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1353 QYEEEQESKAELQRALSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEV 1432
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1433 EDLMLDVERTNAA-------------------CAALDKKQRNFDKILAEwkqkYEETHAELEASQKEARSLGTELFKMKN 1493
Cdd:COG3883 89 GERARALYRSGGSvsyldvllgsesfsdfldrLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1494 AYEESLDQLETLKRENknlQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEAS 1557
Cdd:COG3883 165 ELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
941-1167 |
7.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 941 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAE 1020
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1021 EDKVNTLTkakIKLE--------QQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKkkef 1092
Cdd:COG3883 99 GGSVSYLD---VLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA---- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1093 emsNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQ 1167
Cdd:COG3883 172 ---ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1684-1942 |
7.85e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1684 RANLLQAE--IEELRATLEQTERSRKIAEQelldaservqllhtqntslintKKKLETDISQIQGEMedIVQEARNAEEK 1761
Cdd:COG1196 185 EENLERLEdiLGELERQLEPLERQAEKAER----------------------YRELKEELKELEAEL--LLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1762 AKKAitdaammAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGEVESEQKRNV 1841
Cdd:COG1196 241 LEEL-------EAELEELEAELEELEAELAELEAELEELRLELEELEL--------ELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1842 EAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAE 1921
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
250 260
....*....|....*....|.
gi 1958661053 1922 SQVNKLRVKSREVHTKVISEE 1942
Cdd:COG1196 386 EELLEALRAAAELAAQLEELE 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1639-1892 |
7.96e-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: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1639 ANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELldase 1718
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1719 rvqllhtqntslintkKKLETDISQIQGEMEDIVQEA-RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTV 1797
Cdd:COG4942 93 ----------------AELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1798 KDLQlRLDEAEQlALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKherRVKELTYQTEEDRKNILRLQDLVDK 1877
Cdd:COG4942 157 ADLA-ELAALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*
gi 1958661053 1878 LQAKVKSYKRQAEEA 1892
Cdd:COG4942 232 LEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
851-1009 |
8.68e-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: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLL----KEKNDLQLQVQAEAEGLADA--------------EERC 912
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyRLGRQPPLALLLSPEDFLDAvrrlqylkylaparREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 913 DQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEdecselkKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 992
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
170
....*....|....*..
gi 1958661053 993 DETIAKLTKEKKALQEA 1009
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1458-1942 |
9.14e-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: 47.73 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1458 KILAEWKQKYEETHAELEASQKEARSLGtelfKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIK 1537
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESSR----EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1538 KQVEQEKCELQAALEEAEASLEHEEG--------KILRIQLE----------LNQVKSEIDRKIAEKDEEIDQ-----LK 1594
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQrtvrekerELVDCQREleklnkerrlLNQEKTELLVEQGRLQLQADRhqehiRA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1595 RNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDL 1674
Cdd:TIGR00606 366 RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1675 KEQLAMVERRANLLQAEIEELRAT----LEQTERSRKiAEQELLDASE---------RVQLLHTQNTSLINTKKKLETDI 1741
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSsdriLELDQELRK-AERELSKAEKnsltetlkkEVKSLQNEKADLDRKLRKLDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1742 SQIQGEMEDIVQEARNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAE 1808
Cdd:TIGR00606 525 EQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1809 QLA------LKGGKKQIQKLEARVRELEG--EVESEQKRNVEAVKGLRK-----------HERRVKELTYQT-------E 1862
Cdd:TIGR00606 605 QNKnhinneLESKEEQLSSYEDKLFDVCGsqDEESDLERLKEEIEKSSKqramlagatavYSQFITQLTDENqsccpvcQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1863 EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1942
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1260-1637 |
9.24e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.26 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1260 EDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHA 1339
Cdd:COG5185 155 EVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1340 LQSsrhdcdllREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCA 1419
Cdd:COG5185 235 LKG--------FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1420 SLEKTKQ--------RLQNEVEDLMLDVER-TNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEArslgtELFK 1490
Cdd:COG5185 307 IKKATESleeqlaaaEAEQELEESKRETETgIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE-----ELDS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1491 MKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGgkriheLEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQL 1570
Cdd:COG5185 382 FK-------DTIESTKESLDEIPQNQRGYAQEILAT------LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1571 ELNQVKSEIDrkiAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIR-IKKKMEGDLNEMEIQLN 1637
Cdd:COG5185 449 ELNKVMREAD---EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVStLKATLEKLRAKLERQLE 513
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1234-1377 |
1.10e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1234 EIDDLASNVETVSKAKGNLEKMCRTLEDQVS----ELKSKEEEQQRL---INDLTTQRGRLQTESGEFSRQLDEKEALVS 1306
Cdd:PRK09039 54 ALDRLNSQIAELADLLSLERQGNQDLQDSVAnlraSLSAAEAERSRLqalLAELAGAGAAAEGRAGELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1307 QLSRGKQAFTQQIEELKRQLeeevkakNALAHALQSSRhdcdllreqyEEEQESKAELQRALSKANSEVAQ 1377
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQL-------AALEAALDASE----------KRDRESQAKIADLGRRLNVALAQ 187
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1473-1928 |
1.17e-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: 47.04 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1473 ELEASQKEARSLGTELFKMKNAYEESLDQLEtlkRENKNLQQEISDLTEQIAEggkrihELEKIKKQVEQEKCELQAALE 1552
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKYLEALNKKL---NEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1553 EAEASLEHEEGKILRIQlELNQVKSEIDRKIAEKDEEIDQLKrnhirvvesmqsTLDAEIRSRNDAIRIKKKMEGDL--- 1629
Cdd:pfam05557 133 ELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAEAEQRIK------------ELEFEIQSQEQDSEIVKNSKSELari 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1630 NEMEIQLNHAnRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIA 1709
Cdd:pfam05557 200 PELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1710 EqellDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKakkaITDAAMMAEELK------------ 1777
Cdd:pfam05557 279 E----DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvll 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1778 --KEQD-TSAHLERMKK--NMEQTVKDLQLRLDEAEQLALKGgKKQIQKLEARVRELEGEVES--EQKRNVEAVKGLRKH 1850
Cdd:pfam05557 351 ltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMTQKM-QAHNEEMEAQLSVAEEELGGykQQAQTLERELQALRQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1851 ERRVKELTYQTEED---RKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKL 1927
Cdd:pfam05557 430 QESLADPSYSKEEVdslRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKL 509
|
.
gi 1958661053 1928 R 1928
Cdd:pfam05557 510 Q 510
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
850-982 |
1.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELE---EKMVSLLKEKNDLQLQVQAEAEgLADAEERCDQLIKTKIQLEAKI 926
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 927 KEVTERAEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 982
Cdd:COG1579 113 LELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
968-1410 |
1.24e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.99 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 968 LAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEahqqTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQ 1047
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQE----RLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1048 EKKLRMDLERAKRKLE---GDLKLAQESIMDIENEKQQL----------DERLKKKEFEMSNLQSKIEDEQaigiQLQKK 1114
Cdd:pfam05622 78 LETARDDYRIKCEELEkevLELQHRNEELTSLAEEAQALkdemdilresSDKVKKLEATVETYKKKLEDLG----DLRRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1115 IKELQARIEELEEEieaerasrakaekqrsdlSRELEEISERleeaGGATSAQIEMNKKREAEFQKMrrdLEEATLQHEA 1194
Cdd:pfam05622 154 VKLLEERNAEYMQR------------------TLQLEEELKK----ANALRGQLETYKRQVQELHGK---LSEESKKADK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1195 TAATLRKKHadsvaelgEQIDNLQRVKQKLEKEKSEMKMEIDDL---ASNVETVSKAKGNLEKMCRTLEDQVSELKSKE- 1270
Cdd:pfam05622 209 LEFEYKKLE--------EKLEALQKEKERLIIERDTLRETNEELrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEi 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1271 -EEQQRLIND----LTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAhalqSSRH 1345
Cdd:pfam05622 281 rEKLIRLQHEnkmlRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG----SKAE 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1346 DCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEH 1410
Cdd:pfam05622 357 DSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEER 421
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1318-1558 |
1.51e-04 |
|
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: 45.48 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1318 QIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQEskaELQRALSKansevAQWRTKYETDAIQRTEELEEAK 1397
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAK-----AQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1398 KKLAQRLQAAEEHVEAVNAKCASL-EKTKQRLQNEVEDLMLDVERTNaacaaLDKKQRNFDKILAEWKQKYEETHAELEA 1476
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1477 SQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTeqiAEGGKRIHELEKIKKQVEQEKCELQAALEEAEA 1556
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 1958661053 1557 SL 1558
Cdd:pfam06008 244 SL 245
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1347-1579 |
1.69e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1347 CDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQ 1426
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1427 RLQNEVEDLM----LDVErtnaacaalDKKQRNFD--KILAEWKQKYEETHAELEASQKEARSLGTE-------LFKMKN 1493
Cdd:PRK05771 118 ELEQEIERLEpwgnFDLD---------LSLLLGFKyvSVFVGTVPEDKLEELKLESDVENVEYISTDkgyvyvvVVVLKE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1494 AYEESLDQLETLKRENKNLQQEISdLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEheegKILRIQLELN 1573
Cdd:PRK05771 189 LSDEVEEELKKLGFERLELEEEGT-PSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALY----EYLEIELERA 263
|
....*.
gi 1958661053 1574 QVKSEI 1579
Cdd:PRK05771 264 EALSKF 269
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1643-1843 |
1.81e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1643 AAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERV-- 1720
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELge 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1721 QLLHTQNTSLINTK-------KKLETDISQIQGeMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNM 1793
Cdd:COG3883 91 RARALYRSGGSVSYldvllgsESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1794 EQTVKDLQLRLDEAEQLaLKGGKKQIQKLEARVRELEGEVESEQKRNVEA 1843
Cdd:COG3883 167 EAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1319-1585 |
1.83e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.54 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1319 IEELKRQLEEEVKAKNaLAHALQSSRHDCDLLREQYEEEQESKAELqraLSKANSEVAQWRTKYETDAIQRTEELEEAKK 1398
Cdd:NF033838 71 LSEIQKSLDKRKHTQN-VALNKKLSDIKTEYLYELNVLKEKSEAEL---TSKTKKELDAAFEQFKKDTLEPGKKVAEATK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1399 KLAQRLQAAEEHVEA---------------------VNAKCASLEKTKQRLQNEvedlmLDVERTNAACAALDKKQRN-- 1455
Cdd:NF033838 147 KVEEAEKKAKDQKEEdrrnyptntyktleleiaesdVEVKKAELELVKEEAKEP-----RDEEKIKQAKAKVESKKAEat 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1456 -FDKILAEWKQKYEETHAELEASQKEARSLGTELFKM----KNAYEESLDQLETLKRENKNLQQEISDLTEQ-------- 1522
Cdd:NF033838 222 rLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQdkpkRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspslk 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1523 ----IAEGGKRIHELEK-IKKQVEQEK----------CELQAA-----LEEAEASLEHEEGKILRIQLELNQVKSEIDRK 1582
Cdd:NF033838 302 pekkVAEAEKKVEEAKKkAKDQKEEDRrnyptntyktLELEIAesdvkVKEAELELVKEEAKEPRNEEKIKQAKAKVESK 381
|
...
gi 1958661053 1583 IAE 1585
Cdd:NF033838 382 KAE 384
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1492-1942 |
1.83e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1492 KNAYEESLDQLETLKRENKNLQQEISDLTEQIAEggkRIHELEKIKKQVEQEKcelqaaLEEAEASLEHEEGKILRIQLE 1571
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQARLDELEALIDQ---WLAELEQVIALRRAGG------LEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1572 LNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYR 1651
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1652 NTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLI 1731
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1732 NTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLA 1811
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1812 LKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE 1891
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1892 AEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1942
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
872-1020 |
2.25e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 872 KSEAKRKELEEKMVSLLKEkndlqlqvqAEAEgladAEErcdqlIKTKIQLEAKIKEVTERAEDEEEI---NAELTAKKR 948
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEE---------AKKE----AEA-----IKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 949 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----------ETIAKLTKEkkalqEAHQQTLDDLQ 1018
Cdd:PRK12704 90 RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEelieeqlqelERISGLTAE-----EAKEILLEKVE 164
|
..
gi 1958661053 1019 AE 1020
Cdd:PRK12704 165 EE 166
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
916-1118 |
2.33e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 916 IKTKIQLEaKIKEVTERAED--------EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTE 987
Cdd:PRK05771 36 LKEELSNE-RLRKLRSLLTKlsealdklRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 988 EMAGLDETIAKLTKEKKALQ--EAHQQTLDDLQAEED---KVNTLTKAKIKLEQQVDDLEGSLE-QEKKLRM-----DLE 1056
Cdd:PRK05771 108 EISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYiSTDKGYVyvvvvVLK 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1057 RAKRKLEGDLKLAQESIMDIENEKqQLDERLKKKEFEMSNLQSKIEDeqaigiqLQKKIKEL 1118
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES-------LLEELKEL 241
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1468-1754 |
2.41e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1468 EETHAELEASQKEARS-LGTELFKMKNAYEESL----DQLETLKRENKNLQQEISDLTEqiaeggkrihELEKIKKQVEQ 1542
Cdd:pfam00038 24 EQQNKLLETKISELRQkKGAEPSRLYSLYEKEIedlrRQLDTLTVERARLQLELDNLRL----------AAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1543 EkcelQAALEEAEASLeheegKILRIQL-ELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRN-DAIR 1620
Cdd:pfam00038 94 E----LNLRTSAENDL-----VGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEmDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1621 iKKKMEGDLNEMEIQL-NHANRMAAEALRNYRNTQGILKDTQLHLDDALRGQedlKEQLAMVERRANLLQAEIEELRATL 1699
Cdd:pfam00038 165 -KLDLTSALAEIRAQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1700 EQTERSrkIAEQElldasERVQLLHTQNTSLINtkkKLETDISQIQGEMEDIVQE 1754
Cdd:pfam00038 241 ASLERQ--LAETE-----ERYELQLADYQELIS---ELEAELQETRQEMARQLRE 285
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1672-1917 |
2.56e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1672 EDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQllhTQNTSLINTKKKLETDISQIQGEMEDI 1751
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1752 VQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEqLALKGGKKQIQKLEARVRELEG 1831
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEEEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1832 EVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQsntnLSKFRKLQHELE 1911
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLN 247
|
....*.
gi 1958661053 1912 EAEERA 1917
Cdd:pfam07888 248 ASERKV 253
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
860-1087 |
2.68e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 860 KEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEG--------LADAEERCDQLIKTKIQLEAKIKEVTE 931
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 932 RAEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEEMAGL----DETIAKLT------- 1000
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLkknhEEEVRELQaqvsdtq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1001 -----------------------------KEKKALQEAHQQTLDDLQAEEDKVN-TLTKAKIKLEQ---QVDDLEGSLEQ 1047
Cdd:pfam00038 156 vnvemdaarkldltsalaeiraqyeeiaaKNREEAEEWYQSKLEELQQAAARNGdALRSAKEEITElrrTIQSLEIELQS 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958661053 1048 EKKLRMDLERAKRKLE----GDLKLAQESIMDIENEKQQLDERL 1087
Cdd:pfam00038 236 LKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEM 279
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
885-1097 |
3.17e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 885 VSLLKEKNDLQLQVQAEAEGLADA-----EERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKK 959
Cdd:PHA02562 190 IDHIQQQIKTYNKNIEEQRKKNGEniarkQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 960 DIDdlelTLAKVEK--EKHATenkVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEqq 1037
Cdd:PHA02562 270 KIE----QFQKVIKmyEKGGV---CPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL-- 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1038 vdDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNL 1097
Cdd:PHA02562 341 --ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1494-1711 |
3.36e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1494 AYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK---RIHELEKIKKQVEQ----EKceLQAALEEAEASLEHEEGKIL 1566
Cdd:COG0497 166 AWRALKKELEELRADEAERARELDLLRFQLEELEAaalQPGEEEELEEERRRlsnaEK--LREALQEALEALSGGEGGAL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1567 RIqleLNQVKSEIDRkIAEKDEEIDQLKRNhirvVESMQSTLD---AEIRSRNDAIrikkkmEGD---LNEMEIQLNHAN 1640
Cdd:COG0497 244 DL---LGQALRALER-LAEYDPSLAELAER----LESALIELEeaaSELRRYLDSL------EFDperLEEVEERLALLR 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1641 RMAaealRNYRNTqgilkdtqlhLDDALRGQEDLKEQLAMVERRANL---LQAEIEELRATLEQ-----TERSRKIAEQ 1711
Cdd:COG0497 310 RLA----RKYGVT----------VEELLAYAEELRAELAELENSDERleeLEAELAEAEAELLEaaeklSAARKKAAKK 374
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1320-1829 |
3.42e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1320 EELKRQLEEEVKAKNALAHAlqssrhdcdllREQYEEEQESKAELQRALskansevaqwrtkyetdaiqrtEELEEAKKK 1399
Cdd:COG3096 278 NERRELSERALELRRELFGA-----------RRQLAEEQYRLVEMAREL----------------------EELSARESD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1400 LAQRLQAAEEHVEAVNAKCASLEKTkQRLQNEVEDLMLDVERTNAacaaldkkqrnfdkILAEWKQKYEETHAELEASQK 1479
Cdd:COG3096 325 LEQDYQAASDHLNLVQTALRQQEKI-ERYQEDLEELTERLEEQEE--------------VVEEAAEQLAEAEARLEAAEE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1480 EARSLGTELFKmknaYEESLDQLETlkrenKNLQQeisdlteqiaeggkrihelekikKQVEQekcelqaALEEAEASLE 1559
Cdd:COG3096 390 EVDSLKSQLAD----YQQALDVQQT-----RAIQY-----------------------QQAVQ-------ALEKARALCG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1560 HEEgkilriqLELNQVKSEIDRKIAEKDEEIDQLkrnhiRVVESMQSTLDAEIRSRNDAIRIKKKMEGdlnemEIQLNHA 1639
Cdd:COG3096 431 LPD-------LTPENAEDYLAAFRAKEQQATEEV-----LELEQKLSVADAARRQFEKAYELVCKIAG-----EVERSQA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1640 NRMAAEALRNYRNTQGILKDTQ---LHLDDA---LRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQEL 1713
Cdd:COG3096 494 WQTARELLRRYRSQQALAQRLQqlrAQLAELeqrLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1714 LDASERvqllhtqntsLINTKKKLEtDISQIQGEMEDIVQEARNAEEKAKKAitdAAMMAEELKKEQDTSAHlermkknM 1793
Cdd:COG3096 574 AEAVEQ----------RSELRQQLE-QLRARIKELAARAPAWLAAQDALERL---REQSGEALADSQEVTAA-------M 632
|
490 500 510
....*....|....*....|....*....|....*.
gi 1958661053 1794 EQTVKDLQLRLDEAEQLAlkggkKQIQKLEARVREL 1829
Cdd:COG3096 633 QQLLEREREATVERDELA-----ARKQALESQIERL 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1505-1942 |
3.63e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1505 LKRENKNLQQEISDLTE-----QIAEGGKRIHELEKIKKQVEQEKCEL--------QAALEEAEASLEHEEGKILRIQLE 1571
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPldqytQLALMEFAKKKSLHGKAELLTLRSQLltlctpcmPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1572 LNQVKSEIDRKIaEKDEEIDQLKRNHIRVVESMQS--TLDAEIRSRNDAIRIKKKMEGDLNEMEiQLNHANRMAAEALRN 1649
Cdd:TIGR00618 238 TQQSHAYLTQKR-EAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1650 YRNTQGILKDTQLHLDDALRGQEDLKEQlamvERRANLLQAEIEELRATLEQTERSRKIAEQELLDaSERVQLLHTQNTS 1729
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1730 LINTKKKLETDISQIQGEMEDivQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVK-----DLQLRL 1804
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlqESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1805 DEAEQLalKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQakvks 1884
Cdd:TIGR00618 469 KEREQQ--LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE----- 541
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958661053 1885 ykrqaeEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1942
Cdd:TIGR00618 542 ------TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1689-1916 |
3.95e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1689 QAEIEELRATLEQTERSRKiaEQELLDASERVQLLHTQNTSlintKKKLETDISQIQgEMEDIVQEARNAEEKAKKAITD 1768
Cdd:pfam05557 1 RAELIESKARLSQLQNEKK--QMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1769 AAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRL-DEAEQLalkggKKQIQKLEARVRELEGEVESEQKRNVEAVKGL 1847
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958661053 1848 RKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVksykrQAEEAEEQSNTNLSKFRKLQHELEEAEER 1916
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE-----QDSEIVKNSKSELARIPELEKELERLREH 212
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1664-1927 |
3.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1664 LDDALRGQEDLKEQLAMVER-----RANLLQAEIEELRATLEQTERSRKIAEQELLDASERVqllhtqntslintkkkle 1738
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVL------------------ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1739 TDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLrlDEAEqlalkggkkq 1818
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER---LEELEEERDDLLAEAGL--DDAD---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1819 IQKLEARVRELEGEVESEQKRnveavkgLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNT 1898
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDR-------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260
....*....|....*....|....*....
gi 1958661053 1899 NLSKFRKLQHELEEAEERADIAESQVNKL 1927
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1261-1639 |
4.01e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1261 DQVSELKSKEEEQQRLINDLT-TQRGRLQTEsgefsRQLDEKEALVSQLSrgkQAfTQQIEELKRQLEEeVKAKNALAHA 1339
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEqTLALLDKID-----RQKEETEQLKQQLA---QA-PAKLRQAQAELEA-LKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1340 LQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKK--KLAQRLQAAEEHV 1411
Cdd:PRK11281 116 ETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKggKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1412 EaVNAKCASLE-KTKQR---LQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKY----EETHAELEASQKEARS 1483
Cdd:PRK11281 196 L-LQAEQALLNaQNDLQrksLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRltlsEKTVQEAQSQDEAARI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1484 LGTELFKMKNAYE--------ESLDQLETLKREN---KN----LQQEISDLTEQIA--EGG---KRIhelekikkqVEQE 1543
Cdd:PRK11281 275 QANPLVAQELEINlqlsqrllKATEKLNTLTQQNlrvKNwldrLTQSERNIKEQISvlKGSlllSRI---------LYQQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1544 KCELQAALEEAEASleheeGKI--LRI-QLELNQVKSeidrKIAEKDEEIDQLKRNHirvvesmQSTLDAEIR-SRNDAI 1619
Cdd:PRK11281 346 QQALPSADLIEGLA-----DRIadLRLeQFEINQQRD----ALFQPDAYIDKLEAGH-------KSEVTDEVRdALLQLL 409
|
410 420
....*....|....*....|.
gi 1958661053 1620 RIKKKMEGDLN-EMEIQLNHA 1639
Cdd:PRK11281 410 DERRELLDQLNkQLNNQLNLA 430
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
931-1187 |
4.17e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 931 ERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAglDETIAKLTKEKKALQEAH 1010
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER--KRELERIRQEEIAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1011 QQTLDDLQAEEDKVN--------TLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAK----RKLEGDLKLAQESIMDIEN 1078
Cdd:pfam17380 377 MRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEEERAREMERVRLEEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1079 EKQQLDERLKKKEFEMSNLQSKIEDEQaigiQLQKKIKELQARIEELEEEIEAERAsrAKAEKQRSDLSRELEEIS---- 1154
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELEERKQAM--IEEERKRKLLEKEMEERQkaiy 530
|
250 260 270
....*....|....*....|....*....|....*
gi 1958661053 1155 --ERLEEAGGATSAQIEMNKKREAEfQKMRRDLEE 1187
Cdd:pfam17380 531 eeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1063 |
4.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 842 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQ 921
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 922 LEAKIKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEEMAGLDETIAKLTK 1001
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELEAEFDEARI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1002 EKkaLQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1063
Cdd:PRK02224 649 EE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1095-1327 |
4.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1095 SNLQSKIEDEQAIGIQLQKKIKELQARIeeleeeieaerasrAKAEKQRSDLSRELEEISerLEEAGGATSAQIemnkkr 1174
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQKNGLVD--LSEEAKLLLQQL------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1175 eAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNlqRVKQKLEKEKSEMKMEIDDLAsnvetvSKAKGNLEK 1254
Cdd:COG3206 222 -SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELS------ARYTPNHPD 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1255 McRTLEDQVSELKSK-EEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRgKQaftQQIEELKRQLE 1327
Cdd:COG3206 293 V-IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE-LE---AELRRLEREVE 361
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
936-1331 |
4.71e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 936 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQT 1013
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1014 LDDLQAEEdkvntltkakikLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEsimdIENekqQ 1082
Cdd:PRK11281 118 LSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ----IRN---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1083 LDERLKKKEFEMSNLQSKIEDEQA-IGIQLQKKIKELQARIEELEEeieaerasrakAEKQRSdlsrELEEISERLEEAg 1161
Cdd:PRK11281 179 LKGGKVGGKALRPSQRVLLQAEQAlLNAQNDLQRKSLEGNTQLQDL-----------LQKQRD----YLTARIQRLEHQ- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1162 gATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQI------------DNLqRVKQKLEkeks 1229
Cdd:PRK11281 243 -LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVKNWLD---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1230 emkmeiddlasnvetvskakgNLEKMCRTLEDQVSELK-----SKEEEQQR-------LINDLTTQRGRLQTESGEFSRQ 1297
Cdd:PRK11281 317 ---------------------RLTQSERNIKEQISVLKgslllSRILYQQQqalpsadLIEGLADRIADLRLEQFEINQQ 375
|
410 420 430
....*....|....*....|....*....|....*...
gi 1958661053 1298 LDE---KEALVSQLSRG-KQAFTqqiEELKRQLEEEVK 1331
Cdd:PRK11281 376 RDAlfqPDAYIDKLEAGhKSEVT---DEVRDALLQLLD 410
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1081-1243 |
4.73e-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: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1081 QQLDERLKKKEFEMSNLQSKIEDeqaigiqLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEA 1160
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1161 GG-----ATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEI 1235
Cdd:COG1579 86 RNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 1958661053 1236 DDLASNVE 1243
Cdd:COG1579 166 EELAAKIP 173
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1734-1933 |
5.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1734 KKKLETDISQIQGEMEDIVqEARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKKnmEQTVKDLQLRLDEAEQl 1810
Cdd:COG4913 220 EPDTFEAADALVEHFDDLE-RAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRA--ALRLWFAQRRLELLEA- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1811 ALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKH--------ERRVKELTYQTEEDRKNILRLQDLVDKLQAKV 1882
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1883 KSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNK-LRVKSRE 1933
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRReLRELEAE 427
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1734-1921 |
5.81e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1734 KKKLETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDtsahlermkknmeqtvKDLQLRldeaeqlal 1812
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFE----------------KELRER--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1813 kggKKQIQKLEARVRELEGEVESEQKRnveavkgLRKHERRVkeltyqtEEDRKNILRLQDLVDKLQAKVKS-YKRQAEE 1891
Cdd:PRK12704 81 ---RNELQKLEKRLLQKEENLDRKLEL-------LEKREEEL-------EKKEKELEQKQQELEKKEEELEElIEEQLQE 143
|
170 180 190
....*....|....*....|....*....|
gi 1958661053 1892 AEEQSNTNLSKFRKLQHELEEAEERADIAE 1921
Cdd:PRK12704 144 LERISGLTAEEAKEILLEKVEEEARHEAAV 173
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1760-1932 |
6.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1760 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLalkggkKQIQKLEARVRELEGEVESEQKR 1839
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1840 nveaVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQA-EEAEEQSNTNLSKFRKLQHELEEAEERAD 1918
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....
gi 1958661053 1919 IAESQVNKLRVKSR 1932
Cdd:COG4717 224 ELEEELEQLENELE 237
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1629-1928 |
7.47e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1629 LNEMEIQLnHANRMAAEALRNYRNTQGILK-------------------DTQLHLDDALRGQEDL---KEQLAMVERRAN 1686
Cdd:PRK04863 232 FQDMEAAL-RENRMTLEAIRVTQSDRDLFKhlitestnyvaadymrhanERRVHLEEALELRRELytsRRQLAAEQYRLV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1687 LLQAEIEELratleqtERSRKIAEQELLDASERVQLLhtqNTSLINTKKkletdISQIQGEMEDIVQEArnaeEKAKKAI 1766
Cdd:PRK04863 311 EMARELAEL-------NEAESDLEQDYQAASDHLNLV---QTALRQQEK-----IERYQADLEELEERL----EEQNEVV 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1767 TDAAMMAEELkKEQDTSAHLE--RMKKNM--------EQTVKDLQLR-----LDEAEQ------LALKGGKKQIQKLEAR 1825
Cdd:PRK04863 372 EEADEQQEEN-EARAEAAEEEvdELKSQLadyqqaldVQQTRAIQYQqavqaLERAKQlcglpdLTADNAEDWLEEFQAK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1826 VRELEGEV-ESEQKRNV---------EAVKGLRK---------HERRVKELTYQTEEDRKNILRLQDLVDKLQA------ 1880
Cdd:PRK04863 451 EQEATEELlSLEQKLSVaqaahsqfeQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQLQQLRMRLSEleqrlr 530
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1958661053 1881 KVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNKLR 1928
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
909-1050 |
7.54e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 909 EERCDQLIKTKIQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 987
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 988 EMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKK 1050
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1497-1746 |
8.43e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1497 ESLDQLETLKRENKNLQQEISDLTEQIAEGGKrihELEKIKKQVEQEKCE---------LQAALEEAEASLEheegkilR 1567
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEETREtlstlslrqLESRLAQTLDQLQ-------N 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1568 IQLELNQVKSEIdrkIAEKdeeiDQLKRNHIRVVESMQSTLdaEIRSRNDAIRIKKKmegDLNEMEIQLNHANRMAAEAL 1647
Cdd:PRK11281 140 AQNDLAEYNSQL---VSLQ----TQPERAQAALYANSQRLQ--QIRNLLKGGKVGGK---ALRPSQRVLLQAEQALLNAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1648 RNYR------NTQgilkdtqlhLDDALRGQEDLK-EQLAMVERRANLLQAEIEELR-----ATLEQTERSRKIAE----- 1710
Cdd:PRK11281 208 NDLQrkslegNTQ---------LQDLLQKQRDYLtARIQRLEHQLQLLQEAINSKRltlseKTVQEAQSQDEAARiqanp 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1711 -------------QELLDASERVQLLHTQN-------TSLINTKKKLETDISQIQG 1746
Cdd:PRK11281 279 lvaqeleinlqlsQRLLKATEKLNTLTQQNlrvknwlDRLTQSERNIKEQISVLKG 334
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
955-1214 |
1.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 955 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKL 1034
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1035 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKK 1114
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1115 IKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEA 1194
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260
....*....|....*....|
gi 1958661053 1195 TAATLRKKHADSVAELGEQI 1214
Cdd:COG4372 267 ILVEKDTEEEELEIAALELE 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
868-1072 |
1.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 868 DELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKK 947
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 948 RKLEDECSELK-----KDIDDLeltLAKVEKEKHATENKvknlTEEMAGLDETIAKLTKEKKALQEAhQQTLDDLQAE-E 1021
Cdd:COG3883 96 YRSGGSVSYLDvllgsESFSDF---LDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAK-LAELEALKAElE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 1022 DKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1072
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1456-1917 |
1.14e-03 |
|
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: 44.19 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1456 FDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEisdlTEQIAEGGKRIHELEK 1535
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ----TQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1536 IKKQVEQEKCELQAALEEAEAslehEEGKILRIQLELNQVKSEIdrKIAEKDEEIDQLKRNHIRVVESMQSTLdaeiRSR 1615
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRA----QEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKM----RSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1616 NDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGIL-----KDTQLHLDDALRGQEDLKEQLAMVERRANLLQA 1690
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsireiSCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1691 EIEELRATLEQTERSRKIAEQELLDASERVQL---------LHTQNTSLINTKKKLE-TDISQIQGEMEDIVQEARNAEE 1760
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELqqryaelcaAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1761 KAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKR- 1839
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQr 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1840 ------NVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKLQHELEEA 1913
Cdd:TIGR00618 559 aslkeqMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
....
gi 1958661053 1914 EERA 1917
Cdd:TIGR00618 639 QELA 642
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1554-1784 |
1.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1554 AEASLEHEEGKILRIQLELNQVKSEIDR---KIAEKDEEIDQLKrnhirvvesmqstldAEIRSRNDAIrikKKMEGDLN 1630
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDAlqaELEELNEEYNELQ---------------AELEALQAEI---DKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1631 EMEIQLNHANRMAAEALRNYRNTQGILKDTqlhldDALRGQEDLKEQLamveRRANLLQAEIEELRATLEQTERSRKIAE 1710
Cdd:COG3883 76 EAEAEIEERREELGERARALYRSGGSVSYL-----DVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1711 QELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSA 1784
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1573-1770 |
1.23e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1573 NQVKSEIDRKI--AEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIrikkkmEGDLNEMEIQLNHANRmAAEALRNY 1650
Cdd:NF012221 1563 DKERAEADRQRleQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAI------LEESRAVTKELTTLAQ-GLDALDSQ 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1651 RNTQ-------------GILKDTQLHLDDAlrgQEDLKEQLAMVERR--ANLLQAE--IEELRATLEQTERSRKIAEQEL 1713
Cdd:NF012221 1636 ATYAgesgdqwrnpfagGLLDRVQEQLDDA---KKISGKQLADAKQRhvDNQQKVKdaVAKSEAGVAQGEQNQANAEQDI 1712
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1714 LDASERVQLLHTQNTSLINTKKKLETDIS------QIQGEmedivQEARNAEEKAKKAITDAA 1770
Cdd:NF012221 1713 DDAKADAEKRKDDALAKQNEAQQAESDANaaandaQSRGE-----QDASAAENKANQAQADAK 1770
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1674-1942 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1674 LKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKklETDISQIQGEMEDIVQ 1753
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ--ERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1754 EARNAEEKAkkaitdaaMMAEELKKEQDTSAHLERMKknMEQTVKDLQLR-----------LDEAEQLALKGGKKQIQKL 1822
Cdd:pfam17380 356 EERKRELER--------IRQEEIAMEISRMRELERLQ--MERQQKNERVRqeleaarkvkiLEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1823 -----EARVRELEgEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKnilrlqdlvdKLQAKVKSYKRQAEEAEEQSn 1897
Cdd:pfam17380 426 raeqeEARQREVR-RLEEERAREMERVRLEEQERQQQVERLRQQEEERK----------RKKLELEKEKRDRKRAEEQR- 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1958661053 1898 tnlskfRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 1942
Cdd:pfam17380 494 ------RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1260-1486 |
1.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1260 EDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHA 1339
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1340 LQSSRHDCDLL---------------REQYEEEQESKAELQRALSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRL 1404
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1405 QAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSL 1484
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 1958661053 1485 GT 1486
Cdd:COG3883 251 AA 252
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1457-1756 |
1.45e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1457 DKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKI 1536
Cdd:PLN02939 113 NEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1537 KKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEidrKIAEKDeEIDQLKRNHIRVVESMQSTLDAEirsrn 1616
Cdd:PLN02939 193 KIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAETEERVFKLE----- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1617 daiRIKKKMEGDLNEMEIQLNHANrmaAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELR 1696
Cdd:PLN02939 264 ---KERSLLDASLRELESKFIVAQ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLE 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1697 ATLEQTERSR------KIAEQELLDASERVQLLHTQNTSLIntkKKLETDISQIQGEMEDIVQEAR 1756
Cdd:PLN02939 338 ASLKEANVSKfssykvELLQQKLKLLEERLQASDHEIHSYI---QLYQESIKEFQDTLSKLKEESK 400
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1669-1933 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1669 RGQEDLKEQLAMVERRANL------LQAEIEELRATLEQTERSRKIAEQELldasERVQLLHTQNTSLINTKKKLETDIS 1742
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLeeaekaRQAEMDRQAAIYAEQERMAMEREREL----ERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1743 QIQgEMEDIVQEARNAEEKAKKAITDA----AMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQ 1818
Cdd:pfam17380 376 RMR-ELERLQMERQQKNERVRQELEAArkvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1819 IQKLEARVRELEGEVESEQKRNVEAVKGLRKH----ERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKsyKRQAEEAEE 1894
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEME--ERQKAIYEE 532
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958661053 1895 QSNTNLSKFRKLQHELEE---AEERADIAESQVNKLRVKSRE 1933
Cdd:pfam17380 533 ERRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMERE 574
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1199-1414 |
1.54e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1199 LRKKHADSvAELGEQIDNLQRVKQKLEKEKSE-MKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLI 1277
Cdd:PRK05771 45 LRKLRSLL-TKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1278 NDLTtqrgRLQTESGEFSRQLDEK--EALVSQLSRGKQAFTQQIEElKRQLEEEVKAKN-----ALAHALQSSRHDCDLL 1350
Cdd:PRK05771 124 ERLE----PWGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESD-VENVEYISTDKGyvyvvVVVLKELSDEVEEELK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1351 REQYEEEQ-ESKAELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQAAEEHVEAV 1414
Cdd:PRK05771 199 KLGFERLElEEEGTPSELIREIKEELEEIEKERE----SLLEELKELAKKYLEELLALYEYLEIE 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1197 |
1.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 967 TLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDdlegslE 1046
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1047 QEKKLRMDLERAKRKLEGDLKLAQ--------------ESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAigiQLQ 1112
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLA---ELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1113 KKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQH 1192
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
....*
gi 1958661053 1193 EATAA 1197
Cdd:COG3883 241 AAAAS 245
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
847-1106 |
1.88e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 847 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVqaeaegladaeERCDQLIKtkiQLEAKI 926
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----------EEKDERIE---RLEREL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 927 KEVTERAEDEEEINAELTAkkrkledecseLKKDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------TIAK 998
Cdd:COG2433 451 SEARSEERREIRKDREISR-----------LDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 999 LTKEkkALQEAHQQT---------LDDLQ-AEEDKVNTLTKAKIKL----EQQVDDLEGSLEQEKKLRMDLERAKRKLEG 1064
Cdd:COG2433 519 FTKE--AIRRLEEEYglkegdvvyLRDASgAGRSTAELLAEAGPRAvivpGELSEAADEVLFEEGIPVLPAEDVTIQEVD 596
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1958661053 1065 DLKLAQESIMD--IENEKQQLDERLKKKEFEMsnLQSKIEDEQA 1106
Cdd:COG2433 597 DLAVVDEEELEaaIEDWEERAEERRREKKAEM--LERLISEYRA 638
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1441-1585 |
1.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1441 RTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEarslgtELFKMKNAYE-ESLDQLETLKRENKNLQQEISDL 1519
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKE------EIHKLRNEFEkELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1520 TEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRI---------QLELNQVKSEIDRKIAE 1585
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAAV 173
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
879-1005 |
1.92e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 42.83 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 879 ELEEKMVSLLKEKNDLQLQVQAEAEG-----LADAEERCD----QLIKTKI-QLEAKIKEVTERAEdeeEINAELTAKKR 948
Cdd:pfam10186 23 ELRVDLARLLSEKDSLKKKVEEALEGkeegeQLEDNIGNKklklRLLKSEVaISNERLNEIKDKLD---QLRREIAEKKK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958661053 949 KLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKA 1005
Cdd:pfam10186 100 KIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
850-975 |
2.11e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELEekmvsLLKEKNDLQLQVQAEAEGLADAEERCdqliktkIQLEAKIKEV 929
Cdd:PTZ00491 672 AELLEQEARGRLERQKMHDKAKAEEQRTKLLE-----LQAESAAVESSGQSRAEALAEAEARL-------IEAEAEVEQA 739
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958661053 930 TERAEDEE-EINAELTAKKRKLEDECsELKKDIDDLELT----LAKVEKEK 975
Cdd:PTZ00491 740 ELRAKALRiEAEAELEKLRKRQELEL-EYEQAQNELEIAkakeLADIEATK 789
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1041-1436 |
2.16e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1041 LEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDeqaigiqLQKKIKELQa 1120
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEE-------LEEKYKELS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1121 rieeleeeieaerASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQheataatLR 1200
Cdd:pfam07888 108 -------------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQ-------RK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1201 KKHADSvaelgeqiDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDL 1280
Cdd:pfam07888 168 EEEAER--------KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1281 TTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQ---QIEELKRQLEEevkAKNALAHALQSSRHDCDLLREQYEEE 1357
Cdd:pfam07888 240 RSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLAD---ASLALREGRARWAQERETLQQSAEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1358 QESKAELQRALSKANSEVAQWRTKYEtdaiqrTEELEEAKKKLAQRLQAAEEHVEAVNAKCA--SLEKTKQRLQNEVEDL 1435
Cdd:pfam07888 317 KDRIEKLSAELQRLEERLQEERMERE------KLEVELGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQEL 390
|
.
gi 1958661053 1436 M 1436
Cdd:pfam07888 391 L 391
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
981-1236 |
2.25e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 981 KVKNLTEEMAGLDETIaKLTKEKKALQEAHQQTLDDLQAE-----EDKVNTLTKAKIKLEQQVDDLEgslEQEKKLRMDL 1055
Cdd:PHA02562 175 KIRELNQQIQTLDMKI-DHIQQQIKTYNKNIEEQRKKNGEniarkQNKYDELVEEAKTIKAEIEELT---DELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1056 ErakrKLEGDLKLAQESIMDIENEKQQLDERLK--KKEFEMSNLQSKIEDEQAIGIQLQKKIKELQarieeleeeieaer 1133
Cdd:PHA02562 251 E----DPSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCTQQISEGPDRITKIKDKLKELQ-------------- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1134 asrakaeKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEAtLQHEATAATLRKKHADSVAELGEQ 1213
Cdd:PHA02562 313 -------HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|...
gi 1958661053 1214 IDNLQrvkqKLEKEKSEMKMEID 1236
Cdd:PHA02562 385 QDELD----KIVKTKSELVKEKY 403
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1395-1810 |
2.32e-03 |
|
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: 42.92 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1395 EAKKKLA---QRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMldvertnaacaaldKKQRNFDKILAEWKQKYEETH 1471
Cdd:pfam06160 83 KAKKALDeieELLDDIEEDIKQILEELDELLESEEKNREEVEELK--------------DKYRELRKTLLANRFSYGPAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1472 AELEASQKEARSLGTELFKMKNA--YEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHE-LEKIK----------- 1537
Cdd:pfam06160 149 DELEKQLAEIEEEFSQFEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDqLEELKegyremeeegy 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1538 ----KQVEQEKCELQAALEEAEASLEheegkilriQLELNQVKSEIDrkiaEKDEEIDQLkrnhirvvesmQSTLDAEIR 1613
Cdd:pfam06160 229 alehLNVDKEIQQLEEQLEENLALLE---------NLELDEAEEALE----EIEERIDQL-----------YDLLEKEVD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1614 SRNDAIRIKKKMEGDLNEMEIQLNHANRMAAEALRNYrntqgILKDTQLHLddalrgQEDLKEQLAMVERRANLLQAEIE 1693
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSY-----TLNENELER------VRGLEKQLEELEKRYDEIVERLE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1694 ELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAE-----EKAKKAITD 1768
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFD 433
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1958661053 1769 AAMMAEELKKEqdtsahLERMKKNMEQTVKDLQLRLDEAEQL 1810
Cdd:pfam06160 434 VSDEIEDLADE------LNEVPLNMDEVNRLLDEAQDDVDTL 469
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1111-1862 |
2.40e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1111 LQKKIKELQARIEE-LEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKM-------- 1181
Cdd:pfam10174 1 LQAQLRDLQRENELlRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLqltiqalq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1182 -----RRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKG----NL 1252
Cdd:pfam10174 81 delraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGardeSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1253 EKMCRTLEDQVSELKSKEEEQQRlindlTTQRGRLQTESGEFSRQLDEKE----ALVSQLSRGKQAftQQIEELKRQLEE 1328
Cdd:pfam10174 161 KKLLEMLQSKGLPKKSGEEDWER-----TRRIAEAEMQLGHLEVLLDQKEkeniHLREELHRRNQL--QPDPAKTKALQT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1329 EVKAKNA-----------LAHALQSSRHDCDLLREQYEEE--------QESK------AELQRALSKANSEVAQWRTKYE 1383
Cdd:pfam10174 234 VIEMKDTkisslernirdLEDEVQMLKTNGLLHTEDREEEikqmevykSHSKfmknkiDQLKQELSKKESELLALQTKLE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1384 TDAIQRTEeleeakkklaqrlqaAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDvertnaacaaLDKKQRNFDKilaew 1463
Cdd:pfam10174 314 TLTNQNSD---------------CKQHIEVLKESLTAKEQRAAILQTEVDALRLR----------LEEKESFLNK----- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1464 KQKYeethaeLEASQKEARSLGTELFKMKnayeeslDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQE 1543
Cdd:pfam10174 364 KTKQ------LQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1544 KCELQAALEEAEASLEHEEGKILRIqlelnqvKSEIDRKIAEKDEEIDQLKRN-----------HIRVVESMQSTLDAEI 1612
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERL-------KEQREREDRERLEELESLKKEnkdlkekvsalQPELTEKESSLIDLKE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1613 RSRNDAIRIKKKmEGDLNEMEIQLNHANRMAAEalrnyrnTQGILKDTQlHLDDALRGQEDLKEQLAMVERR-------A 1685
Cdd:pfam10174 504 HASSLASSGLKK-DSKLKSLEIAVEQKKEECSK-------LENQLKKAH-NAEEAVRTNPEINDRIRLLEQEvarykeeS 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1686 NLLQAEIEELRATLEQTE-----RSRKIAEQElldaSERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEE 1760
Cdd:pfam10174 575 GKAQAEVERLLGILREVEnekndKDKKIAELE----SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAD 650
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1761 KAKKAITDAAMMA-EELKKEQD-TSAHLERMKKNMEQTVKDL-QLRLDEAEQLALKGGKKQiQKLEARVRELEGEV---- 1833
Cdd:pfam10174 651 NSQQLQLEELMGAlEKTRQELDaTKARLSSTQQSLAEKDGHLtNLRAERRKQLEEILEMKQ-EALLAAISEKDANIalle 729
|
810 820 830
....*....|....*....|....*....|..
gi 1958661053 1834 --ESEQKRNVEAVKGL-RKHERRVKELTYQTE 1862
Cdd:pfam10174 730 lsSSKKKKTQEEVMALkREKDRLVHQLKQQTQ 761
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1447-1836 |
2.67e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1447 AALDKKQRNFDKILAEWKQKYEETHAELEASQKEARS----LGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQ 1522
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESrvaeLKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1523 IAEGGKRIHELEKIKKQVEQEKCELQAALE-------EAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKdeeidQLKR 1595
Cdd:pfam07888 124 RAAHEARIRELEEDIKTLTQRVLERETELErmkerakKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF-----QELR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1596 NHIRVVESMQSTLDAEIrsrndairikkkmegdlNEMEIQLNHANRMAAE---ALRNYRNTQGILKDTQlhlddalRGQE 1672
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTI-----------------TTLTQKLTTAHRKEAEneaLLEELRSLQERLNASE-------RKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1673 DLKEQLA-MVERR----ANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLhtQNTSLinTKKKLETDISQIQgE 1747
Cdd:pfam07888 255 GLGEELSsMAAQRdrtqAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQ--QSAEA--DKDRIEKLSAELQ-R 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1748 MEDIVQEARNAEEKAKKaitdaammaeELKKEQDTS-AHLERMKKNMEQTVKDLQLRLDEAEQLALkggkkQIQKLEARV 1826
Cdd:pfam07888 330 LEERLQEERMEREKLEV----------ELGREKDCNrVQLSESRRELQELKASLRVAQKEKEQLQA-----EKQELLEYI 394
|
410
....*....|
gi 1958661053 1827 RELEGEVESE 1836
Cdd:pfam07888 395 RQLEQRLETV 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1425-1715 |
2.83e-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: 42.80 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1425 KQRLQNEVEDLMLDVERTNAACAALDKKQRNFDK---ILAEWKQKYEETHAELEASQKEARslgtelfkmknayeesldq 1501
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1502 letlKRENKNLQQEisdlteQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEgkilriqlelnqvksEIDR 1581
Cdd:pfam17380 359 ----KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---------------ERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1582 KIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRikkkmegdLNEMEIQlnhanrMAAEALRNYRNTQgilKDTQ 1661
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--------LEEQERQ------QQVERLRQQEEER---KRKK 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1662 LHLDDALRGQEDLKEQlamverRANLLQAEIEELRATLEQTERSRKIAEQELLD 1715
Cdd:pfam17380 477 LELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1213-1404 |
2.91e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1213 QIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRgrlqtesg 1292
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1293 EFsrqldekealvsqlsrgkQAFTQQIEELKRQ---LEEEVKAKNALAHALQssrhdcdllrEQYEEEQESKAELQRALS 1369
Cdd:COG1579 90 EY------------------EALQKEIESLKRRisdLEDEILELMERIEELE----------EELAELEAELAELEAELE 141
|
170 180 190
....*....|....*....|....*....|....*
gi 1958661053 1370 KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRL 1404
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
850-1158 |
3.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 850 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEV 929
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 930 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKE------K 1003
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqalD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1004 KALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQL 1083
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958661053 1084 DERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLE 1158
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1657-1899 |
3.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1657 LKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKK 1736
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1737 LETDISQIqgemeDIVQEARNAEEkakkAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAlkggk 1816
Cdd:COG3883 98 SGGSVSYL-----DVLLGSESFSD----FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1817 kqiQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQS 1896
Cdd:COG3883 164 ---AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
...
gi 1958661053 1897 NTN 1899
Cdd:COG3883 241 AAA 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
845-1009 |
3.46e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 845 PLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEA 924
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 925 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE---LT----LAKVEKEKHATENKVKNLTEEMAGLDETIA 997
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaieeYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 1958661053 998 KLTKEKK-ALQEA 1009
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
772-1117 |
3.49e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 772 FKAGLLGLLEEMR---------DDKLAQLITRTQAMcrgflarvEYQKMVERRESIFCIQYNIRAFMNVKHWPWMKLFF- 841
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQEL--------KWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 842 ---KIKPLLKSAETEKEMATMKE---EFQKTKDELAKseaKRKELEEKMVSLLKEKNDLQLQVqaeaeglaDAEERCDQL 915
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEGLKEtlkALQVSKYSLQK---KVSEMEQKLQLHLLAKEDHHKQL--------NEIEKYYAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 916 IKTKIQLEAKIKEVTERAEDEE-EINAELTAKKRKLEDECSELKKDIDDL--ELTLAKVE-KEKHATEN--------KVK 983
Cdd:pfam15818 146 ITGQFGLVKENHGKLEQNVQEAiQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqKFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 984 NLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEgslEQEKKLRMDLERAKRKLe 1063
Cdd:pfam15818 226 ELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKV- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1064 gdlKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKE 1117
Cdd:pfam15818 302 ---KENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1458-1763 |
3.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1458 KILAEWKQKYEETHAEL--EASQKEARSLGTELFKMKNAYEESLDQLETLKRENK--NLQQEISDLTEQIAEggkriheL 1533
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------L 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1534 EKIKKQVEQEKCELQAALEEAEASLEHEEGKI--LRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVEsmqstLDAE 1611
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA-----LRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1612 IRSRNDAIRikkkmegdlnemeiqlnhanRMAAEALRNYRNtqgilkdtqlhlddalrgqedlkeQLAMVERRANLLQAE 1691
Cdd:COG3206 300 IAALRAQLQ--------------------QEAQRILASLEA------------------------ELEALQAREASLQAQ 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958661053 1692 IEELRATLEQTERsrkiAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEdIVQEARNAEEKAK 1763
Cdd:COG3206 336 LAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR-VIDPAVVPLKPVS 402
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1428-1741 |
3.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1428 LQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKR 1507
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1508 ENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQvkseidRKIAEKD 1587
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA------LSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1588 EEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNhanrmAAEALRNYRNTQGILKDTQLHLDDA 1667
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG-----LALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958661053 1668 LRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDI 1741
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1391-1926 |
4.13e-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: 41.94 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1391 EELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKqrlqNEVEDLMLDVERtnaacAALDKKQRNFDKILAEWKQKYEET 1470
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVEEMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1471 HAELEASQkearSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKR----IHELEKIKKQVEQEKCE 1546
Cdd:pfam05701 113 GIADEASV----AAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRaeeaVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1547 LQAALEEAE----ASLEHEEGKIlRIQLELNQVKSEIDRKIAEKDEEIDQLkRNHIRVVESMQSTLDAeirsrndAIRIK 1622
Cdd:pfam05701 189 LIATKESLEsahaAHLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1623 KKMEGDLNE-MEIQLNHANRMAAEALRNYRNTQGILKDTQLHLddalrgqEDLKEQLAMVERRANLLQAEIEELRATLEQ 1701
Cdd:pfam05701 260 LDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKEL-------EEVKANIEKAKDEVNCLRVAAASLRSELEK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1702 tersrkiaEQELLDaservqllhtqntSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAitdAAMMAEELKKEQD 1781
Cdd:pfam05701 333 --------EKAELA-------------SLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1782 TSAHLERMKKNMEQTVKDLQLRLDEAEQlaLKGGKKQIQ-KLEARVRELEGEVESEqKRNVEAVKGLRKHERRvKELTYQ 1860
Cdd:pfam05701 389 AAQEAEEAKSLAQAAREELRKAKEEAEQ--AKAAASTVEsRLEAVLKEIEAAKASE-KLALAAIKALQESESS-AESTNQ 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958661053 1861 TEEDRKNILRLQDLvdklqakvKSYKRQAEEAEEQSNTNLSKFRKLQHELEEAEERADIAESQVNK 1926
Cdd:pfam05701 465 EDSPRGVTLSLEEY--------YELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1666-1862 |
4.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1666 DALRGQEDLKEQLAmverranLLQAEIEELRATLEQTERSRKI----------AEQELLDASERVQLLHTQNTSLINTK- 1734
Cdd:PRK11281 46 DALNKQKLLEAEDK-------LVQQDLEQTLALLDKIDRQKEEteqlkqqlaqAPAKLRQAQAELEALKDDNDEETRETl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1735 -----KKLETDISQIQGEMEDiVQEA-----------RNAEEKAKKAITDAAMMAEE----LKKEQDTSAHL---ERMKK 1791
Cdd:PRK11281 119 stlslRQLESRLAQTLDQLQN-AQNDlaeynsqlvslQTQPERAQAALYANSQRLQQirnlLKGGKVGGKALrpsQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1792 NMEQTVKDLQLRLdeaEQLALKG-------GKKQIQKLEARVRELEGEVESEQkrnvEAV--KGLRKHERRVKELTYQTE 1862
Cdd:PRK11281 198 QAEQALLNAQNDL---QRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQ----EAInsKRLTLSEKTVQEAQSQDE 270
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1679-1856 |
4.40e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1679 AMVERRANLLqaEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNA 1758
Cdd:COG1579 1 AMPEDLRALL--DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1759 EEKAKKAITdaammAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEqlalkggkKQIQKLEARVRELEGEVESEQK 1838
Cdd:COG1579 79 EEQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMERIEELE--------EELAELEAELAELEAELEEKKA 145
|
170
....*....|....*...
gi 1958661053 1839 RNVEAVKGLRKHERRVKE 1856
Cdd:COG1579 146 ELDEELAELEAELEELEA 163
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1212-1330 |
4.63e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1212 EQIDNLQRVKQKLEKEKSEMKMEIDDlasnvetVSKAK-GNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGrlqte 1290
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDE-------ASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKE----- 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1958661053 1291 sgefsrQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEV 1330
Cdd:COG0542 479 ------ELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1262-1375 |
4.97e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1262 QVSELKSKEEEqqrLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKA--KNALAHA 1339
Cdd:PRK00409 510 LIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaiKEAKKEA 586
|
90 100 110
....*....|....*....|....*....|....*..
gi 1958661053 1340 LQSSRHDCDLLREQYEEEQESKA-ELQRALSKANSEV 1375
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHELiEARKRLNKANEKK 623
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1786-1904 |
5.46e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1786 LERMKK-NMEQTVKDLQLRLDEAEQL------ALKGGKKQIQKLEARVRELEGEVESEQKRNVEAVkglrkheRRVKELT 1858
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1958661053 1859 YQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEE-------AEEQSNTNLSKFR 1904
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1683-1921 |
6.03e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1683 RRANLLQAEIEELratLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNA---- 1758
Cdd:COG1842 5 RLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLAlekg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1759 -EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQIQKLEARVRELEGeveseQ 1837
Cdd:COG1842 82 rEDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKA--------KKDTLKARAKAAKA-----Q 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1838 KRNVEAVKGLRkherrvkeltyqTEEDRKNILRLQDLVDKLQAKVKSYkrqAEEAEEQSntnlskfrkLQHELEEAEERA 1917
Cdd:COG1842 149 EKVNEALSGID------------SDDATSALERMEEKIEEMEARAEAA---AELAAGDS---------LDDELAELEADS 204
|
....
gi 1958661053 1918 DIAE 1921
Cdd:COG1842 205 EVED 208
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
960-1062 |
7.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 960 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVD 1039
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 1958661053 1040 DLEGSLEQEKKLRMDLERAKRKL 1062
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1175-1435 |
7.43e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1175 EAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKgnlek 1254
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1255 mcRTLEDQVSELKskeeeqqRLINDLTTQRGRLQ------TESGEFSRQLDEKEalVSQLSRgkqaftqQIEELKRQLEE 1328
Cdd:pfam00038 99 --TSAENDLVGLR-------KDLDEATLARVDLEakieslKEELAFLKKNHEEE--VRELQA-------QVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1329 EVKAKNALAHALQSsrhdcdlLREQYEEeqeskaelQRALSKANSEvAQWRTKYE---TDAIQRTEELEEAKKKLAQ--- 1402
Cdd:pfam00038 161 DAARKLDLTSALAE-------IRAQYEE--------IAAKNREEAE-EWYQSKLEelqQAAARNGDALRSAKEEITElrr 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958661053 1403 RLQAAEEHVEAVNAKCASLEK----TKQRLQNEVEDL 1435
Cdd:pfam00038 225 TIQSLEIELQSLKKQKASLERqlaeTEERYELQLADY 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1779-1942 |
7.84e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1779 EQDTSAHLERMKKNMEQtvkdlqlrLDEAEQLALKGgKKQIQKLEaRVRELEGEVEsEQKRNVEAVKGLR------KHER 1852
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYA-AARERLAELEYLRaalrlwFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1853 RVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTN-LSKFRKLQHELEEAEERADIAESQVNKLRVKS 1931
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170
....*....|.
gi 1958661053 1932 REVHTKVISEE 1942
Cdd:COG4913 369 AALGLPLPASA 379
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1816-1924 |
7.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1816 KKQIQKLEARVRELEGEVESEQKRNVEAVKGLRKHERRVKEL---TYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1892
Cdd:COG2433 412 EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArseERREIRKDREISRLDREIERLERELEEERERIEEL 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1958661053 1893 EEQSNTnLSKFRKLQH----------------ELEEAEERADIAESQV 1924
Cdd:COG2433 492 KRKLER-LKELWKLEHsgelvpvkvvekftkeAIRRLEEEYGLKEGDV 538
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1302-1414 |
8.91e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 40.38 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1302 EALVSQLSRGKQAFTQQIEELKRQLEEEVKAKnALAHALqSSRHDCDLLREQYEEEQESKAELQRALSKANSEvaQWRTK 1381
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 1958661053 1382 YEtDAIQRTEELEEAKKKLAQRLQAAEEHVEAV 1414
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
851-1091 |
8.91e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 851 ETEKEMATMKEE---FQKTKDELAKSEAKRKELEEKMVSLLKEknDLQLQVQAEAEgLADAEERCDQLIKTKIQLeaKIK 927
Cdd:PRK01156 487 EIEIEVKDIDEKivdLKKRKEYLESEEINKSINEYNKIESARA--DLEDIKIKINE-LKDKHDKYEEIKNRYKSL--KLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 928 EVTERAEDEEEINAELTAKK-RKLEDECSELKKDIDDLELTLAKVEKE----KHATENKVKNLTEEMAGLDETIaKLTKE 1002
Cdd:PRK01156 562 DLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY-NEIQE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1003 KKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQ 1082
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
....*....
gi 1958661053 1083 LDERLKKKE 1091
Cdd:PRK01156 721 INETLESMK 729
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1297-1527 |
9.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1297 QLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSevA 1376
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR--A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1377 QWRTKYE-------------TDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTN 1443
Cdd:COG3883 95 LYRSGGSvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1444 AACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQI 1523
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....
gi 1958661053 1524 AEGG 1527
Cdd:COG3883 255 AGAA 258
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
856-1328 |
9.44e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 856 MATMKEEFQKTKDELAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQliktkiqlEAKIKE-VTERAE 934
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ--------EARIKDlEAQRAQ 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 935 DE----------------EEINA-ELTAKKRKLedecselkkdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIA 997
Cdd:PRK10246 500 LQagqpcplcgstshpavEAYQAlEPGVNQSRL-----------DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQ 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 998 KLTKEKKALQEAHQQTLDDL---QAEEDKVNTLTKAKIKLEQQVDDL----------EGSLEQEKKLRMDLERAKRKLEG 1064
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCASLnitLQPQDDIQPWLDAQEEHERQLRLLsqrhelqgqiAAHNQQIIQYQQQIEQRQQQLLT 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1065 DLKLAQESIMDIENEKQQLDERlkkkefemsnlqskiEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRS 1144
Cdd:PRK10246 649 ALAGYALTLPQEDEEASWLATR---------------QQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEET 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1145 DLSRELEEISERleeaggATSAQIEMNKKREAEFQKMRRdLEEATLQHEA--TAATLRKKHADSVAELGEQ-IDNLQRVK 1221
Cdd:PRK10246 714 VALDNWRQVHEQ------CLSLHSQLQTLQQQDVLEAQR-LQKAQAQFDTalQASVFDDQQAFLAALLDEEtLTQLEQLK 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958661053 1222 QKLEKEKSEMKMeiddlasnveTVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLiNDLTTQRGRLQTESGEFSRQLDEK 1301
Cdd:PRK10246 787 QNLENQRQQAQT----------LVTQTAQALAQHQQHRPDGLDLTVTVEQIQQEL-AQLAQQLRENTTRQGEIRQQLKQD 855
|
490 500
....*....|....*....|....*..
gi 1958661053 1302 EALVSQLsrgkQAFTQQIEELKRQLEE 1328
Cdd:PRK10246 856 ADNRQQQ----QALMQQIAQATQQVED 878
|
|
| |
