|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-767 |
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: 1447.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 579
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 98986453 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14913 641 KKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-767 |
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: 1326.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK-KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEWTFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvvKGRAEAHF 578
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFQTVSALFRENLNK 658
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASL---FKDYEESGGGGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 659 LMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFiD 738
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 98986453 739 SKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01377 634 GKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-767 |
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: 1219.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 579
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 98986453 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-767 |
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: 1199.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKD-SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 338
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 499 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHF 578
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--DSGKKKVAKKKGSSFQTVSALFRENL 656
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgdSGGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 98986453 737 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-767 |
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: 1193.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 337
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 577
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 578 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATAD---ADSGKKKVAKKKGSSFQTVSALFRE 654
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEgasAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 655 NLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEG 734
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 98986453 735 QFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-767 |
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: 1189.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 337
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 577
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 578 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADS-GKKKVAKKKGSSFQTVSALFRENL 656
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 98986453 737 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-767 |
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: 1186.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDS--KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAAsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 337
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAH 577
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 578 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD-SGKKKVAKKKGSSFQTVSALFRENL 656
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 98986453 737 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-767 |
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: 1164.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDLAKKKD----SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 256
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGPGKKAqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 257 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 336
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 575
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKyE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 576 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADS---GKKKVAKKKGSSFQTVSALF 652
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEdpkSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 653 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 732
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 98986453 733 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-767 |
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: 1156.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 579
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 98986453 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14917 641 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-767 |
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: 1143.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAnKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 338
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 499 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHF 578
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA-DSGKKKVAKKKGSSFQTVSALFRENLN 657
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 658 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 737
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 98986453 738 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-767 |
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: 1044.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL-----GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 579
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 98986453 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14929 635 RKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-767 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1030.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 88 IEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 248 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQ-GEILVASIDD 326
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 327 AEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVK 406
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 407 VGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEK 485
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 486 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNF 564
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 565 QKPKVvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATAD----ADSGKKKVAKK 640
Cdd:pfam00063 472 QKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAEsaaaNESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 641 KGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 720
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 98986453 721 QRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:pfam00063 629 QRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-767 |
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: 994.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 340
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 420
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 421 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 500
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 501 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGR-AEAHFS 579
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAdsgkkKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDS 739
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDN 631
|
650 660
....*....|....*....|....*...
gi 98986453 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14934 632 KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-779 |
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: 989.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 81 NPPKFDRIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRND 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS--------NTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 241 NSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQG-EI 319
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 320 LVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKTAYLMGLNSSDLLK 398
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 399 ALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLC 478
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 479 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQH 557
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 558 LGKSNNFQKPKVvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfatadadsGKKKV 637
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF----------PSGVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 638 AKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYG 717
Cdd:smart00242 537 NAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 718 DFKQRYRVLNASAIPEGQFiDSKKACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRD 779
Cdd:smart00242 617 EFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-767 |
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 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASK--KTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVK-GRAEAHF 578
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKV-AKKKGSSFQTVSALFRENLN 657
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGgRGKKGGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 658 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQfi 737
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 98986453 738 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14909 637 DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-767 |
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: 837.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATIAATGdlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSG---SSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIE---LLLITTNPYDYPFISQGEIL-VASIDDAEELLATD 334
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREelkLELLLSYYYLNDYLNSSGCDrIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 335 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 412
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 413 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 490
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 491 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKV 569
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 570 VKGraeaHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSnrllahlyatfatadadsgkkkvakkkgssfqtvs 649
Cdd:cd00124 477 AKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 650 aLFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 729
Cdd:cd00124 518 -QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 98986453 730 AiPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd00124 597 A-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
31-1112 |
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 98986453 31 PFDAKTYCFVVDSKEEYAKGKIKSsqdgkvTVETEDNRTLVVKPEDV--YAMNPPKFDRIEDMAMLTHLNEPAVLYNLKD 108
Cdd:COG5022 15 PDEEKGWIWAEIIKEAFNKGKVTE------EGKKEDGESVSVKKKVLgnDRIKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 109 RYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVN 188
Cdd:COG5022 89 RYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 189 TKRVIQYFATIAATgdlakkkDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYL 268
Cdd:COG5022 169 AKRIMQYLASVTSS-------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 269 LEKSRVTFQLKAERSYHIFYQILSNKkPELIELLLITTNPYDYPFISQGE-ILVASIDDAEELLATDSAIDILGFTPEEK 347
Cdd:COG5022 242 LEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 348 SGLYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNA 427
Cdd:COG5022 321 DQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 428 LSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI 507
Cdd:COG5022 400 LAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 508 EWTFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSNNFQKPKVvkgrAEAHFSLIHYA 584
Cdd:COG5022 480 EWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRF----RDNKFVVKHYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 585 GTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfatadadsgKKKVAKKKGSSFQTVSALFRENLNKLMSNLR 664
Cdd:COG5022 555 GDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF-----------DDEENIESKGRFPTLGSRFKESLNSLMSTLN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 665 TTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI---DSKK 741
Cdd:COG5022 624 STQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKN 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 742 ACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDDRLAKLITRTQAVCRGFLMRVEFQKMVQRRESIFCIQYNIRS 821
Cdd:COG5022 704 AVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 822 FMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELaKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLD 901
Cdd:COG5022 784 RRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFS 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 902 AEERCDQLIKAKFQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDIDDLELtlakvekekhateNKVKNLTE 981
Cdd:COG5022 863 LLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSSDLI-------------ENLEFKTE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 982 ELSGLDETIAKLTREKKALQEAHQQalddlqaeeDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLK 1061
Cdd:COG5022 929 LIARLKKLLNNIDLEEGPSIEYVKL---------PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1062 LAQEsILDLENDKQQLDERLKKKDFEYCQLQS--KVEDEQTLGLQFQKKIKEL 1112
Cdd:COG5022 1000 ELAE-LSKQYGALQESTKQLKELPVEVAELQSasKIISSESTELSILKPLQKL 1051
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-767 |
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: 814.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAAT---GDLAKKKDSK----MKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 254 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILVASIDDAEELLAT 333
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 334 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 413 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 491
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 492 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksnnfQKPKVVK 571
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 572 G--RAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADADSGKKKVAkkk 641
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaeivgmAQQALTDTQFGARTRK--- 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 642 gSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 721
Cdd:cd14911 551 -GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 98986453 722 RYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14911 630 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-767 |
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: 784.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHK--GRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGra 574
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD-- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 575 EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSS--------FQ 646
Cdd:cd14920 474 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSayktkkgmFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 647 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 98986453 727 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14920 634 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-767 |
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: 722.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM--KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSAI 337
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYSKYR--FLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 496 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKG 572
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 573 raEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF----------ATADADSGKKKVAKkkg 642
Cdd:cd14932 478 --DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkvaGMGESLHGAFKTRK--- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 643 SSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQR 722
Cdd:cd14932 553 GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 98986453 723 YRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14932 633 YEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-767 |
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: 705.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHK--GKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPyDYPFISQGEILVASIDDAEELLATDSAIDIL 340
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 499 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAE 575
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 576 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF--------ATADADSGKKKVAKKKGSSFQT 647
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 648 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 727
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 98986453 728 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14921 635 ANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-767 |
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: 692.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATIAATgdlakkkDSKMKGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGS-------SSGETQV-EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNK-KPELIELLLitTNPYDYPFISQGE-ILVASIDDAEELLATDSA 336
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLP--RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 495 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNN-FQKPKVVKGR 573
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 574 aeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLlahlyatfatadadsgkkkvakkkgssfQTVSALFR 653
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------KTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAipE 733
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 98986453 734 GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01380 596 WLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-767 |
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: 678.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 574
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 575 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF--------ATADADSGKKKVAKKKGSSFQ 646
Cdd:cd14919 473 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 647 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 98986453 727 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14919 631 TPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-767 |
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: 677.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPK--GRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEilVASIDDAEELLA-TDSAIDI 339
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP--SSSPGQERELFQeTLESLRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14930 237 LGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVkgR 573
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHL--R 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 574 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF----------ATADADSGKKKVAkkkgS 643
Cdd:cd14930 472 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegivgleqvsSLGDGPPGGRPRR----G 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 644 SFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRY 723
Cdd:cd14930 548 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 98986453 724 RVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14930 628 EILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-767 |
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: 677.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM--KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEILVASIDDAEELLATDSAID 338
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGra 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPKKLKD-- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 575 EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYA---TFATADADSGKKKVA---KKKGSSFQTV 648
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvdRIVGLDKVSGMSEMPgafKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 649 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 728
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 98986453 729 SAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-767 |
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: 645.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDlakkkdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGSS-----------GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEIL-VASIDDAEELLATDSAID 338
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNCLtIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDT-KLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 498 EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFqkpkvvKGRAEA 576
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 577 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQkSSNRLLAHLYAT-FATADADSGKKKVAKKKGSSFQTVSALFREN 655
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLS-SCSCQLPQLFASkMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 656 LNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQ 735
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ 617
|
650 660 670
....*....|....*....|....*....|..
gi 98986453 736 FIDSkkACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01383 618 DPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-767 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 630.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIaatgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI-----------SGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEILVAS-IDDAEELLATDSAIDI 339
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF---IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 495 FVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPkvvKGR 573
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP---KSD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 574 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKvakkkgssfQTVSALFR 653
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS---------PTLSSQFR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLnASAIPE 733
Cdd:cd01381 536 KSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGIPP 614
|
650 660 670
....*....|....*....|....*....|....
gi 98986453 734 GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01381 615 AHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-767 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 623.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDlakKKDSKMKgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSE---SEVERVK----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 340
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY---VTKGQT 417
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQ-HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHhmFV 496
Cdd:cd01378 314 VEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 L--EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSNNFQKPKVVKG 572
Cdd:cd01378 392 LkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 573 RAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatFATADADSGKKKVakkkgssfqTVSALF 652
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF--PEGVDLDSKKRPP---------TAGTKF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 653 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 732
Cdd:cd01378 539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWP 618
|
650 660 670
....*....|....*....|....*....|....*
gi 98986453 733 EGQFIDsKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01378 619 AWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-767 |
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: 607.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFAtiAATGdlakkKDSKmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTN-----NHSW----VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKK--PELIELLLItTNPYDYPFISQ-GEILVASIDDAEELLATDSAI 337
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14883 310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 LEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKvvKGRAE 575
Cdd:cd14883 390 LEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 576 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-----ATFATADADSGKKKVAKKKGSSFQTVSA 650
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdlLALTGLSISLGGDTTSRGTSKGKPTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 651 LFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASA 730
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*..
gi 98986453 731 IPEGQFIDsKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14883 626 RSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-767 |
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: 601.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFAtiaatgDLAKKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA------YMGGRAVTEGR-SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGE-ILVASIDDAEELLATDSAI 337
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADK--------TAYLMGLNSSDLLKALCFPRVKVGN 409
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVTPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 410 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 489
Cdd:cd01384 308 GIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 490 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQKPK 568
Cdd:cd01384 388 FNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 569 vvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSgkkkvakkkGSSFQTV 648
Cdd:cd01384 466 ----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSS---------SSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 649 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLnA 728
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL-A 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 98986453 729 SAIPEGQFiDSKKACEKLLASIDIDhtQYKFGHTKVFFK 767
Cdd:cd01384 612 PEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-767 |
3.80e-173 |
|
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: 542.06 E-value: 3.80e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATIAatGDLakkKDSKMKgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--GGL---NDSTIK-----KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFiSQGEILVASIDDAEELLATDSAID 338
Cdd:cd14903 151 LVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14903 229 LIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14903 309 KKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKgraeA 576
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR----T 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 577 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY---ATFATADADSGKKKVAKKKGSSF--QTVSAL 651
Cdd:cd14903 464 QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkekVESPAAASTSLARGARRRRGGALttTTVGTQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 652 FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAi 731
Cdd:cd14903 544 FKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG- 622
|
650 660 670
....*....|....*....|....*....|....*..
gi 98986453 732 pEGQFIDSKKACEKLLASIDIDH-TQYKFGHTKVFFK 767
Cdd:cd14903 623 -RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-767 |
1.97e-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: 534.52 E-value: 1.97e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 103 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 182 GAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGA----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLittnpydypfisqgeiLVASIDDAEELLATDSAIDILG 341
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 342 FTPEEKSGLYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------TAYLMGLNSSDLLKALCfPRVKVGNEYV 412
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLT-TRVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 413 TKGQ------TVDQVHHAVNALSKSVYEKLFLWMVTRINQQldtkLPRQ---HFIGVLDIAGFEIFEYNSLEQLCINFTN 483
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQC----IPFEtssYFIGVLDIAGFEYFEVNSFEQFCINYCN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 484 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksN 562
Cdd:cd01382 368 EKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---N 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 563 NFQKPKVVKGRAEAH--------FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGK 634
Cdd:cd01382 444 HFRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 635 KKVAKkkgsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRI 714
Cdd:cd01382 524 KAGKL----SFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 98986453 715 LYGDFKQRYRVLNASAIPEgqfIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-767 |
3.10e-169 |
|
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: 530.89 E-value: 3.10e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATgdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS-----------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSnkKPELIELLLITTNPyDYPFISQGEIL-VASIDDAEELLATDSAID 338
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGCIeVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKTAYLMGLNSSDLLKALCFPRVKVgneyvtKG 415
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEI------KG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 416 Q-------TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQ 487
Cdd:cd14872 301 CdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 488 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnnFQK 566
Cdd:cd14872 381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 567 PKVVKGRaEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSgkkkvakkkGSSFQ 646
Cdd:cd14872 458 YAEVRTS-RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL---FPPSEGDQ---------KTSKV 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 647 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14872 525 TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 98986453 727 NaSAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14872 605 V-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-767 |
1.41e-168 |
|
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: 530.12 E-value: 1.41e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 176 LITGESGAGKTVNTKRVIQYFATIAA--------TGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 247
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSgfaqgasgEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 248 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEILVASIDDA 327
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 328 EELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKTAYLMGLNSSDLLKALCFPRVK 406
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 407 VGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKL 486
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYDQHLGK 560
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 561 SN------------NFQKPKVVKGRaeaHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLlahlyatfata 628
Cdd:cd14890 479 SGsggtrrgssqhpHFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI----------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 629 dadsgkkkvakkKGSSfqtVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRK 708
Cdd:cd14890 545 ------------REVS---VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQ 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 709 GFPNRILYGDFKQRYRVLNASAipegqfiDSKKACEKLLASI-DIDHTQYKFGHTKVFFK 767
Cdd:cd14890 610 GFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-767 |
5.09e-166 |
|
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: 522.78 E-value: 5.09e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKLA 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRN----------NLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQIL---SNKKPELIELLlittNPYDYPFISQG-EILVASIDDAEELLATDSA 336
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLaglPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLLAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADK-----TAYLMGLNSSDLLKALCFPRVKVGNEY 411
Cdd:cd01387 227 MQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDaeiqwVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 412 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 491
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 492 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVv 570
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRM- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 571 kGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAtadADSGKKKVAKKKGSSFQ---- 646
Cdd:cd01387 462 -PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR---AQTDKAPPRLGKGRFVTmkpr 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 647 --TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd01387 536 tpTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 98986453 725 VLNASAIPEGQFIDSKKACEKLLASIDIDhTQYKFGHTKVFFK 767
Cdd:cd01387 616 CLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-767 |
3.50e-164 |
|
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: 518.85 E-value: 3.50e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 103 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 183 AGKTVNTKRVIQYFATIAatgdlakkkdskMKGT---LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01385 84 SGKTESTNFLLHHLTALS------------QKGYgsgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITtnPYDYPFISQGEILVA-SIDDAEELLATDSAI 337
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGaSEEERKELHLKQ--PEDYHYLNQSDCYTLeGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 415
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 416 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL----DTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 491
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 492 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYDQHLGKSNNFQKPKVV 570
Cdd:cd01385 390 QHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 571 kgraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLL--------------AHLYATFATADA--DSGK 634
Cdd:cd01385 468 ----EPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwAVLRAFFRAMAAfrEAGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 635 KKVAKKKGSSF-------------------QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLR 695
Cdd:cd01385 544 RRAQRTAGHSLtlhdrttksllhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 696 CNGVLEGIRICRKGFPNRILYGDFKQRYRVLnasaIPEGQfIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-767 |
7.32e-164 |
|
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: 516.06 E-value: 7.32e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFAtiaatgDLAKKKDskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01379 81 ESGAGKTESANLLVQQLT------VLGKANN----RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQIL----SNKKpeLIELLLITTNPYDYPFISQGEILVASIDDA--EELLAT 333
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 334 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGN 409
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 410 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--DTKLP-RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKL 486
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKS 561
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 562 NNFQKPKvvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAhlyatfatadadsgkkkvakkk 641
Cdd:cd01379 462 KYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 642 gssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 721
Cdd:cd01379 516 ----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLK 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 98986453 722 RYRVL--NASAIPEGqfidSKKACEKLLASIDIDHtqYKFGHTKVFFK 767
Cdd:cd01379 592 RYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-767 |
1.08e-163 |
|
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: 516.94 E-value: 1.08e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATiaatgdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF----- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-------AGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 254 ----GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTN-----------PYDYPFISQGE 318
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENdeklakgadakPISIDMSSFEP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 319 ILV------------ASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVAD 383
Cdd:cd14888 233 HLKfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 384 KTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLD 462
Cdd:cd14888 313 KVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 463 IAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMF 541
Cdd:cd14888 393 IFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 542 PKATDTSFKNKLYDQHLGkSNNFqkpKVVKGRAEAhFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKG-HKRF---DVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 622 YATFATADADSGKKKVAkkkgssFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLE 701
Cdd:cd14888 547 FSAYLRRGTDGNTKKKK------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQ 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 702 GIRICRKGFPNRILYGDFKQRYRVLnasAIPEGQfidskkacekllasidIDHTQYKFGHTKVFFK 767
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-765 |
9.27e-162 |
|
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: 511.26 E-value: 9.27e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 172 --NQSILITGESGAGKTVNTKRVIQYFAtiAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 250 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKP-ELIELLLITTNPYDYPFISQGEILVASIDDAE 328
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 329 ELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEV-ADKTAYLMGLNSSDLLKALCFPRVKV 407
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 408 GNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLP--RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEK 485
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 486 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNF 564
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 565 QKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAhlyatfatadadsgkkkvakkkgss 644
Cdd:cd14901 477 SVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 645 fQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd14901 530 -STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 98986453 725 VLNAS------AIPEGQFIDSKKACEKLLASIDIDHTQykFGHTKVF 765
Cdd:cd14901 609 CLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-767 |
9.44e-158 |
|
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: 500.06 E-value: 9.44e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 106 LKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNpevVEGYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----ENQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 176 LITGESGAGKTVNTKRVIQYFATI--AATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATAskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 254 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPyDYPFISQGEIL-VASIDDAEELLA 332
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNCVeVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 333 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KTAYLMGLNSSDLLKALCFpRVKVGne 410
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 411 yvTKGQ------TVDQVHHAVNALSKSVYEKLFLWMVTRIN----QQL------DTKLPRQHFIGVLDIAGFEIFEYNSL 474
Cdd:cd14892 320 --ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 475 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 552
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 553 LYDQHLGKSNNFQKPkvvkgRAEA-HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNrllahlyatfatadad 631
Cdd:cd14892 477 YHQTHLDKHPHYAKP-----RFECdEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK---------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 632 sgkkkvakkkgssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFP 711
Cdd:cd14892 536 --------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFP 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 712 NRILYGDFKQRYRVL-------NASAIPEGQFIDSKKACEKLLASIDIDHTQykFGHTKVFFK 767
Cdd:cd14892 596 IRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-767 |
1.82e-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: 496.62 E-value: 1.82e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQS--LELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQ-GEILVASIDDAEELLATDSAID 338
Cdd:cd14873 160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITAME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADKTAY-----LMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd14873 239 VMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 414 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 493
Cdd:cd14873 311 TPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 494 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgkSNN--FQKPKVvk 571
Cdd:cd14873 390 IFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPRV-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 572 grAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSnrlLAHLYATFATADADSGKKKVAKKKGSSFQTVSAL 651
Cdd:cd14873 464 --AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESR---FDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 652 FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL-NASA 730
Cdd:cd14873 539 FKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNLA 618
|
650 660 670
....*....|....*....|....*....|....*..
gi 98986453 731 IPEgqfiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14873 619 LPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1924 |
1.31e-155 |
|
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: 508.56 E-value: 1.31e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER 926
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 927 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQ 1006
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1007 ALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDF 1086
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1087 EYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNK 1166
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1167 KREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANL 1246
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1247 EKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKA 1326
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1327 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDSEEQVE 1406
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1407 AVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKC-----EESQAELEASLKESRSLSte 1481
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISaryaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1482 lfkLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILR 1561
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1562 IQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETL 1641
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1642 KHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQN 1721
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1722 TSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1801
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1802 EQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKR 1881
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 98986453 1882 QAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-767 |
6.18e-147 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 469.56 E-value: 6.18e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLSPSDD----------SDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEILVASIDDAEEL----LATDSA 336
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 337 IDIL---GFTPEEKSGLYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADKT-----AYLMGLNSSDLLKALCFPRVKVG 408
Cdd:cd14897 232 TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEYplhavAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 409 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF-----IGVLDIAGFEIFEYNSLEQLCINFTN 483
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 484 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDqHLGKSN 562
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 563 NFQKPKvvKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFatadadsgkkkvakkkg 642
Cdd:cd14897 465 RYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 643 ssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQR 722
Cdd:cd14897 524 ---------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 98986453 723 YRVLNASaiPEGQFIDSKKACEKLLASIDIDhtQYKFGHTKVFFK 767
Cdd:cd14897 595 YKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-753 |
2.25e-146 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 467.86 E-value: 2.25e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 246 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILsnkkpelielllittnpydypfisqgeilvasID 325
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA--------------------------------IG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 326 DAEELLATD------SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKTAYLMGLN 392
Cdd:cd14900 211 ASEAARKRDmyrrvmDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 393 SSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-----DTKLPRQHFIGVLDIAGFE 467
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 468 IFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATD 546
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 547 TSFKNKLYdQHLGKSNNFQKPKVVKGRaeAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNrllahlyatfa 626
Cdd:cd14900 450 TTLASKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ----------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 627 tadadsgkkkvakkkgssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIC 706
Cdd:cd14900 516 -------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 98986453 707 RKGFPNRILYGDFKQRYRVLNASAIPegqfidsKKACEKLLASIDID 753
Cdd:cd14900 571 RAGFPIRLLHDEFVARYFSLARAKNR-------LLAKKQGTSLPDTD 610
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-767 |
6.41e-143 |
|
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: 459.41 E-value: 6.41e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATIAAtgdlaKKKDSKMkgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----GRKDKTI-----AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAI 337
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR-QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSNNFQKPKVVKgra 574
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 575 eAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKG-SSFQTVSALFR 653
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTEL---FGSSEAPSETKEGKSGKGtKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 733
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|....*
gi 98986453 734 GqfiDSKKACEKLLASIDIDHT-QYKFGHTKVFFK 767
Cdd:cd14904 622 K---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-767 |
1.15e-141 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 456.41 E-value: 1.15e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 173 QSILITGESGAGKTVNTKRVIQYFATIAA---------TGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSS 243
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevlTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 244 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYP--FISQGEIL 320
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRydYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 321 -VASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLL 397
Cdd:cd14907 243 eVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 398 KALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--------DTKLPRQHFIGVLDIAGFEIF 469
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 470 EYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 546
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 547 TSFKNKLYDQHlgksNNFQKPKVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfa 626
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF---- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 627 TADADSGKKKVAKKKGSSFQ--TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIR 704
Cdd:cd14907 554 SGEDGSQQQNQSKQKKSQKKdkFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 705 ICRKGFPNRILYGDFKQRYRVLNasaipegqfidskkacekllasididhTQYKFGHTKVFFK 767
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-767 |
8.44e-140 |
|
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: 450.90 E-value: 8.44e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 178 TGESGAGKTVNTKRVIQYFATIAatgdlakkkdsKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-----------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQI---LSNKKPELIELLlittNPYDYPFISQGeilvASIDDAEELLATD 334
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNG----AGCKREVQYWKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 335 -----SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVG 408
Cdd:cd14889 223 ydevcNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 409 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLdtkLPRQHF------IGVLDIAGFEIFEYNSLEQLCINFT 482
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIEL-IEKPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKS 561
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 562 NNFqkpKVVKGRAEAhFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKK 641
Cdd:cd14889 458 SYY---GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQA 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 642 GSSF------QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRIL 715
Cdd:cd14889 534 GSDNfnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPS 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 716 YGDFKQRYRVLnasaIPEGQFIDSKKACEKLLASIDIdhTQYKFGHTKVFFK 767
Cdd:cd14889 614 FAEFAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-826 |
2.25e-138 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 452.56 E-value: 2.25e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 62 VETEDNRTLVVKPEDVYAMNPP-KFDRIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVV 140
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 141 EGYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiAATGDlakkkdskMKGTLED 219
Cdd:PTZ00014 151 RRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGN--------MDLKIQN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 220 QIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELI 299
Cdd:PTZ00014 222 AIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 300 ELLLItTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE---- 375
Cdd:PTZ00014 302 EKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaai 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 376 -PDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR 454
Cdd:PTZ00014 381 sDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 455 QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKP 528
Cdd:PTZ00014 461 KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKG 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 529 MGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVG 608
Cdd:PTZ00014 535 KSVLSILEDQCLAPGGTDEKFVSSCNTNL--KNNPKYKPAKVDSNKN--FVIKHTIGDIQYCASGFLFKNKDVLRPELVE 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 609 LYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFQtvsalfrENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHS 688
Cdd:PTZ00014 611 VVKASPNPLVRDL---FEGVEVEKGKLAKGQLIGSQFL-------NQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSS 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 689 LVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAsAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFKA 768
Cdd:PTZ00014 681 KVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKK 759
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 769 GLLGTLEEMRDDRLAK---LITRTQAVCRGFLMRVEFQKMVQrreSIFCIQYNIRSFMNVK 826
Cdd:PTZ00014 760 DAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKNIK---SLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-767 |
4.19e-134 |
|
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: 435.88 E-value: 4.19e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 170 RENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 249 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIL---SNKKPELIELLLITTN----PYDYPFISQGEIL- 320
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggDEEEHEKYEFHDGITGglqlPNEFHYTGQGGAPd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 321 VASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKTAYLMGLNSSDLL 397
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 398 KALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--DTKLPRQHFIGVLDIAGFEIFEYNSLE 475
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKL 553
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 554 YDQHLGKSNN-------FQKPKVVKGRaeAHFSLIHYAGTVDYSV-SGWLEKNKDPLNETVVGLYQKSSNrllahlyatf 625
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ---------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 626 atadadsgkkkvakkkgssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRI 705
Cdd:cd14908 548 --------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 706 CRKGFPNRILYGDFKQRYRVLnASAIPE-----------GQFIDSKKACEKLLASI---------DIDHTQYKFGHTKVF 765
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldPQKLCVKKMCKDLVKGVlspamvsmkNIPEDTMQLGKSKVF 680
|
..
gi 98986453 766 FK 767
Cdd:cd14908 681 MR 682
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-767 |
8.03e-132 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 427.92 E-value: 8.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRY--TSWMIYTYSGLFCVTVNPYKWLPvyNPEVvEGYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSklDNQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 175 ILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKG--------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 246
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSkkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 247 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQ-GEILVASI 324
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 325 DDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKAL 400
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 401 CFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFE-YNSLEQLCI 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 558
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 559 GKSNNFQKPKvvkgRAEAHFSLI--HYAGTVDYSVSGWLEKNKDplnetvvglyqkssnRLLAHLYATFATadadsgkkk 636
Cdd:cd14891 475 KRHPCFPRPH----PKDMREMFIvkHYAGTVSYTIGSFIDKNND---------------IIPEDFEDLLAS--------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 637 vakkkgssfqtvSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILY 716
Cdd:cd14891 527 ------------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 717 GDFKQRYRVLNASAI------PEGQFIdskkacEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14891 595 AELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-723 |
5.54e-129 |
|
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: 422.76 E-value: 5.54e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP---------VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 170 RENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-EIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 250 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILVA-----SI 324
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQ-KGGKYELLNSYGPSFArkravAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 325 DDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKTAYLMGLNSSDLL 397
Cdd:cd14902 239 KYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDKLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 398 KALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF---------IGVLDIAGFEI 468
Cdd:cd14902 315 TLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFES 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 469 FEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDT 547
Cdd:cd14902 395 LNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 548 SFKNKLYDQHLGksnnfqkpkvvkgraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT 627
Cdd:cd14902 474 ALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 628 ADADSGKKKVAKKKGSSFQT--VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRI 705
Cdd:cd14902 539 DSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650
....*....|....*...
gi 98986453 706 CRKGFPNRILYGDFKQRY 723
Cdd:cd14902 619 ARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-767 |
1.31e-125 |
|
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: 410.53 E-value: 1.31e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATiaatgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS---------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEILVASIDDAEELLATDSAID 338
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLESLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd14876 231 SMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 414 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 493
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 494 MFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKP 567
Cdd:cd14876 391 VFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKL--KSNGKFKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 568 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFQT 647
Cdd:cd14876 463 AKVDSNIN--FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKAL---FEGVVVEKGKIAKGSLIGSQFLK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 648 vsalfreNLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 727
Cdd:cd14876 538 -------QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 98986453 728 AsAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14876 611 L-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-767 |
4.36e-124 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 408.19 E-value: 4.36e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNpevVEGYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 170 RENQSILITGESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTT-ATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 250 RIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPE-LIELLLITTNPYDYPFISQGEILVAS 323
Cdd:cd14895 157 RMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQRN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 324 --IDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------------D 383
Cdd:cd14895 237 dgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 384 KTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQ---QLDTKLPRQH---- 456
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSaspQRQFALNPNKaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 457 ----FIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGI 531
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 532 FSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKvvKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQ 611
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 612 KSSNRLLAHLYATF-ATADADSGKKKVAKKKGSSFQT---VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEH 687
Cdd:cd14895 553 KTSDAHLRELFEFFkASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 688 SLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPegqfidSKKACEKLLASIDIDHTQykFGHTKVFFK 767
Cdd:cd14895 633 AKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-767 |
8.94e-120 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 393.76 E-value: 8.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATiaatgdLAKKKDSKMKGTLEDQIisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKL 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSS------LYQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEIL-VASIDDAEELLATDSAID 338
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGACrLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVadKTAYLMGLNSSDLLKALCFPRVKVGN-EYVTK 414
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEI--HTAARLLQVPPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 415 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF--IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNH 492
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 493 HMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVvk 571
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 572 grAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFQtvsal 651
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSL---FQEAEPQYGLGQGKPTLASRFQ----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 652 frENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAI 731
Cdd:cd14896 533 --QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*..
gi 98986453 732 PEgqfIDSKKACEKLLASIDIDHTQ-YKFGHTKVFFK 767
Cdd:cd14896 611 EA---LSDRERCGAILSQVLGAESPlYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-726 |
8.81e-114 |
|
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: 377.27 E-value: 8.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 178 TGESGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS--PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYpfisqgeiLVASIDDAEE--LLATD 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHLPEGAAFSW--------LPNPERNLEEdcFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 335 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 411
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 412 VT--KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR-QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQ 488
Cdd:cd14880 313 QVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 489 FFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 567
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 568 KVVKgraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFQT 647
Cdd:cd14880 472 KLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKL---FPANPEEKTQEEPSGQSRAPVLT 545
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 648 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14880 546 VVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-724 |
9.81e-114 |
|
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: 379.05 E-value: 9.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 170 RENQSILITGESGAGKTVNTKRVIQYFA-------TIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNS 242
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 243 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNK----KPELIELLLITTNPYDYPFISQG 317
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 318 --EILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 383
Cdd:cd14899 242 lcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 384 KTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--------------- 448
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 449 DTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-K 527
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 528 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVV 607
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 608 GLYQKSSNRLLAHLYATFATADAD--------SGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNET 679
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANgdseldgfGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 98986453 680 KTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-729 |
2.83e-113 |
|
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: 377.78 E-value: 2.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTGK 258
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 259 LASADIETYLLEKSRVTFQL-KAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASI------------- 324
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 325 --DDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKTAYLMGLNSSDLLKA 399
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 400 LCFPRVKVGNE--YVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQH-----------FIGVLDIAGF 466
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDlaggsnkknnlFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 467 EIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKAT 545
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 546 DTSFKNKlYDQHLGKSNNFQKPKVVKGRaeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF 625
Cdd:cd14906 482 EQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 626 ATADADSGKKKvakkkgSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRI 705
Cdd:cd14906 557 ITSTTNTTKKQ------TQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKV 630
|
650 660
....*....|....*....|....
gi 98986453 706 CRKGFPNRILYGDFKQRYRVLNAS 729
Cdd:cd14906 631 RKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-767 |
1.04e-109 |
|
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: 365.36 E-value: 1.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 106 LKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSS----------TDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVA-SIDDAEELLATDSAID 338
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 339 ILgFTPEEKSGLYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 415
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 416 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 496 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyDQHLgKSNNFQKPKvvkgRA 574
Cdd:cd14886 395 KSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFIPGK----GS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 575 EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHlyaTFATADADSGKKKVakkkgssfQTVSALFRE 654
Cdd:cd14886 468 QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNK---AFSDIPNEDGNMKG--------KFLGSTFQL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 655 NLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL---NASAI 731
Cdd:cd14886 537 SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQ 616
|
650 660 670
....*....|....*....|....*....|....*.
gi 98986453 732 PEGQfiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14886 617 NAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-767 |
7.61e-105 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 351.80 E-value: 7.61e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMI-YTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIHF- 253
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSYM-----HSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 254 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILV------ASIDDA 327
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 328 EELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQReeqaepDGTEVADKTAYLMGLNSSDLLKAL---CFpR 404
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN------DKAQIADETPFLTACRLLQLDPAKlreCF-L 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 405 VKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKL--PRQHFIGVLDIAGFEIFEYNSLEQLCINFT 482
Cdd:cd14875 311 VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKS 561
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 562 NNFQKPkvvKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSgkkkvakkk 641
Cdd:cd14875 470 PYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK--------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 642 gssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF-K 720
Cdd:cd14875 538 ----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 98986453 721 QRYRVLNASAIPEGQFIDSKKACEKLLAS----IDIDHTQYKFGHTKVFFK 767
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-767 |
5.47e-103 |
|
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: 346.99 E-value: 5.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 182 GAGKTVNTKRVIQYFATIAATGDLAKKKdskmkgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGVLSV---------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELI-ELLL--ITTNPYDY--PFISQGEilvaSIDDAEELLATDSA 336
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRtELHLnqLAESNSFGivPLQKPED----KQKAAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 337 IDILGFTPEEKSGLYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 414 KGQTVDQVHH------------AVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLE 475
Cdd:cd01386 307 TSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEECM 540
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 541 FPKATDTSFKNKLYdQHLGKSNNFQKPKVVKgRAEA--HFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQkSSN 615
Cdd:cd01386 467 YPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQ-ESQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 616 RLLAHLYATFATADAdsgkkkvakkkgsSFQtvsalfrenLNKLMSNLRTTHPHFVRCIIPN------ETKTPGA----- 684
Cdd:cd01386 544 KETAAVKRKSPCLQI-------------KFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPaagde 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 685 -MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL----NASAIPEGQFIDSKKACEKLLASIDIDHTQYKF 759
Cdd:cd01386 602 lLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKSSYRI 681
|
....*...
gi 98986453 760 GHTKVFFK 767
Cdd:cd01386 682 GLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-767 |
5.19e-95 |
|
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: 322.92 E-value: 5.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 178 TGESGAGKTVNTKRVIQYFATiaatgdlakkKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 K-LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFISQGE----ILVASIDDAEELLA 332
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 333 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 412
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 413 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRIN----QQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQ 488
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 489 FFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 567
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 568 KVVKGRAE-------AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAtfatadadsgkkkvakk 640
Cdd:cd14878 471 PMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ----------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 641 kgSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 720
Cdd:cd14878 534 --SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFL 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 98986453 721 QRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQykFGHTKVFFK 767
Cdd:cd14878 612 SRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQ--MGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-767 |
1.64e-92 |
|
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: 315.03 E-value: 1.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEvvegYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 182 GAGKTVNTKRVIQYFATiaatgdlAKKKDSKMKGTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd14937 79 GSGKTEASKLVIKYYLS-------GVKEDNEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPyDYPFISQGEILVASIDDAEELLATDSAIDILG 341
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 342 FTpEEKSGLYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14937 227 MH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 497 LEQEEYKKEGIEWTFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYDQHLGKSNNFQKPKVVKGRAEA 576
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 577 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKkkvakkkgssfQTVSALFRENL 656
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK-----------NLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIcRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 98986453 737 IDSKKACEKLLASIDIDhtQYKFGHTKVFFK 767
Cdd:cd14937 609 TDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-730 |
1.69e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 309.91 E-value: 1.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvynpEVVEGYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 176 LITGESGAGKTVNTKRVIQYFAtiaatgdlakkKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgt 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 256 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpelielLLITTNPYDYPFISQGEilVASIDDAEELLATDS 335
Cdd:cd14898 140 DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNK--ESIVQLSEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 336 AIDILGFTPEEKsgLYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 415
Cdd:cd14898 212 AMKSLGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 416 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlpRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14898 287 NTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 496 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYDQHLGKSNNFQKPKVVkgr 573
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINTKARDKIKVS--- 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 574 aeahfsliHYAGTVDYSVSGWLEKNKDPLNETVVGlyqkssNRLLahlyatfatadADSGkkkvakkkgsSFQTVSALFR 653
Cdd:cd14898 441 --------HYAGDVEYDLRDFLDKNREKGQLLIFK------NLLI-----------NDEG----------SKEDLVKYFK 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASA 730
Cdd:cd14898 486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-767 |
1.90e-89 |
|
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: 308.89 E-value: 1.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTS--------WMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 172 NQSILITGESGAGKTVNTKRVIQYfatIAATGDLAKKKDSKmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRHGADSQ---GLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 252 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtnpYDYPFISQGEILVAsiddaeell 331
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGDPESTDLRRITA--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 332 atdsAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---TAYLMGLNS------- 393
Cdd:cd14887 223 ----AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvtea 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 394 -----SDLLKALCFPRVKVGNEYV------------TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-------- 448
Cdd:cd14887 299 srkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpse 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 449 -----DTKLPRQ-HFIGVLDIAGFEIFE---YNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----DFG 515
Cdd:cd14887 379 sdsdeDTPSTTGtQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafPFS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 516 MDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SNNFQKPK 568
Cdd:cd14887 459 FPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 569 VVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNrllahlYATFATADADSGKKKVAkkkgSSFQTV 648
Cdd:cd14887 539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACST------YTRLVGSKKNSGVRAIS----SRRSTL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 649 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 728
Cdd:cd14887 609 SAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLP 688
|
730 740 750
....*....|....*....|....*....|....*....
gi 98986453 729 SAIPEgqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14887 689 MALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
97-766 |
2.20e-86 |
|
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: 297.54 E-value: 2.20e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 97 LNEPAVLYNLKDRYTSWMIYTY---SGLfcVTVNPYKWLPVYNPEVVEGYR-------GKKRQEAPPHIFSISDNAYQFM 166
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 167 LTDRENQSILITGESGAGKTVNTKRVIQYFATIAAtgdlAKKKDSKmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFG 246
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSS----HSKKGTK----LSSQISAAEFVLDSFGNAKTLTNPNASRFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 247 KFIRIHFGTTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQG---EILVA 322
Cdd:cd14879 151 RYTELQFNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchpLPLGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 323 SIDDAE--ELLATdsAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLLK 398
Cdd:cd14879 230 GSDDAEgfQELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 399 ALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-DTKLPRQHFIGVLDIAGFEIF---EYNSL 474
Cdd:cd14879 308 SLTYKTKLVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRsstGGNSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 475 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFKNK 552
Cdd:cd14879 388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLEA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 553 LyDQHLGKSNNF-QKPKVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVglyqkssnRLLahlyatfatadad 631
Cdd:cd14879 467 L-RKRFGNHSSFiAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV--------NLL------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 632 sgkkkvakkkGSSFQtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFP 711
Cdd:cd14879 525 ----------RGATQ-----LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYV 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 712 NRILYGDFKQRYrvlnasaIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFF 766
Cdd:cd14879 590 VSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-715 |
9.49e-75 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 264.46 E-value: 9.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 172 NQSILITGESGAGKTVNTKRVIQYFATIaatgdlakKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI--------QTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 252 HFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGE---- 318
Cdd:cd14884 152 IFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 319 --------ILVASIDDAEELLATDSA-----IDILGFTPEEK---SGLYKLTGAVMHYGNMKFKQkqreeqaepdgteva 382
Cdd:cd14884 232 rsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDErqiNEFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 383 dkTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRIN----------QQLDTKL 452
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekdESDNEDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 453 PR--QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDfgmdLAACIELIEKPMG 530
Cdd:cd14884 375 YSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 531 IFSILEEECMFP----KATDTSFKNKLYD----QHLGKSNNFQK--PKVVKGRAEAH------FSLIHYAGTVDYSVSGW 594
Cdd:cd14884 451 IFRRLDDITKLKnqgqKKTDDHFFRYLLNnerqQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 595 LEKNKDPLNETVVGLYQKSSNRLLAHlyatfATADADSGkkkvakkkgsSFQTVSALFRENLNKLMSNLRTTHPHFVRCI 674
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFLRE-----ANNGGNKG----------NFLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 98986453 675 IPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRIL 715
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-749 |
3.23e-72 |
|
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: 255.42 E-value: 3.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPvyNPEVVEGYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 181 SGAGKTVNTKRVIQYFATIAATG---DLAKkkdskmkgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 257
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGGpetDAFK------------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKP-ELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 336
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 337 IDILG--FTpeeksGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 414
Cdd:cd14881 224 LGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 415 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQqldtkLPRQH----------FIGVLDIAGFEIFEYNSLEQLCINFTNE 484
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANS-----LKRLGstlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 485 KLQQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYDQHlgKSN 562
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--RQN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 563 N-FQKPKVVKGRAeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLlahlyaTFATADADsgkkkvakkk 641
Cdd:cd14881 449 PrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------GFATHTQD---------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 642 gssFQTvsalfreNLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 721
Cdd:cd14881 510 ---FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNA 579
|
650 660
....*....|....*....|....*...
gi 98986453 722 RYRVLnASAIPEGQFIDSKKACEKLLAS 749
Cdd:cd14881 580 RYRLL-APFRLLRRVEEKALEDCALILQ 606
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-719 |
1.28e-67 |
|
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: 243.08 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 106 LKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 185 KTVNTKRVIQYFATIaatgDLAKKKdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 264
Cdd:cd14905 85 KSENTKIIIQYLLTT----DLSRSK------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 265 ETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYpfISQ-GEILVASIDDAEELLATDSAIDILGF 342
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY--LNQgGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 343 TPEEKSGLYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKTAYlmglnsSDLLKALCFPRVKVGNEYVT-KGQTVDQV 421
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISdRSMPVNEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 422 HHAVNALSKSVYEKLFLWMVTRINQQLDtklPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14905 300 VENRDSLARSLYSALFHWIIDFLNSKLK---PTQysHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 500 EEYKKEGIEW-TFIDFgMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLydqhlgksNNFQKPKVVKGRAEAHF 578
Cdd:cd14905 377 REYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKPNKF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF----ATADADSGKKKVAKKKGSSFQTVSALFR- 653
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDGVFninaTVAELNQMFDAKNTAKKSPLSIVKVLLSc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 654 -----ENLNKLMSN-------------------LRTTHP-------------HFVRCIIPNETKTPGAMEHSLVLHQLRC 696
Cdd:cd14905 525 gsnnpNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKS 604
|
650 660
....*....|....*....|....*..
gi 98986453 697 NGVLEGIRICRKGFP----NRILYGDF 719
Cdd:cd14905 605 LCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-726 |
3.72e-66 |
|
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: 237.46 E-value: 3.72e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 180 ESGAGKTVNTKRVIQYfatiaatgdLAKKKDSKMKGTLEDQIISanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKY---------LTSQPKSKVTTKHSSAIES---VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILVASIDDAEELLATDSAIDI 339
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKT-----AYLMGLNSSDLLKALcFPRVKVGNEYvtk 414
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFL-LPKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 415 gqTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLpRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 494
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 495 FVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnNFQKPKv 569
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGKAR- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 570 VKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVs 649
Cdd:cd14874 446 NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVSQAQFILRGAQEIA- 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 650 alfrENLNKlmsnlrtTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14874 523 ----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-767 |
8.88e-65 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 233.86 E-value: 8.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 182 GAGKTVNTKRVIQYFATIAatgdlakkkdsKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYLG-----------DGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILS--NKKPELIELLLITTNPYDYPFISQG-------------EILVASIDD 326
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 327 AEELLAtdsaidILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVK 406
Cdd:cd14882 232 FEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 407 VGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLdtKLPR-----QHFIGVLDIAGFEIFEYNSLEQLCINF 481
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 482 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYDQHLGKS 561
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 562 NNFQKPkvvkgrAEAH-FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATadadsgkkkvakk 640
Cdd:cd14882 457 SQFVKK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 641 kgSSFQTVSALFR----ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILY 716
Cdd:cd14882 518 --RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 717 GDFKQRYRVLnasAIPEGQFID-SKKACEKLLasIDIDHTQYKFGHTKVFFK 767
Cdd:cd14882 596 QEFLRRYQFL---AFDFDETVEmTKDNCRLLL--IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-724 |
4.57e-63 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 231.01 E-value: 4.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 103 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 173 QSILITGESGAGKTVNTKRVIQYFATIAATGDLA--KKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 251 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKK--PELIELLLITTNPYDYPFISQGEILVASID-DA 327
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 328 EELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKTAYLMGLNSSDLLKALCF--- 402
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALKDPAQILLAAKLLeve 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 403 PRV------------KVGNEYVT--KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR---------QHFIG 459
Cdd:cd14893 324 PVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivinSQGVH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 460 VLDIAGFEIFE--YNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELIE-KPM 529
Cdd:cd14893 404 VLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEdKPF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 530 GIFSILEEECMFPKATDTSFKNKLY---DQHLGKSNNFQKPKVVKGRAEAH------FSLIHYAGTVDYSVSGWLEKNKD 600
Cdd:cd14893 484 GIFDLLTENCKVRLPNDEDFVNKLFsgnEAVGGLSRPNMGADTTNEYLAPSkdwrllFIVQHHCGKVTYNGKGLSSKNML 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 601 PLNETVVGLYQKSSNRLL-AHLYATFATADADSGKKKVAK--KKGSSFQTVSALFRENLN--------------KLMSNL 663
Cdd:cd14893 564 SISSTCAAIMQSSKNAVLhAVGAAQMAAASSEKAAKQTEErgSTSSKFRKSASSARESKNitdsaatdvynqadALLHAL 643
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 664 RTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd14893 644 NHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-251 |
5.15e-60 |
|
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: 203.73 E-value: 5.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 122 FCVTVNPYKWLPVYNPEVVEG-YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 201 ATGDLAKKKD-----SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 251
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 ... |
100-765 |
2.03e-49 |
|
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: 189.28 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 179 GESGAGKTVNTKRVIQYFATIA------ATGDLAKKKDSKM-------KGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 245
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVkgsrrlPTNLNDQEEDNIHneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 246 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQILsNKKPELIELLLITTNPYDYPFISQGEILVASID 325
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII-NGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 326 DAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 382
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 383 DKTAYL----MGLNSSDLLKAlcFPRVKVGNEYV-TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQ---QLDTKLPR 454
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKY--FTTNYIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 455 QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM--GIF 532
Cdd:cd14938 397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 533 SILEEECMfPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAhFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQK 612
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 613 SSNRLLAHLYATFataDADSGKKKVAKKKGSSFQTVSALF---------------RENLNKLMSNLRTTHPHFVRCIIPN 677
Cdd:cd14938 555 SENEYMRQFCMFY---NYDNSGNIVEEKRRYSIQSALKLFkrrydtknqmavsllRNNLTELEKLQETTFCHFIVCMKPN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 678 ETKTP-GAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAsaipegqfiDSKKACEKLLASIDIDHTQ 756
Cdd:cd14938 632 ESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYE 702
|
....*....
gi 98986453 757 YKFGHTKVF 765
Cdd:cd14938 703 WMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1173-1928 |
3.22e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.40 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1173 LKLRRDLEEATLQHEAMVAALrKKHADSVAELGEQIDNLQRVKQKLEK-----------EKSEFKLEIDDLSSSMESVSK 1241
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1242 SKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLE 1321
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1322 EENKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRlqds 1401
Cdd:TIGR02168 327 ELESKLDELAEELAE-------LEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQL---- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1402 EEQVEAVNAKCASLEKTKQRLQGEVEDLmvdVERANSLAAALDKKQrnfdkvLAEWKTKCEESQAELEASLKESRSLSTE 1481
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1482 LFKLKNAYEEALDQLETVKRENKNLEQEIA---DLTEQIAENGKTIHELEKSRKQI---------------ELEKADIQL 1543
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDsleRLQENLEGFSEGVKALLKNQSGLsgilgvlselisvdeGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1544 ALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDL 1623
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1624 NEIEI--QLSHANRQAAETLKHLRSVQgqLKDTQLHLDDALRGQEDlKEQLAIVERRANL--LQAEVEELRATLEQTERA 1699
Cdd:TIGR02168 623 GGVLVvdDLDNALELAKKLRPGYRIVT--LDGDLVRPGGVITGGSA-KTNSSILERRREIeeLEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1700 RKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAH 1779
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1780 LERMKKNLEQTVKDLQhrldeaeqlalkggkKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDR 1859
Cdd:TIGR02168 780 AEAEIEELEAQIEQLK---------------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1860 KNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDF 1928
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
840-1453 |
1.85e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.50 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 840 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAK 919
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 920 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKA 999
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1000 LQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDE 1079
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1080 RLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQ--RSDYARELEELSERLEEAGGV 1157
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvlIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1158 TSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRvkqkLEKEKSEFKLEIDDLSSSME 1237
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS----DLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1238 SVSKSKANLEKICRTLEDQLSEARGKNEEIQRSlselttqKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELK 1317
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAG-------GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1318 RQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQR 1397
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1398 LQD-------SEEQVEAVNAKCASLEKTKQRLQGEVEDLM-----VDVERANSLAAALDKKQRNFDKV 1453
Cdd:COG1196 776 IEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNENFQEL 843
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
921-1852 |
4.26e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.46 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 KEVTERAEDEEEINAEltakkrKLEDECSELKKDIDDLELTLAKVEKekhatenkVKNLTEELSGLDetIAKLTREKKAL 1000
Cdd:TIGR02168 174 RKETERKLERTRENLD------RLEDILNELERQLKSLERQAEKAER--------YKELKAELRELE--LALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQekklrvdLERNKRKLEGDLKLAQESILDLENDKQQLDER 1080
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-------LEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1081 LKkkdfeycQLQSKVEDEQTLGLQFQKKIKELQARIeeleeeieaeraTRAKTEKQrsdyareleelserleeaggVTST 1160
Cdd:TIGR02168 311 LA-------NLERQLEELEAQLEELESKLDELAEEL------------AELEEKLE--------------------ELKE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1161 QIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVS 1240
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSK----VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1241 KSKAnlekicrtlEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQL 1320
Cdd:TIGR02168 428 KKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1321 EEE----NKAKNALAHALQSSRHDcDLLREQYEEEQEGKAELQRALSKANSEVAqwrTKYETDAIQRTEELEEAKK---- 1392
Cdd:TIGR02168 499 ENLegfsEGVKALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvt 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1393 ----------KLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdkvlaewKTKCE 1462
Cdd:TIGR02168 575 flpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAK----------KLRPG 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1463 ESQAELEASLKESRSLSTelfklKNAYEEALDQLETvKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQ 1542
Cdd:TIGR02168 645 YRIVTLDGDLVRPGGVIT-----GGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1543 LALEEAEAALEHEEAKILRIQLELTQVKSEIDRkIAEKDEEIEQLKRNYQRTVETMQSALDaevrsrnEAIRLKKKMEGD 1622
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQ 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1623 LNEIEIQLSHANRQaaetlkhLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQterarkl 1702
Cdd:TIGR02168 791 IEQLKEELKALREA-------LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES------- 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1703 AEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKaitdaammaeelkkeqdtsahLER 1782
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE---------------------LRR 915
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1783 MKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLETRIREL-EFELEGEQKKNTESVKGLRKYERRVKELT 1852
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEV--------RIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
931-1872 |
5.17e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.46 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 931 EEINAELTAKKRKLEDECS------ELKKDIDDLELTLAKVEKEKHatENKVKNLTEELSGLDETIAKLTREKKALQEAH 1004
Cdd:TIGR02168 192 EDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEEL--REELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1005 QQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQekklrvdLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKK 1084
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQI-------LRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1085 DFEYCQLQSKVEDEQTLGLQFQKKIKELQarieeleeeieaeratraktekqrsdyareleelserleeaggvtstqiEL 1164
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELE-------------------------------------------------SR 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1165 NKKREAEFLKLRRDLEEATLQheamVAALRKKhadsVAELGEQIDNLQRVKQKLEKEKSEFKLEIDdlsssmesvskska 1244
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQ----IASLNNE----IERLEARLERLEDRRERLQQEIEELLKKLE-------------- 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1245 nlekicrtlEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEE- 1323
Cdd:TIGR02168 432 ---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLe 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1324 ---NKAKNALAHALQSSRHDcDLLREQYEEEQEGKAELQRALSKANSEVAqwrTKYETDAIQRTEELEEAKK-------- 1392
Cdd:TIGR02168 503 gfsEGVKALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpl 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1393 ------KLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdkvlaewKTKCEESQA 1466
Cdd:TIGR02168 579 dsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAK----------KLRPGYRIV 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1467 ELEASLKESRSLSTelfklKNAYEEALDQLETvKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALE 1546
Cdd:TIGR02168 649 TLDGDLVRPGGVIT-----GGSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1547 EAEAALEHEEAKILRIQLELTQVKSEIDRkIAEKDEEIEQLKRNYQRTVETMQSALDaevrsrnEAIRLKKKMEGDLNEI 1626
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQL 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1627 EIQLSHANRQaaetlkhLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQterarklAEQE 1706
Cdd:TIGR02168 795 KEELKALREA-------LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAE 860
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1707 LLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKN 1786
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVR 937
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1787 LEQTVKDL--QHRLDEAEQLALK-GGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVL 1863
Cdd:TIGR02168 938 IDNLQERLseEYSLTLEEAEALEnKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
....*....
gi 98986453 1864 RLQDLVDKL 1872
Cdd:TIGR02168 1018 TLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1732 |
4.89e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.00 E-value: 4.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKAL 1000
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLErnKRKLEGDLKLAQESILDLENDKQQLDER 1080
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1081 LKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAEratrakteKQRSDYARELEELSERLEEAGGVTST 1160
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL--------EGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1161 QIELNKKREAeflklrrdleeatlqheAMVAALRKkHADSVAelgeqIDNLQRVKQKLE--KEKSEFKLEIDDLSSSMEs 1238
Cdd:TIGR02168 528 LISVDEGYEA-----------------AIEAALGG-RLQAVV-----VENLNAAKKAIAflKQNELGRVTFLPLDSIKG- 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1239 vskskanlekicRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQ----------------TEAGELSRQLEEKESIVS-- 1300
Cdd:TIGR02168 584 ------------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRIVTld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1301 -QLSRSKQAFTQQTEE-----LKRQLE-EENKAKnalahalqssrhdcdlLREQYEEEQEGKAELQrALSKANSEVAQWR 1373
Cdd:TIGR02168 652 gDLVRPGGVITGGSAKtnssiLERRREiEELEEK----------------IEELEEKIAELEKALA-ELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1374 TKYETDAIQRTEELEEAKKKLAQRlqdsEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKV 1453
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1454 LAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENgktIHELEKSRKQ 1533
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL---AAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1534 IELEKADIQlaleeaeaaleheeakilriqlELTQVKSEIDRKIAEKDEEIEQLkRNYQRTVETMQSALDAEVRSRNEAI 1613
Cdd:TIGR02168 868 IEELESELE----------------------ALLNERASLEEALALLRSELEEL-SEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1614 rlkKKMEGDLNEIEIQLSHANRQAAEtlkhlrsvqgqlkDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEEL-RAT 1692
Cdd:TIGR02168 925 ---AQLELRLEGLEVRIDNLQERLSE-------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVN 988
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 98986453 1693 LEqterarklAEQELLDSNERVQLLHTQNTSLIHTKKKLE 1732
Cdd:TIGR02168 989 LA--------AIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
221-707 |
6.77e-25 |
|
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: 113.30 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 221 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 289
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 290 ILS--NKKPEL----IELLLITTNPYDYPFISQGEILVASIDDAEELLATD--------SAIDILGFTPEEKSGLYKLTG 355
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 356 AVMHYGNMKFKQKQREEQAEPDGT---EVADKTAYLMGLNSSDLLKALCFPR-VKVGNEYVTKGQTVD--QVHHAVNALS 429
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 430 KSVYEKLFLWMVTRINQ--------------QLDTKLPRQHFIGVL---DIAGFEIFEYNSLEQLCINFTNEKLqqFFNH 492
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--YARE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 493 HMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYDQHLGKSNN--FQ 565
Cdd:cd14894 567 EQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSsrLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 566 KPKVVKGRAEAH---------FSLIHYAGTVDYSVSGWLEKNKDPL-NETVVGLYQKSSN---RLLAHLYATFATADADS 632
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSShfcRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 633 GKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICR 707
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1163-1924 |
2.01e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.07 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1163 ELNKKREAeflkLRRDLEEATLQHEAMVAALRKKHADsVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKS 1242
Cdd:TIGR02168 236 ELREELEE----LQEELKEAEEELEELTAELQELEEK-LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1243 KANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKEsivsqlsrskqaftQQTEELKRQLEE 1322
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------------AELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1323 ENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaqrLQDSE 1402
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE---LEELQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1403 EQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKtkceesQAELEAS-LKESRSLSTE 1481
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK------ALLKNQSgLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1482 LFKLKNAYEEAldqLETVKRENKNleqeiADLTEQIAENGKTIHELEKSRKQ----IELEKADIQLALEEAEAALEHEEA 1557
Cdd:TIGR02168 528 LISVDEGYEAA---IEAALGGRLQ-----AVVVENLNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1558 kILRIQLELTQVKSEIDRKIA----------EKDEEIEQLKRNYQR--------------------TVETMQSALdaevr 1607
Cdd:TIGR02168 600 -FLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggvitggSAKTNSSIL----- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1608 SRNEAIrlkKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVE 1687
Cdd:TIGR02168 674 ERRREI---EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1688 ELRATLEQTERARKLAEQELLDSNERVQLLHTQntslihtKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMA 1767
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1768 EELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERR 1847
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLA--------AEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1848 VKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFR-KAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1529 |
8.13e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 110.15 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTL---VQEKNDLQLQVQAESENLLDAEERCD---QLIKAKF-QLEAK 919
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEqqkQILRERLaNLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 920 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKA 999
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1000 LQEAHQQALDDLQAEEDKVNSLNKTKSKL-----EQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDK 1074
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1075 QQLDERLKKKDFEYCQLQSKVEDEQTLGlQFQKKIKELQARIEELEEEIEAERATRAKTEKQ--------------RSDY 1140
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFS-EGVKALLKNQSGLSGILGVLSELISVDEGYEAAieaalggrlqavvvENLN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1141 ARELEELSERLEEAGGVT--------STQIELN----KKREAEFLKLRRDLEEATLQHEAMVAAL--------------- 1193
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTflpldsikGTEIQGNdreiLKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldnale 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1194 ------------------------------------------RKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDD 1231
Cdd:TIGR02168 637 lakklrpgyrivtldgdlvrpggvitggsaktnssilerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1232 LSSSME-------SVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSR 1304
Cdd:TIGR02168 717 LRKELEelsrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1305 SKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdAIQRT 1384
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESEL 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1385 EELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERAN-SLAAALDKKQRNFDKVLAEWKTKCEE 1463
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1464 SQAELEASLKESRSLSTELFKLKNAYEE-------ALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEK 1529
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1166-1828 |
1.47e-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: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1166 KKREAEfLKLrrdleEATLQHEAMVAALRkkhadsvAELGEQIDNLQR----------VKQKL-EKEKSEFKLEIDDLSS 1234
Cdd:COG1196 173 RKEEAE-RKL-----EATEENLERLEDIL-------GELERQLEPLERqaekaeryreLKEELkELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1235 SMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTE 1314
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1315 ELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdaiqrtEELEEAKKKL 1394
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-----------EELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1395 AQRLQDSEEQveavnakcaslEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdkvlaewktkcEESQAELEASLKE 1474
Cdd:COG1196 389 LEALRAAAEL-----------AAQLEELEEAEEALLERLERLEEELEELEEAL--------------AELEEEEEEEEEA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEH 1554
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1555 EEAKILRiqleltqvkseIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAevrsrneAIRLKKKMEGDLNeiEIQLSHAN 1634
Cdd:COG1196 524 GAVAVLI-----------GVEAAYEAALEAALAAALQNIVVEDDEVAAAA-------IEYLKAAKAGRAT--FLPLDKIR 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1635 RQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERV 1714
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1715 QLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDL 1794
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
650 660 670
....*....|....*....|....*....|....
gi 98986453 1795 QHRLDEAEQLALKGGKKQIQKLETRIRELEFELE 1828
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1284-1924 |
1.51e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.38 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1284 EAGELSRQLEEKESIVSQLSRSKQAFTQQT---EELKRQLE----EENKAKNALAHALQSSRHDCDLLREQYEEEQEGKA 1356
Cdd:TIGR02168 163 EAAGISKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEKAERYKELKAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1357 ELQRALSKANSEvaqwRTKYETDAIQRTEELEEAKKK---LAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDV 1433
Cdd:TIGR02168 243 ELQEELKEAEEE----LEELTAELQELEEKLEELRLEvseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1434 ERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADL 1513
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1514 TEQIAENGKTIHELEKSRKQ--------------------------IELEKADIQLALEEAEAALEHEEAKILRIQLELT 1567
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERlqqeieellkkleeaelkelqaeleeLEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1568 QVKSEIDRKIAEKD--EEIEQLKRNYQRTVETM---QSALDAEVRSRNEAIRLKKKME--------GDLNEIEIQLSHAN 1634
Cdd:TIGR02168 479 AAERELAQLQARLDslERLQENLEGFSEGVKALlknQSGLSGILGVLSELISVDEGYEaaieaalgGRLQAVVVENLNAA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1635 RQAAETLK-----------------------------HLRSVQGQLKD-----TQLH---------------LDDALRGQ 1665
Cdd:TIGR02168 559 KKAIAFLKqnelgrvtflpldsikgteiqgndreilkNIEGFLGVAKDlvkfdPKLRkalsyllggvlvvddLDNALELA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1666 EDLKEQLAIV-------------------------ERRANL--LQAEVEELRATLEQTERARKLAEQELLDSNERVQLLH 1718
Cdd:TIGR02168 639 KKLRPGYRIVtldgdlvrpggvitggsaktnssilERRREIeeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLR 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1719 TQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL 1798
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1799 DEAEQlALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKS 1878
Cdd:TIGR02168 799 KALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 98986453 1879 YKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1639 |
1.54e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.38 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEFQKTKDELAKSEAKRKELE------EKLVTLVQEKNDLQLQVQAESenLLDAEERCDQLIKAKFQLEA 918
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 919 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKK 998
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 999 ALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLD 1078
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1079 ERLKKKDFEYCQLQSKVE--DEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGG 1156
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1157 VTSTQ------------IELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAelgeqIDNLQRVKQKLE--KEK 1222
Cdd:TIGR02168 494 LERLQenlegfsegvkaLLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAflKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1223 SEFKLEIDDLSSSMEsvskskanlekicRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQ----------------TEAG 1286
Cdd:TIGR02168 569 ELGRVTFLPLDSIKG-------------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1287 ELSRQLEEKESIVS---QLSRSKQAFTQQTEE-----LKRQLE-EENKAKnalahalqssrhdcdlLREQYEEEQEGKAE 1357
Cdd:TIGR02168 636 ELAKKLRPGYRIVTldgDLVRPGGVITGGSAKtnssiLERRREiEELEEK----------------IEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1358 LQrALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdsEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERAN 1437
Cdd:TIGR02168 700 LA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1438 SLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQI 1517
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1518 AENGKTIHELEKSR--KQIELEKADIQLALEEAEAALEHEEAKILRIQL-ELTQVKSEIDRKIAEKDEEIEQLKRNYQRT 1594
Cdd:TIGR02168 855 ESLAAEIEELEELIeeLESELEALLNERASLEEALALLRSELEELSEELrELESKRSELRRELEELREKLAQLELRLEGL 934
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 98986453 1595 ---VETMQSALDAEVR-SRNEAIRLKKKMEGDLNEIEIQLSHANRQAAE 1639
Cdd:TIGR02168 935 evrIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1313-1910 |
4.44e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1313 TEELKRQLEE-ENKAKNAL-AHALQSSRHDCDL---------LREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtdai 1381
Cdd:COG1196 195 LGELERQLEPlERQAEKAErYRELKEELKELEAellllklreLEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1382 qrteELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKC 1461
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1462 EESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADI 1541
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1542 QLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRnYQRTVETMQSALDAEVRSRNEAIRLKKKMEG 1621
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL-LEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1622 DLNE------------------IEIQLSHANRQAAETLKHLRSVQGQLKDTQlhldDALRGQEDLKEQLAivERRANLLQ 1683
Cdd:COG1196 506 FLEGvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKA--GRATFLPL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1684 AEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDA 1763
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1764 AMMAEELKKEQDTSahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRK 1843
Cdd:COG1196 660 GSLTGGSRRELLAA--LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1844 YERRVKELTYQSEEDRKNVLRLQDLvDKLQVKVKSYKRQ-----------AEEADEQANAHltKFRKAQHE-LEEAEER 1910
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDL-EELERELERLEREiealgpvnllaIEEYEELEERY--DFLSEQREdLEEARET 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1579 |
9.73e-22 |
|
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: 103.22 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKndlQLQVQAESENLLDAEERCDQLIKAKF--------- 914
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE---QLRVKEKIGELEAEIASLERSIAEKEreledaeer 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 --QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAK 992
Cdd:TIGR02169 324 laKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 993 LTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQekklrvdLERNKRKLEGDLKLAQESILDLEN 1072
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK-------QEWKLEQLAADLSKYEQELYDLKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1073 DKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELqarieelEEEIEAERATRAKTEKQRSDYARELEELSERLE 1152
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQLGSVGERYATAIEVAAGNRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1153 EA-----GGVTSTQIELNKKRE---AEFL---KLRRDLEEATLQHEAMVAALrkkhADSVAELGEQIDNLQR-------V 1214
Cdd:TIGR02169 550 NNvvvedDAVAKEAIELLKRRKagrATFLplnKMRDERRDLSILSEDGVIGF----AVDLVEFDPKYEPAFKyvfgdtlV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1215 KQKLEKEKS---EFKL-----EIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAG 1286
Cdd:TIGR02169 626 VEDIEAARRlmgKYRMvtlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1287 ELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEenkaknalahalqssrhdcdlLREQYEEEQEGKAELQRALSKAN 1366
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE---------------------LEEDLSSLEQEIENVKSELKELE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1367 SEVAQwrtkYETDAIQRTEELEEAKKKLAQrlqdseEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKK 1446
Cdd:TIGR02169 765 ARIEE----LEEDLHKLEEALNDLEARLSH------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1447 QRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHE 1526
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1527 LEKSRKQIElEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAE 1579
Cdd:TIGR02169 915 KRKRLSELK-AKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
866-1423 |
1.34e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 866 KSEAKRKELEEklvtLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLE 945
Cdd:COG1196 219 KEELKELEAEL----LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 946 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTK 1025
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1026 SKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQF 1105
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1106 QKKIKELQARIEELEEEIEAE----RATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEE 1181
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLeaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1182 A--TLQHEAMVAALRKKHADSVAELGEQIDNLqrvKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKIcRTLEDQLSE 1259
Cdd:COG1196 535 AyeAALEAALAAALQNIVVEDDEVAAAAIEYL---KAAKAGRATFLPLDKIRARAALAAALARGAIGAAV-DLVASDLRE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1260 ARGKNEEIQRSLSELTTQKSRLQTeAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRH 1339
Cdd:COG1196 611 ADARYYVLGDTLLGRTLVAARLEA-ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1340 DcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTK 1419
Cdd:COG1196 690 E---EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
....
gi 98986453 1420 QRLQ 1423
Cdd:COG1196 767 RELE 770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1201-1910 |
3.80e-21 |
|
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: 101.30 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1201 VAELGEQIDNLQRVKQKLEK------EKSEFKL-----EIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQR 1269
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERyqallkEKREYEGyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1270 SLSELTTQKSRL-QTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEenkaknalahaLQSSRHDCDLLREQY 1348
Cdd:TIGR02169 273 LLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-----------LEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1349 EEEQEGKAELQRALSkanSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVED 1428
Cdd:TIGR02169 342 EREIEEERKRRDKLT---EEYAELKEELE-DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1429 LMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQ 1508
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1509 EIADLTEQIAENGKTIHELEKSRK----------------QIELEKAD--------IQLALEEAEAALEHEEAKILR--- 1561
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryATAIEVAAgnrlnnvvVEDDAVAKEAIELLKRRKAGRatf 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1562 IQLELTQVKSEIDRKIAEK------------DEEIEQ-LKRNYQRT--VETMQSA-----------LDAEV--------- 1606
Cdd:TIGR02169 578 LPLNKMRDERRDLSILSEDgvigfavdlvefDPKYEPaFKYVFGDTlvVEDIEAArrlmgkyrmvtLEGELfeksgamtg 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1607 --RSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQA 1684
Cdd:TIGR02169 658 gsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1685 EVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLmqLQSEVEDASRDARNAEEKAKKAITDAA 1764
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLR 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1765 MMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKK----QIQKLETRIRELEFELEGEQKKNTESV 1838
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELE 895
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1839 KGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEaDEQANAHLTKFRKAQHELEEAEER 1910
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1388-1922 |
2.98e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.47 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1388 EEAKKKLAQ------RLQDSEEQVEAvnaKCASLEK------TKQRLQGEVEDLmvdveRANSLAAALD---KKQRNFDK 1452
Cdd:COG1196 175 EEAERKLEAteenleRLEDILGELER---QLEPLERqaekaeRYRELKEELKEL-----EAELLLLKLReleAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1453 VLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRK 1532
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1533 QIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEA 1612
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1613 IRL------KKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEV 1686
Cdd:COG1196 407 EAEeallerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1687 EELRATLEQTERARKLAEQEL-----LDSNERVQLLHTQNTSLIHTKKKLETDL-----MQLQSEVEDASRDARNAEEKA 1756
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaAALQNIVVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1757 KKA-------ITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL---------DEAEQLALKGGKKQIQKLETRI 1820
Cdd:COG1196 567 KAAkagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgRTLVAARLEAALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1821 RELEFELEGEQkkntesvKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKA 1900
Cdd:COG1196 647 REVTLEGEGGS-------AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580
....*....|....*....|..
gi 98986453 1901 QHELEEAEERADIAESQVNKLR 1922
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEEL 741
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1002-1802 |
9.18e-20 |
|
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: 96.73 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1002 EAHQQALDDLQAEEDKVNSLN-KTKSKLEQQVEDLESSLEQ---EKKLRVDLERNKRKLEGDLKlaqesildlendkQQL 1077
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHeKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR-------------NQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1078 DERLKKKDFEYCQLQSKVEDEQTlglqfqkKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGV 1157
Cdd:pfam15921 148 QNTVHELEAAKCLKEDMLEDSNT-------QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1158 TSTQIELNKKREAEFLKLRrdleeaTLQHEAMVAALRKKHADSVAELgeqidnLQRVKQKLEKEKSEFKLEIDDLSSSME 1237
Cdd:pfam15921 221 AISKILRELDTEISYLKGR------IFPVEDQLEALKSESQNKIELL------LQQHQDRIEQLISEHEVEITGLTEKAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1238 SVSKSKANLEKICRTLEDQlseARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEK-ESIVSQLSRSKQAFTQQTEEL 1316
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1317 KRQLEEENKAKNALAHAL---QSSRHDCDLLREQYE---EEQEGKA----ELQRALSKANSEVaqwrtkyetdaiQRTEE 1386
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLLadlHKREKELSLEKEQNKrlwDRDTGNSitidHLRRELDDRNMEV------------QRLEA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1387 LEEAKKKLAQ--------RLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDL------MVDVERANS-LAAALDKKQRNFD 1451
Cdd:pfam15921 434 LLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtLESSERTVSdLTASLQEKERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1452 KVLAEwktkCEESQAELEASLKESRSLSTELFKLKNAYEE--ALD-QLETVKRENKNLEQEIADLTEQIAENGKTIHELE 1528
Cdd:pfam15921 514 ATNAE----ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEceALKlQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1529 KSRKQIELEKADIQLALEEAEAALEHEEAKILRIQ-----LELTQVK-----SEIDRKIAEKDEEIEQLKRNYQRTVETM 1598
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1599 QS-ALDAEVRSRNeaIRLK-KKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGqlkdTQLHlddALRGQEDLKEQLAIVE 1676
Cdd:pfam15921 670 NSlSEDYEVLKRN--FRNKsEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG----SDGH---AMKVAMGMQKQITAKR 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1677 RRANLLQAEVEELRATLEQTERARKLAEQElldSNERVQLLHTQNTSlihtKKKLETDLMQLQSEVEDASRDARNAEEKA 1756
Cdd:pfam15921 741 GQIDALQSKIQFLEEAMTNANKEKHFLKEE---KNKLSQELSTVATE----KNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 98986453 1757 KKAITDAAMMAEELKKEQDTSAHLErmkknleqtvkdLQHRLDEAE 1802
Cdd:pfam15921 814 DKASLQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1701 |
1.18e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.21 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEMAtmkEEFQKTKDELAKSEAKrkELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 KEVTERAEDE-EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKA 999
Cdd:TIGR02169 275 EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1000 LQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDE 1079
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1080 RLKkkdfeycQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSD----YARELEELSERLEEAG 1155
Cdd:TIGR02169 435 KIN-------ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKlqreLAEAEAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1156 GVTSTQIELNKKREAeFLKLRRDLEEATLQHEAM--VAALRKKHA-----DSVAElgEQIDNLQRVKQ------KLEKEK 1222
Cdd:TIGR02169 508 GGRAVEEVLKASIQG-VHGTVAQLGSVGERYATAieVAAGNRLNNvvvedDAVAK--EAIELLKRRKAgratflPLNKMR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1223 SEFKleidDLSSSMESVSKSKA-NLEKICRTLEDQLSEARG-----KNEEIQRSLseltTQKSRLQTEAGELsrqLEEKE 1296
Cdd:TIGR02169 585 DERR----DLSILSEDGVIGFAvDLVEFDPKYEPAFKYVFGdtlvvEDIEAARRL----MGKYRMVTLEGEL---FEKSG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1297 SIV--SQLSRSKQAFT-QQTEELKRQLEEENKAKNALAhalqssrhdcDLLREQYEEEQEGKaELQRALSKANSEVAqwr 1373
Cdd:TIGR02169 654 AMTggSRAPRGGILFSrSEPAELQRLRERLEGLKRELS----------SLQSELRRIENRLD-ELSQELSDASRKIG--- 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1374 tkyetDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMvdvERANSLAAALDKKQRNFDKv 1453
Cdd:TIGR02169 720 -----EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---EDLHKLEEALNDLEARLSH- 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1454 laewkTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQ 1533
Cdd:TIGR02169 791 -----SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1534 IELEKADIQLALEEAEAALEHEEAKILRIQLELtqvkSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAI 1613
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQL----RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1614 RLKKKMEGDLNEIEIQlshANRQAAET-LKHLRSVQGQLKDtqlHLDDALRGQEDLKEQLAIverranlLQAEVEELRAT 1692
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQ---AELQRVEEeIRALEPVNMLAIQ---EYEEVLKRLDELKEKRAK-------LEEERKAILER 1008
|
....*....
gi 98986453 1693 LEQTERARK 1701
Cdd:TIGR02169 1009 IEEYEKKKR 1017
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1275-1932 |
1.18e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 93.32 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1275 TTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEElkrqleeenkaKNALAHALQSSRHDCDLLREQYEEEQEG 1354
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-----------KNALQEQLQAETELCAEAEEMRARLAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1355 KAELQRALSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQDSEEQVEAVnakcaslEKTKQRLQGEVEDLMVDVE 1434
Cdd:pfam01576 70 KQELEEILHELESRLEEEE--------ERSQQLQNEKKKMQQHIQDLEEQLDEE-------EAARQKLQLEKVTTEAKIK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1435 RANSLAAALDKKQRNFDKVlaewKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLET-VKRENK--------- 1504
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKE----RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEErLKKEEKgrqelekak 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1505 -NLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKdEE 1583
Cdd:pfam01576 211 rKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR-NK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1584 IEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQ-LKDTQLHLDDAL 1662
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaLEELTEQLEQAK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1663 RGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELldsnervQLLHTQNTSLIHTKKKLETDLMQLQSEV 1742
Cdd:pfam01576 370 RNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQL-------QELQARLSESERQRAELAEKLSKLQSEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1743 EDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKD-------LQHRLDEAEQlALKGGKKQIQK 1815
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQledernsLQEQLEEEEE-AKRNVERQLST 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1816 LETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEED-------RKNVLRLQDLVDKLQVKVKSYK-------- 1880
Cdd:pfam01576 522 LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKaaaydklEKTKNRLQQELDDLLVDLDHQRqlvsnlek 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1881 -----------------RQAEE---ADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSR 1932
Cdd:pfam01576 602 kqkkfdqmlaeekaisaRYAEErdrAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
831-1435 |
2.09e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.90 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 831 MKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDlQLQVQAEsENLLDAEERCDQLI 910
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAE-EAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 911 KAKFQLEAKIKEvTERAEDEEEINAEltaKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEELSGLDETI 990
Cdd:PTZ00121 1340 EAKKAAEAAKAE-AEAAADEAEAAEE---KAEAAEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADEL 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 991 AKLTREKKALQEAHQQALDDLQAEEdkvnslNKTKSKLEQQVEDLESSLEQEKKlrvdLERNKRKLEgDLKLAQESILDL 1070
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKKAEEKKKADE------AKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAE-EAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1071 ENDKQQldERLKKKDFEycqlQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEaeratRAKTEKQRSDYARELEELSER 1150
Cdd:PTZ00121 1480 EEAKKA--DEAKKKAEE----AKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-----KKAEEAKKADEAKKAEEKKKA 1548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1151 LeeaggvtstqiELNKKREAEFLKLRRDLEEATLQHEAMVAALRKkhadsvAELGEQIdnlqrvkqklEKEKSEFKLEID 1230
Cdd:PTZ00121 1549 D-----------ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKA----------EEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1231 DLSSSMESVSKSKANLEKIcrtledqLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFT 1310
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKI-------KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1311 QQTEELKRQLEEENKAKNALAHALQSSRhDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL--- 1387
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkd 1752
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 98986453 1388 EEAKKKLAQRLQDSEEQVEAVNAKCASLekTKQRLQGEVEDLMVDVER 1435
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1247-1924 |
3.64e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1247 EKICRTLEDqLSEARGKNEEIQRSLSELTTQKSRLQTEAG------ELSRQLEEKE-----SIVSQLSRSKQAFTQQTEE 1315
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEgyellKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1316 LKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKA-ELQRALSKANSEVAQWRtkyetDAIqrtEELEEAKKKL 1394
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLE-----RSI---AEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1395 AQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKE 1474
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAaleh 1554
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE---- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1555 eeaKILRIQLELTQVKSEIDRKIAEKDE---------------------------EIEQLKRNYQRTVETMQSA-LDAEV 1606
Cdd:TIGR02169 477 ---EYDRVEKELSKLQRELAEAEAQARAseervrggraveevlkasiqgvhgtvaQLGSVGERYATAIEVAAGNrLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1607 RSRN----EAIRLKKKMEG-------------------------------DLNEIEIQLSHANRQA------AETLKHLR 1645
Cdd:TIGR02169 554 VEDDavakEAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavDLVEFDPKYEPAFKYVfgdtlvVEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1646 SVQGQLKDTQLHLD------------DALRGQE----DLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLD 1709
Cdd:TIGR02169 634 RLMGKYRMVTLEGElfeksgamtggsRAPRGGIlfsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1710 SNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknleq 1789
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR------ 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1790 tvkDLQHRLDEAEQLALKgGKKQIQKLETRIRELE-------FELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNV 1862
Cdd:TIGR02169 788 ---LSHSRIPEIQAELSK-LEEEVSRIEARLREIEqklnrltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1863 LRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
918-1794 |
3.73e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 918 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEELSGLDETIAK 992
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 993 LTREKKALQEAHQQALDDLQAEEDKVNSLNKTKS-KLEQQVEDLESSLEQekklrvdlernkrkLEGDLKLAQESILDLE 1071
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIAS--------------LERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1072 NDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERL 1151
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1152 EEAGGVTSTQIELNKKREAEFLKLRRDLEEAtlqhEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfkleidd 1231
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE------- 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1232 lsssmesvsksKANLEKICRTLEDQLSEArgkneeiQRSLSELTTQKSRLQTEAGELSRQLEEKES-------IVSQLSR 1304
Cdd:TIGR02169 471 -----------LYDLKEEYDRVEKELSKL-------QRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1305 SKQAFTQQTEELKRQ------LEEENKAKNA--LAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKY 1376
Cdd:TIGR02169 533 VGERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1377 ETD---AIQRT---EELEEAKKKLAQ-RLQDSE-EQVEAVNA------KCASLEKTKQRLQGEVEDLMVDVERANSLAAA 1442
Cdd:TIGR02169 613 EPAfkyVFGDTlvvEDIEAARRLMGKyRMVTLEgELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1443 LDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGK 1522
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1523 TIHELEKSRKQIELEKADiqlaleeaeaaleheeAKILRIQLELTQVKSEIdRKIAEKDEEIEQLKRNYQRTVETMQSAL 1602
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSH----------------SRIPEIQAELSKLEEEV-SRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1603 DAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQlhlddalRGQEDLKEQLAIVERRANLL 1682
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK-------KERDELEAQLRELERKIEEL 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1683 QAEVEELRATLEQTERARKLAEQEL--LDSNERVQLLHTQNtslihtkkklETDLMQLQSEVEDASRDARNAEEKAKKAI 1760
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELseIEDPKGEDEEIPEE----------ELSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
890 900 910
....*....|....*....|....*....|....
gi 98986453 1761 TDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDL 1794
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1258-1912 |
4.50e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1258 SEARGKNEEIQRSLSELTTQKSRLQ--TEAGELSRQLEE--KESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNAL--- 1330
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEeaKKKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARkae 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1331 -AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE----TDAIQRTEEL----EEAKKKLAQR---- 1397
Cdd:PTZ00121 1174 dAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEdakkAEAVKKAEEAkkdaEEAKKAEEERnnee 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1398 LQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRS 1477
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1478 LSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKS----RKQIELEK-ADIQLALEEAEAAL 1552
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeekKKADEAKKkAEEDKKKADELKKA 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1553 EHEEAKILRIQLELTQV-KSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLS 1631
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKkKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1632 HANRQAAETLKhlrSVQGQLKDTQLHLDDALRGQEDLK---EQLAIVERRANLLQAEVEELRAT--LEQTERARKlAEQE 1706
Cdd:PTZ00121 1494 EAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKK-AEEA 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1707 LLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKN 1786
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1787 LEQTVKDLQH-RLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRL 1865
Cdd:PTZ00121 1642 EAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 98986453 1866 QDLVDKLQVKVKSYKRQAEEAD---EQANAHLTKFRKAQHELEEAEERAD 1912
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
973-1591 |
8.58e-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: 86.61 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 973 ENKVKNLTEELSGLDETIAKLTREKKALQeahqqalDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERN 1052
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1053 KRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAK 1132
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1133 TEKQRSDyareleelserleeaggvtstqieLNKKREAEFLKLrrdleeatlqheAMVAALRKKHAdsvaELGEQIDNLQ 1212
Cdd:TIGR04523 185 IQKNIDK------------------------IKNKLLKLELLL------------SNLKKKIQKNK----SLESQISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1213 RVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQL 1292
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1293 EEkeSIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQW 1372
Cdd:TIGR04523 305 EQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1373 RtkyetdaiQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDK 1452
Cdd:TIGR04523 383 K--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1453 VLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRK 1532
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1533 QIELEKADIQlaleeaeaaleheeAKILRIQLELTqvKSEIDRKIAEKDEEIEQLKRNY 1591
Cdd:TIGR04523 535 EKESKISDLE--------------DELNKDDFELK--KENLEKEIDEKNKEIEELKQTQ 577
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1109-1733 |
2.18e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1109 IKELQARIeeleeeieaeratrAKTEKQRSD---YAREleelserleeaggvtstQIELnKKREAEFLKLRRDLEEATLQ 1185
Cdd:COG1196 195 LGELERQL--------------EPLERQAEKaerYREL-----------------KEEL-KELEAELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1186 heaMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNE 1265
Cdd:COG1196 243 ---ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1266 EIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLR 1345
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1346 EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKcASLEKTKQRLQGE 1425
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL-AELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1426 VEDLMVDVERANSLAAALDKKQRNFDKVLAEWKtkceesQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKN 1505
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVK------AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1506 LEQEiADLTEQIAENGK------TIHELEKSRKQIELEKADIQLALEE---AEAALEHEEAKILRIQLELTQVKSEIDRK 1576
Cdd:COG1196 553 VEDD-EVAAAAIEYLKAakagraTFLPLDKIRARAALAAALARGAIGAavdLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1577 IAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQL 1656
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1657 HLDDALRGQ---EDLKEQLAIVERRANLLQAE------------------VEELRATLEQTERARK-------LAEQELL 1708
Cdd:COG1196 712 AEEERLEEEleeEALEEQLEAEREELLEELLEeeelleeealeelpeppdLEELERELERLEREIEalgpvnlLAIEEYE 791
|
650 660
....*....|....*....|....*
gi 98986453 1709 DSNERVQLLHTQNTSLIHTKKKLET 1733
Cdd:COG1196 792 ELEERYDFLSEQREDLEEARETLEE 816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1456 |
3.21e-16 |
|
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: 85.12 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIK 921
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 922 EVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREK---- 997
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGerya 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 998 KALQEAHQQALDDLQAEEDKVNS------------------LNKTKSKL---------------------EQQ------- 1031
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflpLNKMRDERrdlsilsedgvigfavdlvefDPKyepafky 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1032 -------VEDLESSLEQEKKLR-VDLE---------------------RNKRKLEGDLKLAQESILDLENDKQQLDERLK 1082
Cdd:TIGR02169 619 vfgdtlvVEDIEAARRLMGKYRmVTLEgelfeksgamtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1083 KKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYareleelserleeaggvtstqi 1162
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV---------------------- 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1163 elnkkrEAEFLKLRRDLEEATLQHEAMVAALRKKHADsvaELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKS 1242
Cdd:TIGR02169 757 ------KSELKELEARIEELEEDLHKLEEALNDLEAR---LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1243 KANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKsrlqteaGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEE 1322
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1323 ENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQDSE 1402
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEPVNMLAI 978
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1403 EQVEAVNAKCASLEKTKQRLQGEVEDL-----MVDVERANSLAAALDKKQRNFDKVLAE 1456
Cdd:TIGR02169 979 QEYEEVLKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1209-1906 |
3.71e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.02 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1209 DNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLsELTTQKSRLQTEAGEL 1288
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1289 SRQLEEKESIVSQLSRSKQAFTQQTEELK-----RQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALS 1363
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRARKAAPlaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1364 KANSEVAQW-RTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVedlmvdveranSLAAA 1442
Cdd:TIGR00618 346 LLQTLHSQEiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ-----------ATIDT 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1443 LDKKQRNFDKVLAEWKTKCEESQAELEaslkESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGK 1522
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQELQQRYAE----LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1523 TIHE--LEKSRKQIELEKADIQ-LALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKR---NYQRTVE 1596
Cdd:TIGR00618 491 VVLArlLELQEEPCPLCGSCIHpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASlkeQMQEIQQ 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1597 TMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVE 1676
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1677 RRANLLQAEVEE-LRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKL---ETDLMQLQSEVEDASRDARNA 1752
Cdd:TIGR00618 651 LQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLrelETHIEEYDREFNEIENASSSL 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1753 EEKAKKAITDAAMMAEELKKEQDTS-AHLERMKKNLEQTVKDLQHRLDEAEQLalkggkkqIQKLETRIRELEfELEGEQ 1831
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTGAELSHL--------AAEIQFFNRLRE-EDTHLL 801
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 1832 KKNTESVKGLRKYERRVKELT-YQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQaNAHLTKFRKAQHELEE 1906
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ-LAQLTQEQAKIIQLSD 876
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1526 |
3.72e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.19 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQlqvQAESENLLDAEERCDQlIKAKFQ 915
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR---KAEDAKKAEAVKKAEE-AKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 916 LEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTR 995
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 996 EKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQ 1075
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1076 QLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEeeieaeratRAKTEKQRSDYARELEELSERLEEAG 1155
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1156 GVTSTQIELNKKREAEFLKLRRDlEEATLQHEAMVAALRKKHADSVAELGEQidnlqrvKQKLEKEKSEFKLEIDDLsss 1235
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEA--- 1539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1236 meSVSKSKANLEKICRTLEDQLSEARGKNEEIQRSlseltTQKSRLQTEAGELSRQLEEKEsIVSQLSRSKQAFTQQTEE 1315
Cdd:PTZ00121 1540 --KKAEEKKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEE 1611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1316 LKRqlEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL---EEAKK 1392
Cdd:PTZ00121 1612 AKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaEEDEK 1688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1393 KLAQRLQDSEEQ---VEAVNAKCASLEKTKQRLQGEVEDLMVDVERAnslaaaldKKQRNFDKVLAEWKTKCEESQAELE 1469
Cdd:PTZ00121 1689 KAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1470 ASLKESRSLSTELFKLKNAYEEaldqlETVKRENKNLEQEIADLTEQIAENGKTIHE 1526
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1301-1906 |
4.13e-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: 84.78 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1301 QLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVaqwrtkyeTDA 1380
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1381 IQRT-EELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQrlqgEVEDLMVDVERANSlaaaldkkqrnfDKVLAEWKT 1459
Cdd:pfam15921 147 LQNTvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG------------KKIYEHDSM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1460 KCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKN----LEQEIADLTEQ-IAENGKTIHELEKSRKQI 1534
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkielLLQQHQDRIEQlISEHEVEITGLTEKASSA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1535 ELEKADIQLALEEAEAALEHEEAKILRiQLeltqvkSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALD------AEVRS 1608
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARNQNSMYMR-QL------SDLESTVSQLRSELREAKRMYEDKIEELEKQLVlanselTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1609 RNEAIRLK--------KKMEGDLNEIEIQLSHANRQAAE----------TLKHLR----------------------SVQ 1648
Cdd:pfam15921 364 ERDQFSQEsgnlddqlQKLLADLHKREKELSLEKEQNKRlwdrdtgnsiTIDHLRrelddrnmevqrleallkamksECQ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1649 GQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRA---TLEQTERARKLAEQELldsNERVQLLHTQNTSLI 1725
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASL---QEKERAIEATNAEIT 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1726 HTKKKLETDLMQLQ--SEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQD-----------TSAHLERMKKNLEQTVK 1792
Cdd:pfam15921 521 KLRSRVDLKLQELQhlKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrTAGAMQVEKAQLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1793 DLQHRLDEAEQLALKGGKKqIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNvlrLQDLVDKL 1872
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE---LNSLSEDY 676
|
650 660 670
....*....|....*....|....*....|....
gi 98986453 1873 QVKVKSYKRQAEEADEQANAHLTKFRKAQHELEE 1906
Cdd:pfam15921 677 EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
964-1864 |
4.55e-16 |
|
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: 84.64 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 964 KVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAhqqalDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEK 1043
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET-----ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1044 KLRvdLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEI 1123
Cdd:pfam02463 218 KLE--LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1124 EAERATRAKTEKQRSDYARELEELSERLEEAggvtSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAE 1203
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1204 LGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQT 1283
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1284 EAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALS 1363
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1364 KANSEVAQwrtKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAAL 1443
Cdd:pfam02463 532 GDLGVAVE---NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1444 DKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKT 1523
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1524 IHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALD 1603
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1604 AEVRSRNEAIRLKKKMEgdlNEIEIQLSHANRQAAETLKHLRSVQgQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQ 1683
Cdd:pfam02463 769 LSLKEKELAEEREKTEK---LKVEEEKEEKLKAQEEELRALEEEL-KEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1684 AEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDarnaEEKAKKAITDA 1763
Cdd:pfam02463 845 EQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL----NLLEEKENEIE 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1764 AMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRK 1843
Cdd:pfam02463 921 ERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
890 900
....*....|....*....|.
gi 98986453 1844 YERRVKELTYQSEEDRKNVLR 1864
Cdd:pfam02463 1001 EEEKKKLIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1596 |
1.13e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQlEAKIKEVT 924
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 925 ERAEDEEEINAeltAKKRKLEDECSELKKDIDDLELTLA-KVEKEKHATENKV---KNLTEELSGLDETIAKLTREKKAL 1000
Cdd:PTZ00121 1170 RKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALDDLQAEEDKVNSLNKTKSKLEQ--QVEDLESSLEQEKKLRVDLERNKRKLEgDLKLAQESILDLENDKQQLD 1078
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1079 ERLKKKDfeycQLQSKVEdEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAggvt 1158
Cdd:PTZ00121 1326 EAKKKAD----AAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA---- 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1159 STQIELNKKREAEflkLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMES 1238
Cdd:PTZ00121 1397 KKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1239 VSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSElttQKSRLQTEAGELSRQLEEkesiVSQLSRSKQAFTQQTEELKR 1318
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1319 QLEEENKAKNaLAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEvaQWRTKYETDAIQRTEEL---EEAKKKLA 1395
Cdd:PTZ00121 1547 KADELKKAEE-LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAkkaEEAKIKAE 1623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1396 QRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEdlmvdvERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKES 1475
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA------EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1476 RSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSrkqiELEKADIQLALEEAEAALEHE 1555
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEI 1773
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 98986453 1556 EAKILRIQLEltQVKSEIDRKIAEKDEEIEQLKRNYQRTVE 1596
Cdd:PTZ00121 1774 RKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1078-1839 |
1.18e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 83.65 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1078 DERLK--KKDFEYCQLQSKVEDEQTLglQFQKKIKELQARIEELEEEIEAERATRAKTEK-QRSDYARELEELSERLEEA 1154
Cdd:PTZ00121 1069 DEGLKpsYKDFDFDAKEDNRADEATE--EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEAR 1146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1155 GGVTSTQIELNKK-REAEFLKLRRDLEEATLQHEAMVA-ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEfKLEIDDL 1232
Cdd:PTZ00121 1147 KAEDAKRVEIARKaEDARKAEEARKAEDAKKAEAARKAeEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1233 SSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQrsLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQ 1312
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1313 TEELKRQLEEENKAKNALAHAlQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEE---LEE 1389
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1390 AKKKLAQRLQDSEEQVEAVNAKCASLE-KTKQRLQGEVEDLMVDVERANSLAAAldKKQRNFDKVLAEWKTKCEESQAEL 1468
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1469 EASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEiADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEA 1548
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1549 EAALEHEEAKILRIQLELTqvKSEIDRKIAEKDEEiEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDlneiEI 1628
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EA 1612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1629 QLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERA----RKLAE 1704
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedeKKAAE 1692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1705 QELLDSNErvqllhtqntslihtKKKLEtdlmQLQSEVEDASRDArnaeEKAKKAITDAAMMAEELKKEQDTSAHLERMK 1784
Cdd:PTZ00121 1693 ALKKEAEE---------------AKKAE----ELKKKEAEEKKKA----EELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1785 KNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVK 1839
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
836-1330 |
3.07e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.61 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ 915
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 916 LEAKIKEVTERAEDEEEINAELT---AKKRKLEDECSELKKDIDDLELTLAKVE---------------------KEKHA 971
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 972 TENKVKNLTEELSGLDETIAKLTREKKalQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLER 1051
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1052 NKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRA 1131
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1132 KTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQ---HEAMVAALRKKHADS---VAELG 1205
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElksKEKELKKLNEEKKELeekVKDLT 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1206 EQIDNLQRVKQKLEKEKSEFKLEIDDLSS--SMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQT 1283
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 98986453 1284 EAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNAL 1330
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1287-1804 |
8.83e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 8.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1287 ELSRQLEEKES--IVSQLSRSKQAFTQQTEELKRQLEEENKAKnalahalqSSRHDCDLLREQYEEEQEGKAELQRALSK 1364
Cdd:PRK02224 191 QLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1365 ANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANS 1438
Cdd:PRK02224 263 LRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1439 LAAALDKKQRNFDKVLAEWKTKCEESQAELEAS---LKESRS----LSTELFKLKNAYEEALDQLETVKRENKNLEQEIA 1511
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAreaVEDRREeieeLEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1512 DLTEQIAENGKTIHELEKSRKQIE--------------LEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDR-- 1575
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERae 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1576 KIAEKDEEIEQLKRNYQRTVETMQSAlDAEVRSRNEAIRLKKKMEGDLN-EIEIQLSHANRQAAETLKHLRSVqGQLKDT 1654
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAER-RETIEEKRERAEELRERAAELEaEAEEKREAAAEAEEEAEEAREEV-AELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1655 QLHLDDALRGQEDLKEQLAIVERranlLQAEVEELRATLEQ-----TERARKLAEQelldsNERVQllhtqntslihtkk 1729
Cdd:PRK02224 581 LAELKERIESLERIRTLLAAIAD----AEDEIERLREKREAlaelnDERRERLAEK-----RERKR-------------- 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1730 kletdlmQLQSEVEDAS-RDARNAEEKAKKAITDAAMMAEELKKEQDT--------SAHLERMK------KNLEQTVKDL 1794
Cdd:PRK02224 638 -------ELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDlqaeigavENELEELEelrerrEALENRVEAL 710
|
570
....*....|
gi 98986453 1795 QHRLDEAEQL 1804
Cdd:PRK02224 711 EALYDEAEEL 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1227-1886 |
1.48e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1227 LEIDDLSSSMESVSKSKANLEKICRTLEDQLSeargKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSK 1306
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIK----RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1307 Q---AFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQ--RALSKANSEVAQWRTKYEtdai 1381
Cdd:PRK03918 231 KeleELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYL---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1382 QRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVdveranslaaaLDKKQRNFDKVLAEwktkc 1461
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----------LEERHELYEEAKAK----- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1462 eesQAELEASLKESRSLSTElfKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADI 1541
Cdd:PRK03918 371 ---KEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1542 QLALEeaeaaleheeakiLRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRtvetmqsaLDAEVRSRNEAIRLKKKMEg 1621
Cdd:PRK03918 446 TEEHR-------------KELLEEYTAELKRIEKELKEIEEKERKLRKELRE--------LEKVLKKESELIKLKELAE- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1622 DLNEIEIQLSHAN----RQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANllqaEVEELRATLEQte 1697
Cdd:PRK03918 504 QLKELEEKLKKYNleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD----ELEEELAELLK-- 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1698 RARKLAEQELLDSNERVQLLHTQNTSLIhtkkkletdlmqlqsEVEDASRDARNAEEKAKKAITDAAMMAEELkkeQDTS 1777
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEYL---------------ELKDAEKELEREEKELKKLEEELDKAFEEL---AETE 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1778 AHLERMKKNLEQtvkdLQHRLDEAEQlalKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTyQSEE 1857
Cdd:PRK03918 640 KRLEELRKELEE----LEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-KAKK 711
|
650 660
....*....|....*....|....*....
gi 98986453 1858 DRKNVLRLQDLVDKLQVKVKSYKRQAEEA 1886
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1599 |
2.13e-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: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 844 AETEKEMATMKEefqktkdELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:pfam02463 275 KEEEKEKKLQEE-------ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 924 TERAEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEA 1003
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLE----QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1004 HQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKK 1083
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1084 KDFEYCQ--LQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQ 1161
Cdd:pfam02463 504 KARSGLKvlLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1162 IELNKKREAEFLKLRRDLE--EATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESV 1239
Cdd:pfam02463 584 IPKLKLPLKSIAVLEIDPIlnLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSE 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1240 SKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKEsiVSQLSRSKQAFTQQTEELKRQ 1319
Cdd:pfam02463 664 VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE--ELLADRVQEAQDKINEELKLL 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1320 LEEENKAKNALAHALQSSRHDCDLLREqyEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1399
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKEEEKSE--LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1400 DSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERAN----SLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKES 1475
Cdd:pfam02463 820 EQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErleeEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1476 RSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHE 1555
Cdd:pfam02463 900 KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA 979
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 98986453 1556 EAKILRIQLELTQVKSEIDRKIAEKDEEI-EQLKRNYQRTVETMQ 1599
Cdd:pfam02463 980 IEEFEEKEERYNKDELEKERLEEEKKKLIrAIIEETCQRLKEFLE 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
916-1445 |
4.78e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 916 LEAKIKEVTERAE--DEEEINAELT--------AKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSG 985
Cdd:PRK02224 211 LESELAELDEEIEryEEQREQARETrdeadevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 986 LDETIAKLtREKKALQEAHQQALDDLQAEedkvnslnktkskLEQQVEDLESSLEQEkklRVDLERNKRKLEGdlklAQE 1065
Cdd:PRK02224 291 LEEERDDL-LAEAGLDDADAEAVEARREE-------------LEDRDEELRDRLEEC---RVAAQAHNEEAES----LRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1066 SILDLEndkqqldERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDyarele 1145
Cdd:PRK02224 350 DADDLE-------ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE------ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1146 elserleeaggVTSTQIELnKKREAEFLKLRRDLEEATLQHEAMVAALR----------KKHADSVAELGEQIDNLQRVK 1215
Cdd:PRK02224 417 -----------LREERDEL-REREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1216 QKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKIcRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEK 1295
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1296 ESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAhALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTK 1375
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAE 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1376 YETDAIqrtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDK 1445
Cdd:PRK02224 643 FDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
973-1627 |
5.39e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 973 ENKVKNLTE---ELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRV-- 1047
Cdd:PRK03918 161 ENAYKNLGEvikEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEei 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1048 -DLERNKRKLEGDLKlaqesilDLENDKQQLDERLKKKDFEYCQLQSKVEDeqtlglqfQKKIKELQARIEELEEEIEAE 1126
Cdd:PRK03918 241 eELEKELESLEGSKR-------KLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1127 RATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREaeflKLRRDLEEATLQHEAMVAALRKKhadsvaelge 1206
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAKAKK---------- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1207 qiDNLQRVKQKLEKEksefkleiddlsssmesvskskaNLEKICRTLEdqlsEARGKNEEIQRSLSELTTQKSRLQTEAG 1286
Cdd:PRK03918 372 --EELERLKKRLTGL-----------------------TPEKLEKELE----ELEKAKEEIEEEISKITARIGELKKEIK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1287 ELSRQLEEKESIVSQLSRSKQAFtqqTEELKRQLEEENKAKnalahaLQSSRHDCDLLREQYEEEQEGKAELQRALSKaN 1366
Cdd:PRK03918 423 ELKKAIEELKKAKGKCPVCGREL---TEEHRKELLEEYTAE------LKRIEKELKEIEEKERKLRKELRELEKVLKK-E 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1367 SEVAQWRTKYetdaiqrtEELEEAKKKLaqrlqdSEEQVEAVNAKCASLEKTKQR---LQGEVEDLMVDVERANSL---A 1440
Cdd:PRK03918 493 SELIKLKELA--------EQLKELEEKL------KKYNLEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEELkkkL 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1441 AALDKKQRNFDKVLAEWKTKCEE----SQAELEASLKESRSLSTELFKLKNAYEEaldqLETVKRENKNLEQEIADLTEQ 1516
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKE----LEREEKELKKLEEELDKAFEE 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1517 IAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLE-LTQVKSEIDRKIAEKDEEIEQLKRnYQRTV 1595
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEeLEKRREEIKKTLEKLKEELEEREK-AKKEL 713
|
650 660 670
....*....|....*....|....*....|...
gi 98986453 1596 ETMQSALDAEVRSRNEAIRLKKKM-EGDLNEIE 1627
Cdd:PRK03918 714 EKLEKALERVEELREKVKKYKALLkERALSKVG 746
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1196-1920 |
7.09e-14 |
|
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: 77.57 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1196 KHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGK--------NEEI 1267
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDElngelsaaDAAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1268 QRSLSELTT--------QKSRLQTEAGELSR------QLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHa 1333
Cdd:pfam12128 318 AKDRSELEAledqhgafLDADIETAAADQEQlpswqsELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1334 lqssrhdcDLLREQYEEEQEGKAELQRALSKANSEvaqWRTKYEtdaiQRTEELEEAKKKLAQRLQDSEEQVEAVNAKca 1413
Cdd:pfam12128 397 --------DKLAKIREARDRQLAVAEDDLQALESE---LREQLE----AGKLEFNEEEYRLKSRLGELKLRLNQATAT-- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1414 slektkqrlqgevEDLMVDveranslaaaldkkQRNFDkvlaewkTKCEESQAELEASLKESRSLSTELFKLKNAYEEAL 1493
Cdd:pfam12128 460 -------------PELLLQ--------------LENFD-------ERIERAREEQEAANAEVERLQSELRQARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1494 DQLETVKRENKNLEQEIADLTEQ-IAENGKTIHELeksRKQIELEKADIQLAleeaeaaleheeakILRIQLELTQVKSE 1572
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQlFPQAGTLLHFL---RKEAPDWEQSIGKV--------------ISPELLHRTDLDPE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1573 IDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIrlkkkmegdlnEIEIQLSHANRQAAEtlKHLRSVQGQLK 1652
Cdd:pfam12128 569 VWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKA-----------EEALQSAREKQAAAE--EQLVQANGELE 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1653 DTQLHLDDALRGQEDLKEQLaivERRANLLQAEVeelRATLEQTERARKLAEQELLD-SNERVQLLHTQNTSLIHTKKKL 1731
Cdd:pfam12128 636 KASREETFARTALKNARLDL---RRLFDEKQSEK---DKKNKALAERKDSANERLNSlEAQLKQLDKKHQAWLEEQKEQK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1732 ETDLMQLQS---EVEDASRD-------ARNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNLEQTVKDLQH 1796
Cdd:pfam12128 710 REARTEKQAywqVVEGALDAqlallkaAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAV 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1797 RLDEA--------EQLALKGGKKQIQKLETRiRELEfELEGEQKKNTESVKglrkyeRRVKELTYQSEEDRKNVLRLQDL 1868
Cdd:pfam12128 790 RRQEVlryfdwyqETWLQRRPRLATQLSNIE-RAIS-ELQQQLARLIADTK------LRRAKLEMERKASEKQQVRLSEN 861
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1869 VDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQheLEEAEERADIAESQVNK 1920
Cdd:pfam12128 862 LRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ--LEDLKLKRDYLSESVKK 911
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
867-1606 |
1.33e-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: 76.55 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 867 SEAKRKELEEKLVTLvqekndLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLED 946
Cdd:TIGR00618 121 LAAKKSETEEVIHDL------LKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 947 ECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLTEELSGLDETIAKLTREKKALQEAH--QQALDDLQAEEDKVNS 1020
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1021 ----LNKTKSKLEQQVEDLESSLEQEKKLRVDLER---NKRKLEGDLKLAQESILDLENDKQQLD----ERLKKKDFEYC 1089
Cdd:TIGR00618 275 qeavLEETQERINRARKAAPLAAHIKAVTQIEQQAqriHTELQSKMRSRAKLLMKRAAHVKQQSSieeqRRLLQTLHSQE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1090 QLQSKVEDEQTLGL-QFQKKIKELQ---ARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAG--GVTSTQIE 1163
Cdd:TIGR00618 355 IHIRDAHEVATSIReISCQQHTLTQhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGqlAHAKKQQE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1164 LNKKReaefLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE---FKLEIDDLSSSMESVS 1240
Cdd:TIGR00618 435 LQQRY----AELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvlaRLLELQEEPCPLCGSC 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1241 KSKA-------NLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQA---FT 1310
Cdd:TIGR00618 511 IHPNparqdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQ 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1311 QQTEELKRQLEEENKAKNALAhalqssrhdcDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEA 1390
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEDMLA----------CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERV 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1391 KKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLmvdvERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEA 1470
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML----AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1471 -------SLKESRSLS-TELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQ 1542
Cdd:TIGR00618 737 redalnqSLKELMHQArTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1543 LALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEV 1606
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
897-1483 |
1.34e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 897 ENLLDAEERCDQLIKAKFQ-LEAKIKEVTERAEDEEEINAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 975
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 976 VKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEE------DKVNSLNKTKSKLEQQV----------EDLESSL 1039
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeeylDELREIEKRLSRLEEEIngieerikelEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1040 EQEKKLRVDLERNKRKLEGDLKLAQEsILDLENDKQQLDERLKKKDFEycQLQSKVEDEQTLGLQFQKKIKELQARIEEL 1119
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1120 EEEIEAERATRAKTEKQRSDYARELEELSERLEEaggvtstqiELNKKREAEFLKLRRDLEEATLQHEAMVAALRK---- 1195
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK---------ELLEEYTAELKRIEKELKEIEEKERKLRKELRElekv 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1196 -KHADSVAELGEQIDNLQRVKQKLEKEKSEfKLEIDDLSSSMESVSKSKanLEKICRTLEDQLSEArgknEEIQRSLSEL 1274
Cdd:PRK03918 489 lKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIK--LKGEIKSLKKELEKL----EELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1275 TTQKSRLQTEAGELSRQLEEKEsivsqlSRSKQAFTQQTEELKRQLEEENKAKNAlAHALQSSRHDCDLLREQYEEEQEG 1354
Cdd:PRK03918 562 EKKLDELEEELAELLKELEELG------FESVEELEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1355 KAELQRALSKANSEVAQWRTKYETDaiqRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVE 1434
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 98986453 1435 RANSLAAALDKKQRNFDKVlAEWKTKCEesqaelEASLKESRSLSTELF 1483
Cdd:PRK03918 712 ELEKLEKALERVEELREKV-KKYKALLK------ERALSKVGEIASEIF 753
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
850-1706 |
1.50e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 76.55 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 850 MATMKEEFQKTKDELA---KSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLD-AEERCDQLIKAKFQLEAKIKEVTE 925
Cdd:pfam02463 147 IAMMKPERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 926 RAEDEEEINAE----LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQ 1001
Cdd:pfam02463 227 LYLDYLKLNEEridlLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1002 EAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSL-------EQEKKLRVDLERNKRKLEgdlkLAQESILDLENDK 1074
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELkeleikrEAEEEEEEELEKLQEKLE----QLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1075 QQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEA 1154
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1155 GGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSS 1234
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1235 SMESVSKSKANLEKICRTLEDQLSEARGKneeiqRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTE 1314
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALT-----ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1315 ELKRQLEEENKAKnalaHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTK-YETDAIQRTEELEEAKKK 1393
Cdd:pfam02463 618 DDKRAKVVEGILK----DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1394 LAQRLQDSEEQVEAVnakcASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLK 1473
Cdd:pfam02463 694 ILRRQLEIKKKEQRE----KEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1474 ESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALE 1553
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1554 HEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHA 1633
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1634 NRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQE 1706
Cdd:pfam02463 930 LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
866-1579 |
3.33e-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: 75.06 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 866 KSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLE 945
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 946 DEC-------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKV 1018
Cdd:TIGR04523 110 SEIkndkeqkNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1019 NSLNKTKSKLEQQVEDLESSLEQEKKLRVDLErnkrKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDE 1098
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQIS----ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1099 QTlglQFQKKIKELQARIEELEEEIEAERATRAKTEkqrsdyareleelserleeaggvtstqiELNKKREAEFLKlrrd 1178
Cdd:TIGR04523 266 KK---QLSEKQKELEQNNKKIKELEKQLNQLKSEIS----------------------------DLNNQKEQDWNK---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1179 leeatlqheamvaalrkkhadsvaELGEQIDNLQRVKQKLEKEKSEFKLEIDDLsssmesvskskanlekicrtledqls 1258
Cdd:TIGR04523 311 ------------------------ELKSELKNQEKKLEEIQNQISQNNKIISQL-------------------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1259 eargkNEEIqrslSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAF-------TQQTEELKRQLEEENKAKNALA 1331
Cdd:TIGR04523 341 -----NEQI----SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYkqeiknlESQINDLESKIQNQEKLNQQKD 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1332 HALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRLQDSEEQV 1405
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1406 EAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASL--KESRSLSTELF 1483
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIE 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1484 KLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQ 1563
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
730
....*....|....*....
gi 98986453 1564 LELTQVK---SEIDRKIAE 1579
Cdd:TIGR04523 652 ETIKEIRnkwPEIIKKIKE 670
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
847-1640 |
8.84e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 73.93 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEercdqLIKAKFQLEAKIKEVTER 926
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARD-----SLIQSLATRLELDGFERG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 927 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQ 1006
Cdd:TIGR00606 386 PFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1007 A---LDDLQAEEDKVNSLNKTKSKLEQQ--VEDLESSLEQEKKLRVDLERNKRKLEGDL------KLAQESILDLENDKQ 1075
Cdd:TIGR00606 466 LegsSDRILELDQELRKAERELSKAEKNslTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDKM 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1076 QLDERLKKKDF----EYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERL 1151
Cdd:TIGR00606 546 DKDEQIRKIKSrhsdELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1152 EEAGGVTSTQIElnkkrEAEFLKLRRDLEEATLQhEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDD 1231
Cdd:TIGR00606 626 DKLFDVCGSQDE-----ESDLERLKEEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1232 LSSSMESVSKSKANLEKICRTLEDQLSE----ARGKNEEIQRSLSELTTQKSRLQ---TEAGELSRQLEEKE----SIVS 1300
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQkvnRDIQRLKNDIEEQEtllgTIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1301 QLSRSKQAFTQQT--EELKRQLEEENKAKNALAHALQSSrhDCDLLREQYEEEQEGKAELQRALSKA---NSEVAQWRTK 1375
Cdd:TIGR00606 780 EEESAKVCLTDVTimERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKielNRKLIQDQQE 857
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1376 YETDAIQRTEELEEAKKKLAQRLQdseeQVEAVNAKCASLEKTKQRLQGEVEDLMvdvERANSLAAALDKKQRNFDKVLA 1455
Cdd:TIGR00606 858 QIQHLKSKTNELKSEKLQIGTNLQ----RRQQFEEQLVELSTEVQSLIREIKDAK---EQDSPLETFLEKDQQEKEELIS 930
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1456 EWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDqletvkRENKNLEQEIADLTEQIAENGKtihELEKSRKQIE 1535
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD------DYLKQKETELNTVNAQLEECEK---HQEKINEDMR 1001
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1536 LEKADIQLALEEAEAALEHEEAKILRIQL-ELTQVKSEIDRKIAEkdEEIEQLKRNYQRtvetMQSALDAEVRSRNEAIR 1614
Cdd:TIGR00606 1002 LMRQDIDTQKIQERWLQDNLTLRKRENELkEVEEELKQHLKEMGQ--MQVLQMKQEHQK----LEENIDLIKRNHVLALG 1075
|
810 820
....*....|....*....|....*.
gi 98986453 1615 LKKKMEGDLNEIEIQLSHANRQAAET 1640
Cdd:TIGR00606 1076 RQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1177-1872 |
9.42e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1177 RDLEEAtlqHEAMVAALRK--------KHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIddlsssmesvskskanLEK 1248
Cdd:COG4913 235 DDLERA---HEALEDAREQiellepirELAERYAAARERLAELEYLRAALRLWFAQRRLEL----------------LEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1249 ICRTLEDQLSEARGKneeiqrsLSELTTQKSRLQTEAGELSRQLEekesivsqlsrskQAFTQQTEELKRQLEEENKAKN 1328
Cdd:COG4913 296 ELEELRAELARLEAE-------LERLEARLDALREELDELEAQIR-------------GNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1329 ALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQD----- 1400
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealAEAEAALRDLRRELRELEAEIASlerrk 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1401 ---SEEQVEAVNAKCASLEKTKQRL----------------QGEVE--------DLMVDVERANSLAAALDK---KQR-N 1449
Cdd:COG4913 436 sniPARLLALRDALAEALGLDEAELpfvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1450 FDKVlaewktkcEESQAELEASLKESRSLSTELFKLKNAYEEALDQL----------ETVkrenKNLEQEIADLTE--QI 1517
Cdd:COG4913 516 YERV--------RTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvDSP----EELRRHPRAITRagQV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1518 AENGkTIHELEK-------------SRKQIELEKADIQlaleeaeaaleheeakilRIQLELTQVKSEIdRKIAEKDEEI 1584
Cdd:COG4913 584 KGNG-TRHEKDDrrrirsryvlgfdNRAKLAALEAELA------------------ELEEELAEAEERL-EALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1585 EQLKRNYQRTVETMQSALD-----AEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLD 1659
Cdd:COG4913 644 QERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1660 DALRGQEDLKEQLAIVERRANL-LQAEVEELRATLEQTERARKLAEQelldsnervqlLHTQNTSLIHTKKKLETDLMQL 1738
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELREN-----------LEERIDALRARLNRAEEELERA 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1739 QSE--------VEDASRDARNAEEKAKkaitdaamMAEELkKEQDTSAHLERMKKNLEQT----VKDLQHRLDEAEQLAl 1806
Cdd:COG4913 793 MRAfnrewpaeTADLDADLESLPEYLA--------LLDRL-EEDGLPEYEERFKELLNENsiefVADLLSKLRRAIREI- 862
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1807 kggKKQIQKLETRIRELEF------ELEGEQKKNTEsvkgLRKYERRVKELT-----YQSEEDRKNVLRLQDLVDKL 1872
Cdd:COG4913 863 ---KERIDPLNDSLKRIPFgpgrylRLEARPRPDPE----VREFRQELRAVTsgaslFDEELSEARFAALKRLIERL 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1923 |
1.16e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1382 QRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKqrlqGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKC 1461
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1462 EESQaELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE---NGKTIHELEKSRKQIELEK 1538
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1539 ADIQLALEEAEaaleheeaKILRIQLELTQVKSEIdrkiaeKDEEIEQLKRNYQrtvetmqsaldaevrsrnEAIRLKKK 1618
Cdd:PRK03918 355 EELEERHELYE--------EAKAKKEELERLKKRL------TGLTPEKLEKELE------------------ELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1619 MEGDLNEIEIQLSHANRQAAE---TLKHLRSVQGQLKDTQLHLDDALRGQ--EDLKEQLAIVERRANLLQAEVEELRATL 1693
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKElkkAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1694 EQTERarklaeqeLLDSNERVQLLHTQNTSLIHTKKKLETDLMQlqsEVEDASRDARNAEEKAKKAITDAAMMAEELKKE 1773
Cdd:PRK03918 483 RELEK--------VLKKESELIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1774 QDtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEfELEGEQKKNTESVKGLRKYERRVKELTY 1853
Cdd:PRK03918 552 EE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1854 QSEEDRKNVLRLQDLVDKLQVKVKSYKRQ-AEEADEQANAHLTKFRKA----QHELEEAEERADIAESQVNKLRA 1923
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRElaglRAELEELEKRREEIKKTLEKLKE 701
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1386 |
1.85e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKL--VTLVQEKNDLQLQVQAESENLLDAEERcdqLIKAKFQLEA 918
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELRE---IEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 919 KIKEVTERAEDEEEINA---ELTAKKRKLEDECSELKKDIDDLELTLAKVEkekhatenKVKNLTEELSGLdeTIAKLTR 995
Cdd:PRK03918 322 EINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHELYEEAKAKKE--------ELERLKKRLTGL--TPEKLEK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 996 EKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKleGDLKLAQESILDLENDKQ 1075
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1076 QLDERLKKKDFEYCQLQSKVEDEQTLGLQFQ--KKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEE 1153
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1154 aggvtstQIELNKKREAEFLKLRRDLEE--ATLQHEamvaaLRKKHADSVAELGEQIDNLQRVKQK---LEKEKSEFKLE 1228
Cdd:PRK03918 550 -------KLEELKKKLAELEKKLDELEEelAELLKE-----LEELGFESVEELEERLKELEPFYNEyleLKDAEKELERE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1229 IDDLSSSMESVSKSKANLEKIcrtlEDQLSEARGKNEEIQRSLSELTTQKSRLQTEagELSRQLEEKESIVSQLSRSKQA 1308
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAET----EKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAELEELEKRREE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1309 FTQQTEELKRQLEEENKAKNALaHALQSSRHDCDLLREQY-----EEEQEGKAELQRALSKANSEVAQwrTKYETDAIQR 1383
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVKA 768
|
...
gi 98986453 1384 TEE 1386
Cdd:PRK03918 769 EEN 771
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1415-1924 |
2.32e-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: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1415 LEKTKQRLQGEVEDLMVDVERANSLAaalDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALD 1494
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1495 QLETVKrenknleqeiaDLTEQIAENGKTihELEKSRKQIELEKADIQLALEEAEAALEHEEAKILR----IQLELTQVK 1570
Cdd:pfam15921 153 ELEAAK-----------CLKEDMLEDSNT--QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEhdsmSTMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1571 SEIDRKIAEKDEEIEQLKRNYqRTVETMQSALDAEVRSRNEAI--RLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQ 1648
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRI-FPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1649 GQLKDTQlhlddalrgqEDLKEQLAIVERRANLLQAEVEELRATLEQterARKLAEQELLDSNERVQLLHTQntslihtk 1728
Cdd:pfam15921 299 SQLEIIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELRE---AKRMYEDKIEELEKQLVLANSE-------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1729 kkletdLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkg 1808
Cdd:pfam15921 358 ------LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM----- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1809 gkkQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKnvlRLQDLVDKLqvkvkSYKRQAEEADE 1888
Cdd:pfam15921 427 ---EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEEL-----TAKKMTLESSE 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 98986453 1889 QANAHLTKfrkaqhELEEAEERADIAESQVNKLRAK 1924
Cdd:pfam15921 496 RTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
845-1404 |
2.55e-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: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEFQKTKDELaksEAKRKELEEKLVTLVQEKNDLQLQVQAESE-NLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 924 TERAEDE---------------EEINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEELSGL 986
Cdd:pfam15921 305 QEQARNQnsmymrqlsdlestvSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 987 DETIAKltREKKALQEAHQ-------------------QALDDLQAEEDKVNSLNKT-----KSKLEQQVEDLE---SSL 1039
Cdd:pfam15921 383 LADLHK--REKELSLEKEQnkrlwdrdtgnsitidhlrRELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQgknESL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1040 EQEKKLRVDLERNKRKLEG----------DLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEdeqtLGLQFQKKI 1109
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKvveeltakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKLQELQHL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1110 K----ELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNK-----KREAEFLKLRRDLE 1180
Cdd:pfam15921 537 KnegdHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeindrRLELQEFKILKDKK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1181 EATLQH-EAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKAN-------LEKICRT 1252
Cdd:pfam15921 617 DAKIRElEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseeMETTTNK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1253 LEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEK----ESIVSQLSRSKQAFTQQTEELKRQLEEENKAKN 1328
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ 776
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1329 ALAHALQSSRH---DCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQDSEEQ 1404
Cdd:pfam15921 777 ELSTVATEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKELQ 849
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
838-1429 |
3.94e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 838 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLqlqvQAESENLLDAEERCDQLIKAKFQLE 917
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 918 AKIKEVTERAEdeeeinaELTAKKRKLEDECSELKKdiddleltLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREK 997
Cdd:PRK03918 259 EKIRELEERIE-------ELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 998 KALQEahqqALDDLQAEEDKVNSLNKTKSKLEQQVEDLESS---LEQEKKLRVDLERNKRKLEG-DLKLAQESILDLEND 1073
Cdd:PRK03918 324 NGIEE----RIKELEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1074 KQQLDERLKKKDFEYCQLQSKVEDEQTlGLQFQKKIK--------ELQARIEELEEEIEAERATRAKTEKQRSDYARELE 1145
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKK-AIEELKKAKgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1146 ELSErleeaggvtsTQIELNKKREAEFLKLR------RDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLE 1219
Cdd:PRK03918 479 RKEL----------RELEKVLKKESELIKLKelaeqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1220 KEKSEFKLEIDDLSSSMESVSKSKANLEKICRTL----EDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEK 1295
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1296 ESIVSQLSRSKQAFtqqtEELKRQLEEENKAKNalahalqssrhdcdllREQYEEEQEGKAELQRALSKANSEVaqwrtk 1375
Cdd:PRK03918 629 DKAFEELAETEKRL----EELRKELEELEKKYS----------------EEEYEELREEYLELSRELAGLRAEL------ 682
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1376 yetdaiqrtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQgEVEDL 1429
Cdd:PRK03918 683 ---------EELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEEL 726
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1571-1936 |
4.37e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1571 SEIDRKIAEKDEEIEQLKRNYQR---TVETMQSALDAEVRSRNEAIR---LKKKME--------GDLNEIEIQLSHANRQ 1636
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqaLLKEKReyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1637 AAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQL-AIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQ 1715
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1716 LLHTQNTSLIHTKKKLETDLMQLQSEvedasRDARNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNLEQTVKDLQ 1795
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKR-----RDKLTEEYAELKEELED--LRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1796 HRLDEAeQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESvkglrkyERRVKELTYQSEEDRKNVLRLQDLVDKLQVK 1875
Cdd:TIGR02169 399 REINEL-KRELDRLQEELQRLSEELADLNAAIAGIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1876 VksYKRQAEEADEQanahlTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVH 1936
Cdd:TIGR02169 471 L--YDLKEEYDRVE-----KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1413-1802 |
5.62e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1413 ASLEKTKQRLQGEVEDLMVDVERANSLaaaLDKKQRNFDKvLAEWKTKCEESQAeLEASLKEsrslsTELFKLKNAYEEA 1492
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLI---IDEKRQQLER-LRREREKAERYQA-LLKEKRE-----YEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1493 LDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADiqlaleeaeaaleHEEAKILRIQLELTQVKSE 1572
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-------------LGEEEQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1573 I---DRKIAEKDEEIEQLKRNYQrtvetmqsaldaevrsrneairlkkKMEGDLNEIEIQLSHANRQAAETLKHLRSVQG 1649
Cdd:TIGR02169 303 IaslERSIAEKERELEDAEERLA-------------------------KLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1650 QLKDTQLHLddalrgqEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKK 1729
Cdd:TIGR02169 358 EYAELKEEL-------EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1730 KLETDLMQLQSEVEDASRDARNAEEKAKKAitdAAMMAEELKKEQDTSAHLERMKKNLEQtvkdLQHRLDEAE 1802
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKYEQELYDLKEEYDRVEKELSK----LQRELAEAE 496
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
6.62e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 61.68 E-value: 6.62e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 98986453 33 DAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1246-1519 |
7.09e-12 |
|
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: 70.65 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1246 LEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENK 1325
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1326 AKNALAHALQSSRhdcdllreQYEEEQEGKAELQRALSKANSevaqwrtKYETDAI-QRTEELEEAKKKLAQRLQDSEEQ 1404
Cdd:pfam09726 480 ARASAEKQLAEEK--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1405 VEAVNAKCASLEKTKQRlQGEVEDLMvdveraNSLAAALDKKQrnfdkvlaewktkceesqaELEASLKESRSLSTELFk 1484
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ-------------------HLENSLSAETRIKLDLF- 597
|
250 260 270
....*....|....*....|....*....|....*
gi 98986453 1485 lkNAYEEALDQLETVKRENKNLEQEIADLTEQIAE 1519
Cdd:pfam09726 598 --SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1566-1932 |
4.13e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1566 LTQVKSEIDRK---------------IAEKDEEIEQLKRNYQRTVETMQSALD--AEVRSRNEAIrlkKKMEGDLNEIEI 1628
Cdd:PRK02224 189 LDQLKAQIEEKeekdlherlngleseLAELDEEIERYEEQREQARETRDEADEvlEEHEERREEL---ETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1629 QLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQE-DLKEQLAIVERRANLlQAEVEELRATLEQTERARKLAEQEL 1707
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARREEL-EDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1708 LDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDAS----------RDARNAEEKAKKAITDAAMMAEELKKEQDts 1777
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRReeieeleeeiEELRERFGDAPVDLGNAEDFLEELREERD-- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1778 aHLERMKKNLEQTVKDLQHRLDEAEQLaLKGGK---------------------KQIQKLETRIRELEFELEgEQKKNTE 1836
Cdd:PRK02224 423 -ELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVE-EVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1837 SVKGLRKYERRVKELtyqsEEDRKNVlrlQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAES 1916
Cdd:PRK02224 500 RAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
410
....*....|....*.
gi 98986453 1917 QVNKLRAKTRDFTSSR 1932
Cdd:PRK02224 573 EVAELNSKLAELKERI 588
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1724 |
6.20e-11 |
|
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: 67.89 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEmatmkeefqktkdelakseakRKELEEKLvtlvqekNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKAL 1000
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLegDLKLAQESILDLendkQQLDER 1080
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKAISA----RYAEER 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1081 lkkkdfeycqlqskvedeqtlglqfqkkikelqarieeleeeieaeraTRAKTEKqrsdyareleelserleeaggvtst 1160
Cdd:pfam01576 625 ------------------------------------------------DRAEAEA------------------------- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1161 qielnKKREAEFLKLRRDLEEATlqheamvaalrkkhadsvaelgEQIDNLQRVKQKLekeksefKLEIDDLSSSMESVS 1240
Cdd:pfam01576 632 -----REKETRALSLARALEEAL----------------------EAKEELERTNKQL-------RAEMEDLVSSKDDVG 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1241 KSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEekesivsqlsRSKQAFTQQTEELKRQL 1320
Cdd:pfam01576 678 KNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE----------RDLQARDEQGEEKRRQL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1321 EEEnkaknalahalqssrhdcdlLRE-QYEEEQEGKaelQRALSKAnsevaqwrtkyetdaiqrteeleeAKKKLAQRLQ 1399
Cdd:pfam01576 748 VKQ--------------------VRElEAELEDERK---QRAQAVA------------------------AKKKLELDLK 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1400 DSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSlaaaldkkqrnfdkvlaewktkceeSQAELEASLKESRSls 1479
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA-------------------------SRDEILAQSKESEK-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1480 telfKLKNAYEEAL---DQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEE 1556
Cdd:pfam01576 834 ----KLKNLEAELLqlqEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1557 AKILRIQLELTQVKSEI--DRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAirLKKKMEGDLNEIEIQLSHAN 1634
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQLEEQLEQES 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1635 RQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERV 1714
Cdd:pfam01576 988 RERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESN 1067
|
890
....*....|
gi 98986453 1715 QLLHTQNTSL 1724
Cdd:pfam01576 1068 ESMNREVSTL 1077
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1255-1709 |
6.63e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1255 DQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFT--QQTEELKRQLEEENKAKNALAH 1332
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1333 ALQSSRHdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKC 1412
Cdd:COG4717 154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1413 ASLEKTKQRLQ-----GEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKN 1487
Cdd:COG4717 230 EQLENELEAAAleerlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1488 AYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEheeakilriqLELT 1567
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL----------LAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1568 QVKSEID-RKIAEKDEEIEQLKRnyqrTVETMQSALDAEVRSRNEAIRlkkkmEGDLNEIEIQLSHANRQAAETLKHLRS 1646
Cdd:COG4717 380 GVEDEEElRAALEQAEEYQELKE----ELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1647 VQGQLKDTQLHLDDALRGQE--DLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLD 1709
Cdd:COG4717 451 LREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1444-1925 |
9.24e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 9.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1444 DKKQRNFDKVLAEWKTKCEESQAEL---EASLKESRSLSTELFKLKNAYEEALDQLETvkrenknLEQEIADLTEQIAEN 1520
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERREELET-------LEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1521 GKT-------IHELEKSRKQIELEKADIQLALEEAEAALEHeeakilriqleLTQVKSEIDRKIAEKDEEIEQLKRNYQR 1593
Cdd:PRK02224 271 EREreelaeeVRDLRERLEELEEERDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1594 TVETMQSALD--AEVRSRNEAIRLK-KKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKE 1670
Cdd:PRK02224 340 HNEEAESLREdaDDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1671 QLAIVERRANLLQAEVEELRATLEQTER---ARKLAE--QELLDSnERVQLLHTQNTSlihtKKKLETDLMQLQSEVEDa 1745
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEAlleAGKCPEcgQPVEGS-PHVETIEEDRER----VEELEAELEDLEEEVEE- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1746 sRDARNAEekakkaitdaammAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLETRIRELEF 1825
Cdd:PRK02224 494 -VEERLER-------------AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE--------RAEELRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1826 ELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDkLQVKVKSYKRQAE----------EADEQANAHLT 1895
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT-LLAAIADAEDEIErlrekrealaELNDERRERLA 630
|
490 500 510
....*....|....*....|....*....|
gi 98986453 1896 KFRKAQHELEEAEERADIAESQVNKLRAKT 1925
Cdd:PRK02224 631 EKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1344-1920 |
9.77e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1344 LREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNaKCASLEKTKQRLQ 1423
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR-KAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1424 GEVEDLMVDVERANSLAAALDKKQrnfdkvlAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKREN 1503
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARK-------AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1504 KNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEE 1583
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1584 IEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDlneiEIQLSHANRQAAETLKHLRSVQgQLKDTQLHLDDALR 1663
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA----EKKKEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKK 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1664 GQEDLKEQLAiVERRANLLQAEVEELRatleQTERARKLAEQelldsnervqllhtqntslihtKKKLEtdlmqlqsEVE 1743
Cdd:PTZ00121 1406 KADELKKAAA-AKKKADEAKKKAEEKK----KADEAKKKAEE----------------------AKKAD--------EAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1744 DASRDARNAEEKAKKAitDAAMMAEELKKEQDTSAHLERMKKNLEQTVK---------DLQHRLDEAEQLALKGGKKQIQ 1814
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKA--EEAKKADEAKKKAEEAKKADEAKKKAEEAKKkadeakkaaEAKKKADEAKKAEEAKKADEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1815 KLETRIRELEFELEGEQKKNTESVKG--LRKYERRVK-ELTYQSEEDRKNVLRLQDLVDKLQVK---------VKSYKRQ 1882
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEArieevmklyEEEKKMK 1608
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 98986453 1883 AEEA--DEQANAHLTKFRKAQHELEEAEERADIAESQVNK 1920
Cdd:PTZ00121 1609 AEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1344-1923 |
1.76e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1344 LREQYEEEQEgkAELQRALSKANSEVAqwrtkyETDAIqrTEELEEAKKKLAQRLQDSEEqveavnakcaSLEKTKQRLQ 1423
Cdd:PRK02224 192 LKAQIEEKEE--KDLHERLNGLESELA------ELDEE--IERYEEQREQARETRDEADE----------VLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1424 gEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESrslstelfKLKNAYEEAL-DQLETVKRE 1502
Cdd:PRK02224 252 -ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--------GLDDADAEAVeARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1503 NKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEeaeaaleheeakilRIQLELTQVKSEIDR---KIAE 1579
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA--------------ELESELEEAREAVEDrreEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1580 KDEEIEQLKRNYQRTVETMQSALD--AEVRSRNEAIRlkkkmeGDLNEIEIQLSHANRQAAETLKHLRSVQ----GQLKD 1653
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDflEELREERDELR------EREAELEATLRTARERVEEAEALLEAGKcpecGQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1654 TQLHLDDAlrgqEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQ--ELLDSNERV-QLLHTQNTSLIHTKKK 1730
Cdd:PRK02224 463 GSPHVETI----EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLeELIAERRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1731 LETdlmqLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEqTVKDLQHRLDEAEQlalkggk 1810
Cdd:PRK02224 539 AEE----LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAED------- 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1811 kqiqkletRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQ-DLVDKLQVKVKSYKRQAEEADEQ 1889
Cdd:PRK02224 607 --------EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELREERDD 678
|
570 580 590
....*....|....*....|....*....|....
gi 98986453 1890 ANAHLTKFRKAQHELEEAEERADIAESQVNKLRA 1923
Cdd:PRK02224 679 LQAEIGAVENELEELEELRERREALENRVEALEA 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1054-1692 |
2.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1054 RKLEGDLKLAQESILDlenDKQQLDERLKKkdfeycQLQSKVEDEQTLGLQ-FQKKIKELQARIEeleeeieaeratrak 1132
Cdd:PRK02224 168 RERASDARLGVERVLS---DQRGSLDQLKA------QIEEKEEKDLHERLNgLESELAELDEEIE--------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1133 tekqrsdyareleelserleeaggvtstqiELNKKREaeflKLRRDLEEAtlqhEAMVAALRKKHaDSVAELGEQIDNLQ 1212
Cdd:PRK02224 224 ------------------------------RYEEQRE----QARETRDEA----DEVLEEHEERR-EELETLEAEIEDLR 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1213 RVKQKLEKEKSEFKLEIDDLSSSMEsvskskanlekicrTLEDQLSEARGKNEeiqrsLSELTTQKSRLQTEagELSRQL 1292
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLE--------------ELEEERDDLLAEAG-----LDDADAEAVEARRE--ELEDRD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1293 EEKESIVSQLSRSKQAFTQQTEELkrqleeenkaknalahalqssRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQW 1372
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESL---------------------REDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1373 RTkyetdaiqRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVEranSLAAALDKKQRNF-- 1450
Cdd:PRK02224 383 RE--------EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR---TARERVEEAEALLea 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1451 -----------DKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYE---EALDQLETVKRENKNLEQEIADLTEQ 1516
Cdd:PRK02224 452 gkcpecgqpveGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlvEAEDRIERLEERREDLEELIAERRET 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1517 IAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDR--KIAEKDEEIEQLKRNYQRT 1594
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERL 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1595 VETMQ--SALDAEVRSRNEAIRLKKK-MEGDLNEIEIQLSHANRQAAET--------LKHLRSVQGQLKDTQLHLDDALR 1663
Cdd:PRK02224 612 REKREalAELNDERRERLAEKRERKReLEAEFDEARIEEAREDKERAEEyleqveekLDELREERDDLQAEIGAVENELE 691
|
650 660 670
....*....|....*....|....*....|..
gi 98986453 1664 GQEDLKEQLAIVERRANLLQA---EVEELRAT 1692
Cdd:PRK02224 692 ELEELRERREALENRVEALEAlydEAEELESM 723
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1202-1743 |
3.08e-10 |
|
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: 65.15 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1202 AELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRL 1281
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1282 QTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRA 1361
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1362 LSKAnsevaqwrtkyeTDAIQRTEELEeakKKLAQRLQDSEEqVEAVNAKCAS---LEKTKQRLQGEVEDL---MVDVER 1435
Cdd:pfam05557 162 QSSL------------AEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHLnenIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1436 ANSLAAALDKKQRNFDKVLAEwKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTE 1515
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYREE-AATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1516 QiaengktIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRkiaekdeeIEQLKRNYQRTV 1595
Cdd:pfam05557 305 S-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDG--------YRAILESYDKEL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1596 eTMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKdtqlhlddALRGQEDLKEQLAIV 1675
Cdd:pfam05557 370 -TMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--------ALRQQESLADPSYSK 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 1676 ERRANLLQaEVEELRATLEQTERARKLAEQEL--------LDSNERVQLLHTQNTSLIHTKKKLEtDLMQLQSEVE 1743
Cdd:pfam05557 441 EEVDSLRR-KLETLELERQRLREQKNELEMELerrclqgdYDPKKTKVLHLSMNPAAEAYQQRKN-QLEKLQAEIE 514
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1425 |
5.03e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLD-AEERCDQLIKAKFqleaki 920
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEAGL------ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 kevtERAEDEeeinaeltakkrKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKAL 1000
Cdd:PRK02224 305 ----DDADAE------------AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKlaqesilDLENDKQQLDER 1080
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-------ELEATLRTARER 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1081 LKkkdfeycqlqskvEDEQtlgLQFQKKIKELQARIEEleeeieaeratraktekqrsdyareleelserleeaggvtST 1160
Cdd:PRK02224 442 VE-------------EAEA---LLEAGKCPECGQPVEG----------------------------------------SP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1161 QIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKkhADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVS 1240
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1241 KSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSR------QLEEKESIVSQLSRSKQAFTQQTE 1314
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1315 ELKRQLEEENKAKNALAHALQSSRhdcdllreqYEEEQEGKAELQRALSKANSEVAQWRTkyETDAIQRT--------EE 1386
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEAR---------IEEAREDKERAEEYLEQVEEKLDELRE--ERDDLQAEigavenelEE 692
|
570 580 590
....*....|....*....|....*....|....*....
gi 98986453 1387 LEEAKKKLAQrLQDSEEQVEAVNAKCASLEKTKQRLQGE 1425
Cdd:PRK02224 693 LEELRERREA-LENRVEALEALYDEAEELESMYGDLRAE 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
990-1369 |
5.83e-10 |
|
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: 64.69 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 990 IAKLTREKKALQEAHQQALDDLQAE----EDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQE 1065
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKieelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1066 SILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQrsdyarele 1145
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--------- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1146 elserleeaggVTSTQIELNKKREAEfLKLRRDLEEATLQHEAMVAALRKKhADSVAELGEQIDNLQRVKQKLEKEKSEF 1225
Cdd:TIGR02168 812 -----------LTLLNEEAANLRERL-ESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEELESELEAL 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1226 KLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQ-LSR 1304
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEA 958
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1305 SKQAFTQQTEELKRQLEEENKAKNAL---------AHALQSSRHDcdLLREQYEEEQEGKAELQRALSKANSEV 1369
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKERYD--FLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1269 |
6.17e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQA--ESENLLDAEERCDQLIKAK 913
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAkkAEEDKNMALRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 914 fqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDiddlELTLAKVEKEKHATENKVKNLTEELSGLDETIAKL 993
Cdd:PTZ00121 1591 ---EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 994 TREKKALQEAHQQALDDLQAEEDKvnslnktkSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEND 1073
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1074 KQQLDERLKKKDfeycqlQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRS--DYARELEELSERL 1151
Cdd:PTZ00121 1736 KKEAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMevDKKIKDIFDNFAN 1809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1152 EEAGGVTSTQIeLNKKREAEFLKLR---------RDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1222
Cdd:PTZ00121 1810 IIEGGKEGNLV-INDSKEMEDSAIKevadsknmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD 1888
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 98986453 1223 SEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQR 1269
Cdd:PTZ00121 1889 EIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREE 1935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1076 |
6.99e-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: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKAL 1000
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALDDLQAEEDkVNSLNKTKSKLEQQVEDLES-------SLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEND 1073
Cdd:TIGR02169 937 EDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
...
gi 98986453 1074 KQQ 1076
Cdd:TIGR02169 1016 KRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
950-1318 |
1.05e-09 |
|
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: 63.92 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 950 ELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLE 1029
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1030 QQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKI 1109
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1110 KELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLR---RDLEEATLQH 1186
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeelRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1187 EAMVAALRKKHADSVAELGEQidnLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKN-- 1264
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNla 990
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1265 -----EEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQlsRSKQAFTQQTEELKR 1318
Cdd:TIGR02168 991 aieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE--RFKDTFDQVNENFQR 1047
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1187-1596 |
1.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1187 EAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKIcRTLEDQLSEARGKNEE 1266
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1267 IQRsLSELTTQKSRLQTEAGELSRQLEEkesiVSQLSRSKQAFTQQTEELKRQLEEE-NKAKNALAHALQSSRHDCDLLR 1345
Cdd:COG4717 131 YQE-LEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1346 EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQrtEELEEAK---------------------------------- 1391
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARlllliaaallallglggsllsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1392 -------KKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTkcEES 1464
Cdd:COG4717 284 gllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1465 QAELEASLKESRSLsteLFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEK--SRKQIELEKADIQ 1542
Cdd:COG4717 362 ELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1543 LALEEAEAALEHEEAKILRIQLELTQVKSeiDRKIAEKDEEIEQLKRNYQRTVE 1596
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAE 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
847-1393 |
1.75e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.12 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER 926
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 927 AEDEEEINAELTAKKRKLEDECSELKKDIDD-------LELTLAKVEK--EKHAT-ENKVKNLTEELSGLDETIAKLTRE 996
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKiknkllkLELLLSNLKKkiQKNKSlESQISELKKQNNQLKDNIEKKQQE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 997 ----KKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLER-NKRKLEGDLKLAQESILDLE 1071
Cdd:TIGR04523 241 inekTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlNNQKEQDWNKELKSELKNQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1072 NDKQQLDERLKKKDFEYCQLQSKVEdeqtlglQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERL 1151
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1152 EEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMvAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDD 1231
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1232 LsssmesvsksKANLEKICRTLEDQLSEARGKNEEiqrsLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQ 1311
Cdd:TIGR04523 473 L----------SRSINKIKQNLEQKQKELKSKEKE----LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1312 QTEELKRQLEE--ENKAKNALAHALQSSRHDCDLLREQYEE---EQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEE 1386
Cdd:TIGR04523 539 KISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSlkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
....*..
gi 98986453 1387 LEEAKKK 1393
Cdd:TIGR04523 619 LEKAKKE 625
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1278-1905 |
1.83e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.82 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1278 KSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLRE----------Q 1347
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarsaektkK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1348 YEEEQEGK----AELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQ 1423
Cdd:pfam05483 174 YEYEREETrqvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1424 GEVEDLMVDVERANSLAAALDKKQRNFDKVLAEwktkceesqaeleaSLKESRSLSTELFKLKNAYEEALDQLETVKREN 1503
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKE--------------LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1504 KNLEQEIADLTEqiaENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKdEE 1583
Cdd:pfam05483 320 QIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1584 IEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEgdlneieiqlshanrqaaetlkhlrSVQGQLKDTQLHLDDALR 1663
Cdd:pfam05483 396 MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE-------------------------ELKGKEQELIFLLQAREK 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1664 GQEDLKEQLAIVERRANLLQAEVEELRATLEQteraRKLAEQELLDSNERVQL----LHTQNTSLIHTKKKLETDLMQLQ 1739
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAHCDKLLLenkeLTQEASDMTLELKKHQEDIINCK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1740 SEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQD-TSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGG--KKQIQKL 1816
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNnlKKQIENK 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1817 ETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKnvlRLQDLVDKLQVKVKSYKRQAE---EADEQANAH 1893
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISEEkllEEVEKAKAI 683
|
650
....*....|..
gi 98986453 1894 LTKFRKAQHELE 1905
Cdd:pfam05483 684 ADEAVKLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1215-1442 |
2.11e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1215 KQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEE 1294
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1295 KESIVSQLSRSKQAfTQQTEELKRQLEEENkaKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRT 1374
Cdd:COG4942 102 QKEELAELLRALYR-LGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1375 KYETDAIQRtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAA 1442
Cdd:COG4942 179 LLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
853-1519 |
2.61e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.43 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 853 MKEEFQKTKDELAKSEAKRKELEEKLVTLvqeKNDLQLQVQAESENLLDAEercdqliKAKFQLEAKIKEVTERAED-EE 931
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 932 EINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQAL 1008
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1009 DDLQAEEDKVNSLNKTKSKL----EQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKK 1084
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1085 DFEYCQLqSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIEL 1164
Cdd:pfam05483 390 SSELEEM-TKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEH 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1165 NKKREAEflkLRRDLEEATLQHeamvaalrkkhadsvAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKA 1244
Cdd:pfam05483 469 YLKEVED---LKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1245 NLEKICRTLEDQLSEARGKNEEIQRSLselttqksrlqteagelsrqLEEKESIVSQLSRSkqaftqqtEELKRQLEEEN 1324
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEF--------------------IQKGDEVKCKLDKS--------EENARSIEYEV 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1325 KAKNALAHALQSSrhdCDLLREQYEEEQEGKAELQ---RALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDS 1401
Cdd:pfam05483 583 LKKEKQMKILENK---CNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1402 EEQVEAVNAkcaslekTKQRLQGEVEDLMVDVERANSLAAALDKK---------------QRNFDKVLAEWKTKCEESQA 1466
Cdd:pfam05483 660 QKEIEDKKI-------SEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemvalmekhKHQYDKIIEERDSELGLYKN 732
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1467 ELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE 1519
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
840-1107 |
3.06e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.15 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 840 LLKSAETEKEMATMK-----EEFQKTKDELAKSEAKRKE-----LEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQL 909
Cdd:pfam10174 264 LLHTEDREEEIKQMEvykshSKFMKNKIDQLKQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 910 ikakfqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDET 989
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 990 IAKLTREKKALQEAHQQA------LDDLQAEEDKV-NSLNKTKSKLEQQVEDLESSLEQEKKlrvDLERNKRKLEGDLKL 1062
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTdtalttLEEALSEKERIiERLKEQREREDRERLEELESLKKENK---DLKEKVSALQPELTE 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 98986453 1063 AQESILDLENDKQQLDERLKKKDFEYCQL----QSKVEDEQTLGLQFQK 1107
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQLKK 542
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1385-1927 |
3.42e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1385 EELEEAK-KKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKqrnfdkvlaeWKTKCEE 1463
Cdd:TIGR02169 218 KEKREYEgYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK----------IKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1464 SQAELEASLkesRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQL 1543
Cdd:TIGR02169 288 EQLRVKEKI---GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1544 ALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIaekdEEIEQLKRNYQRTVETMQSaLDAEVRSRNEAIrlkKKMEGDL 1623
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLK----REINELKRELDRLQEELQR-LSEELADLNAAI---AGIEAKI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1624 NEIEIQLShanrqaaETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRAT---LEQTERAR 1700
Cdd:TIGR02169 437 NELEEEKE-------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEERVRGG 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1701 KLAEQELLDSNERVqllHTQNTSLIHTKKKLETDLM-----QLQSEVEDASRDARNAEE--KAKKAitdAAMMAEELKKE 1773
Cdd:TIGR02169 510 RAVEEVLKASIQGV---HGTVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIEllKRRKA---GRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1774 QDTSAHLERMKKN-----------------------LEQTVkdLQHRLDEAEQL------------------ALKGG--- 1809
Cdd:TIGR02169 584 RDERRDLSILSEDgvigfavdlvefdpkyepafkyvFGDTL--VVEDIEAARRLmgkyrmvtlegelfeksgAMTGGsra 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1810 -----------KKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVK- 1877
Cdd:TIGR02169 662 prggilfsrsePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEe 741
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1878 -----SYKRQAEEADEQANAHLTK----FRKAQHELEEAEE--RADIAESQVNKLRAKTRD 1927
Cdd:TIGR02169 742 leedlSSLEQEIENVKSELKELEArieeLEEDLHKLEEALNdlEARLSHSRIPEIQAELSK 802
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
848-1352 |
3.42e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAES--ENLLDAEERCDQLIKAKFQLEAKIKEVTE 925
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 926 RAEDEEEINAELTAKKRKLEDECselkkdiddleltlakvEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQ 1005
Cdd:COG4717 161 LEEELEELEAELAELQEELEELL-----------------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1006 QalddlqaeedkvnslnktkskLEQQVEDLESSLEQEKklrvdLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKD 1085
Cdd:COG4717 224 E---------------------LEEELEQLENELEAAA-----LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1086 FEYCQLQSKVedeqTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELN 1165
Cdd:COG4717 278 VLFLVLGLLA----LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1166 KKREAEFLKLRRDLEEATLQheamvAALRKKHADSVAELGEQIDNLQRvKQKLEKEKSEFKLEIDDLS--SSMESVSKSK 1243
Cdd:COG4717 354 REAEELEEELQLEELEQEIA-----ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLgeLEELLEALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1244 ANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEaGELSRQLEEKESIVSQLsrskqaftqqteelkRQLEEE 1323
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAEL---------------RELAEE 491
|
490 500
....*....|....*....|....*....
gi 98986453 1324 NKAKNALAHALQSsrhdcdlLREQYEEEQ 1352
Cdd:COG4717 492 WAALKLALELLEE-------AREEYREER 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
845-1230 |
4.00e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEFQKTKD-------ELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAE------------SENLLDAEER 905
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKqlsekqkELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkelkselknqEKKLEEIQNQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 906 CDQLIKAKFQLEAKI----KEVTERAEDEEEINAELTAKKRKLEDecseLKKDIDDLELTLAKVEKEKHATENKVKNLTE 981
Cdd:TIGR04523 330 ISQNNKIISQLNEQIsqlkKELTNSESENSEKQRELEEKQNEIEK----LKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 982 ELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLK 1061
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1062 LAQES-------ILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQarieeLEEEIEAERATRAKTE 1134
Cdd:TIGR04523 486 QKQKElkskekeLKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE-----DELNKDDFELKKENLE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1135 KQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSvAELGEQIDNLQRV 1214
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN-EKLSSIIKNIKSK 639
|
410
....*....|....*.
gi 98986453 1215 KQKLEKEKSEFKLEID 1230
Cdd:TIGR04523 640 KNKLKQEVKQIKETIK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1468-1936 |
5.91e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1468 LEASL-KESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALE 1546
Cdd:COG4717 47 LLERLeKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1547 EaeaaleheeakilriqLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVEtmqsaLDAEVRSRNEAIRlkkKMEGDLNEI 1626
Cdd:COG4717 127 L----------------LPLYQELEALEAELAELPERLEELEERLEELRE-----LEEELEELEAELA---ELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1627 EIQLSHANRQaaetlkhlrsvqgQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQE 1706
Cdd:COG4717 183 LEQLSLATEE-------------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1707 LLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMK 1784
Cdd:COG4717 250 LLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1785 KNLEQTVKDLQHRLDEAEQLalKGGKKQIQKLETRIRELEFELEGEQ---KKNTESVKGLR----------KYERRVKEL 1851
Cdd:COG4717 330 LPPDLSPEELLELLDRIEEL--QELLREAEELEEELQLEELEQEIAAllaEAGVEDEEELRaaleqaeeyqELKEELEEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1852 TYQSEEDRKNVLRLQDLVDK--LQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIA------ESQVNKLRA 1923
Cdd:COG4717 408 EEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAellqelEELKAELRE 487
|
490
....*....|...
gi 98986453 1924 KTRDFTSSRMVVH 1936
Cdd:COG4717 488 LAEEWAALKLALE 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
915-1300 |
9.37e-09 |
|
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: 60.29 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLT 994
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 995 REKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDK 1074
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1075 QQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYAreleelserlEEA 1154
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1155 GGVTSTQIELNKKreaeflklRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSS 1234
Cdd:pfam07888 265 AQRDRTQAELHQA--------RLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1235 SMESVSKSKANL--EKICRTLedQLSEARGKNEEIQRSLSELTTQKSRLQTEAGEL---SRQLEEKESIVS 1300
Cdd:pfam07888 337 ERMEREKLEVELgrEKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVA 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1314-1924 |
1.55e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1314 EELKRQLEEENKAKNALAHALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQwrTKYETdAIQRTEELEEAKKK 1393
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1394 LAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE-VEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASL 1472
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1473 KESR----SLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLteqiAENGKTI-HELEKSRKQI--ELEKADIQlal 1545
Cdd:COG4913 387 AEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNIpARLLALRDALaeALGLDEAE--- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1546 eeaeaaleheeakiLRIQLELTQVKseidrkiaEKDEE----IEQLKRNYQRT--VEtmqSALDAEVRSRNEAIRLKKKM 1619
Cdd:COG4913 460 --------------LPFVGELIEVR--------PEEERwrgaIERVLGGFALTllVP---PEHYAAALRWVNRLHLRGRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1620 egDLNEIEIQLSHANRQAAETlkhlRSVQGQLkDTQLHlddALRGQedLKEQLAiveRRANLLQAE-VEELRA-----TL 1693
Cdd:COG4913 515 --VYERVRTGLPDPERPRLDP----DSLAGKL-DFKPH---PFRAW--LEAELG---RRFDYVCVDsPEELRRhpraiTR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1694 E-QTERARKLAEQELLDSNERVQLLHTQNTSLIhtkKKLETDLMQLQSEVEDASRDARNAEEKAkkaitdaammaEELKK 1772
Cdd:COG4913 580 AgQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKL---AALEAELAELEEELAEAEERLEALEAEL-----------DALQE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1773 EQDTSAHLERMKKNlEQTVKDLQHRLDEAEQlalkggkkQIQKLET---RIRELEFELEGEQKKNTESVKGLRKYERRVK 1849
Cdd:COG4913 646 RREALQRLAEYSWD-EIDVASAEREIAELEA--------ELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIG 716
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1850 ELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEAD----EQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaaaLGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1423-1924 |
1.75e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1423 QGEVEDLMVDVERANSLAaaldKKQRNFDKVLAEWKtKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRE 1502
Cdd:PRK03918 134 QGEIDAILESDESREKVV----RQILGLDDYENAYK-NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1503 NKNLEQEIADLTEQIAENGKTIHELEKSRKqiELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDE 1582
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKE--EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1583 EIEQLKRNYQRTVETMQSALDAEvrsrNEAIRLKKKMEGDLNEIEIQLSHANRQAAEtLKHLRSVQGQLKDTQLHLDDAL 1662
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDEL----REIEKRLSRLEEEINGIEERIKELEEKEER-LEELKKKLKELEKRLEELEERH 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1663 RGQEDLKEQLAIVER-RANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKL---------- 1731
Cdd:PRK03918 362 ELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvc 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1732 -----ETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQtVKDLQHRLDEAEQLAL 1806
Cdd:PRK03918 442 greltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1807 KGGKKQIQKLETRIRELEFELEGeQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRlqDLVDKLQVKVKSYKRQAEEA 1886
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLK--ELEELGFESVEELEERLKEL 597
|
490 500 510
....*....|....*....|....*....|....*...
gi 98986453 1887 DEQANAHLtKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:PRK03918 598 EPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEE 634
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1379-1706 |
1.91e-08 |
|
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: 59.70 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1379 DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLmvdvERANSLAAalDKKQRNFDKVLAEWK 1458
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA----ERYQALLK--EKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1459 ---TKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNL--------EQEIADLTEQIAENGKTIHEL 1527
Cdd:TIGR02169 234 aleRQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1528 EKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDE---EIEQLKRNYQRTVE---TMQSA 1601
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEFAETRDelkDYREK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1602 LDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANL 1681
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340
....*....|....*....|....*
gi 98986453 1682 LQAEVEELRAtlEQTERARKLAEQE 1706
Cdd:TIGR02169 474 LKEEYDRVEK--ELSKLQRELAEAE 496
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
848-1113 |
1.95e-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: 59.74 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKakfQLEAKIKEVTERA 927
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK---QIENLEEKEMNLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 928 EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQA 1007
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1008 LDDLQAEEDKVNSLN----KTKSKLEQQVEDLESSLE----QEKKLRVDLERNKRKLEGDLKLAQ-----------ESIL 1068
Cdd:pfam05483 628 NKQLNAYEIKVNKLElelaSAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKeidkrcqhkiaEMVA 707
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 98986453 1069 DLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:pfam05483 708 LMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIK 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1255-1471 |
3.14e-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: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1255 DQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHAL 1334
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1335 QSSRHD-CDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQDSE 1402
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1403 EQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAS 1471
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
893-1513 |
4.53e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 893 QAESENLLDAEERCDQ-LIKAKFQLeAKIKEVTERAEDEEeinaelTAKKRKLEDE---CSELKKDIDDleltlaKVEKE 968
Cdd:PRK02224 137 QGEVNKLINATPSDRQdMIDDLLQL-GKLEEYRERASDAR------LGVERVLSDQrgsLDQLKAQIEE------KEEKD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 969 KHATENKvknLTEELSGLDETI---------AKLTREKKALQ-EAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESS 1038
Cdd:PRK02224 204 LHERLNG---LESELAELDEEIeryeeqreqARETRDEADEVlEEHEERREELETLEAEIEDLRETIAETEREREELAEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1039 LEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKkkdfeycQLQSKVEDEQTLGLQFQKKIKELqariee 1118
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDE-------ELRDRLEECRVAAQAHNEEAESL------ 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1119 leEEIEAERATRAKTEKQRSDyareleelserlEEAGGVTSTQIELNKKREAeflklRRDLEEAtlqheamVAALRKKHA 1198
Cdd:PRK02224 348 --REDADDLEERAEELREEAA------------ELESELEEAREAVEDRREE-----IEELEEE-------IEELRERFG 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1199 DSvaelGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKI-----CRTLE---------DQLSEARGKN 1264
Cdd:PRK02224 402 DA----PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagkCPECGqpvegsphvETIEEDRERV 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1265 EEIQRSLSELTTQKSRLQ------TEAGELSRQ---LEEKESIVSQLSRSKQAFTQQTEElkrQLEEENKAKNALAHALQ 1335
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEerleraEDLVEAEDRierLEERREDLEELIAERRETIEEKRE---RAEELRERAAELEAEAE 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1336 SSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiqRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASL 1415
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA--AIADAEDEIERLREKREALAELNDERRERLAEK 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1416 EKTKQRLQGEVEDlmvdveraNSLAAALDKKQRnfdkvlaewktkCEESQAELEASLKESRSLSTELFKLKNAYEEALDQ 1495
Cdd:PRK02224 633 RERKRELEAEFDE--------ARIEEAREDKER------------AEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
650
....*....|....*...
gi 98986453 1496 LETVKRENKNLEQEIADL 1513
Cdd:PRK02224 693 LEELRERREALENRVEAL 710
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1212-1910 |
5.25e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.52 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1212 QRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQ 1291
Cdd:TIGR00606 362 HIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1292 LEEKESI----VSQLSRSKQAFTQQTEELKRQLEEEN---KAKNALAHALQSSRHDCDLLREQYEeeQEGKAELQRALSK 1364
Cdd:TIGR00606 442 IELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQelrKAERELSKAEKNSLTETLKKEVKSL--QNEKADLDRKLRK 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1365 ANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCAS-------LEKTKQRLQGEVEDLMVDVERAN 1437
Cdd:TIGR00606 520 LDQEMEQ--LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGyfpnkkqLEDWLHSKSKEINQTRDRLAKLN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1438 SLAAALDKKQRNFDKVLaEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQI 1517
Cdd:TIGR00606 598 KELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1518 AENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQV-------KSEIDRKIAEKDE-------- 1582
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPElrnklqkv 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1583 --EIEQLKRNYQRT---VETMQSALD-AEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQL 1656
Cdd:TIGR00606 757 nrDIQRLKNDIEEQetlLGTIMPEEEsAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1657 HLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATL----EQTERARKLAEQELLDSNErVQLLHTQNTSLIHTKKKLE 1732
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKlqigTNLQRRQQFEEQLVELSTE-VQSLIREIKDAKEQDSPLE 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1733 TDLMQLQSEVEDAsrdARNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNLEQTVKDLQHRLDEAEQl 1804
Cdd:TIGR00606 916 TFLEKDQQEKEEL---ISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK- 991
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1805 alkgGKKQIQKlETRIRELEFELEGEQKKNTESVKGLRKYERRVKEL-----TYQSEEDRKNVLRLQDLVDKLQVKVKSY 1879
Cdd:TIGR00606 992 ----HQEKINE-DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEMGQMQVLQMKQEHQKLEENIDLI 1066
|
730 740 750
....*....|....*....|....*....|.
gi 98986453 1880 KRQAEEADEQANAHLTKFRKAQHELEEAEER 1910
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1385-1939 |
6.16e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1385 EELEEAKkklaQRLQDSEEQVEA---VNAKCASLEKTKQRLQG-EVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTK 1460
Cdd:COG4913 235 DDLERAH----EALEDAREQIELlepIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1461 CEESQAELEAslkesrsLSTELFKLKNAYEEA-LDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKA 1539
Cdd:COG4913 311 LERLEARLDA-------LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1540 DIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKR---NYQRTVETMQSALDAEVRSRNEAIRLK 1616
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPARLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1617 kkmeGDLneIEIQLSHAN-RQAAETlkhlrsvqgqlkdtqlhlddALRGQ--------EDLKEQLAIVERRAnllqaeve 1687
Cdd:COG4913 464 ----GEL--IEVRPEEERwRGAIER--------------------VLGGFaltllvppEHYAAALRWVNRLH-------- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1688 eLRATLeQTERARKLAEQELLDSNERVQLLHtqntslihtkkKLETDLMQLQSEVED--ASRDA----RNAEE--KAKKA 1759
Cdd:COG4913 510 -LRGRL-VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAelGRRFDyvcvDSPEElrRHPRA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1760 ITDAAMMaeelkkeqdtsahlermKKNLEQTVKDLQHRLDE--------AEQLALKggKKQIQKLETRIRELEFELEgeq 1831
Cdd:COG4913 577 ITRAGQV-----------------KGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLE--- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1832 kKNTESVKGLRKYERRVKELTYQSEED------RKNVLRLQDLVDKL---QVKVKSYKRQAEEADEQANAHLTKFRKAQH 1902
Cdd:COG4913 635 -ALEAELDALQERREALQRLAEYSWDEidvasaEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKG 713
|
570 580 590
....*....|....*....|....*....|....*..
gi 98986453 1903 ELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESE 1939
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
888-1113 |
6.56e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 888 LQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK 967
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 968 EKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKtksKLEQQVEDLESSLEQEKKLRV 1047
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP---ARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1048 DLERNKRKLEGDLKLAQESILDLE---NDKQQLDERLKKKDFEY-CQLQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEalkAERQKLLARLEKELAELaAELAELQQEAEELEALIARLEAEAA 237
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1320-1828 |
6.88e-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: 57.39 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1320 LEEENKAKNALAHAlqssrhdCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEeaKKKLAQRLQ 1399
Cdd:pfam05622 2 LSEAQEEKDELAQR-------CHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLL--LQKQLEQLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1400 DSEEQVEA----VNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVlaewktkceesqAELEASLKes 1475
Cdd:pfam05622 73 EENFRLETarddYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKV------------KKLEATVE-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1476 rslstelfklknAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHE 1555
Cdd:pfam05622 139 ------------TYKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1556 EA---KILRIQLELTQVKSEIDRKIAEKD---EEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQ 1629
Cdd:pfam05622 207 DKlefEYKKLEEKLEALQKEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1630 LSHANRqaAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLeqterarklaeqelld 1709
Cdd:pfam05622 287 LQHENK--MLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKAL---------------- 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1710 snervQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMK 1784
Cdd:pfam05622 349 -----QEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYK 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 98986453 1785 KNLEQ---TVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELE 1828
Cdd:pfam05622 424 KYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1278-1698 |
7.73e-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: 57.21 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1278 KSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE 1357
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1358 L---QRALSKANSEvaqwrtkyetdAIQRTEELEEAKKKLAQRLQDSEeqveavnakcASLEKTKQRlqgevedlmvdVE 1434
Cdd:pfam07888 113 LseeKDALLAQRAA-----------HEARIRELEEDIKTLTQRVLERE----------TELERMKER-----------AK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1435 RANSLaaaldkkqrnfdkvLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLT 1514
Cdd:pfam07888 161 KAGAQ--------------RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1515 EQIAENGKTIHELEKSRKQIELEkadiqlaleeaeaaleheeakilriQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRT 1594
Cdd:pfam07888 227 RKEAENEALLEELRSLQERLNAS-------------------------ERKVEGLGEELSSMAAQRDRTQAELHQARLQA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1595 VETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQ-------------GQLKDTQL-HLDD 1660
Cdd:pfam07888 282 AQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQeermereklevelGREKDCNRvQLSE 361
|
410 420 430
....*....|....*....|....*....|....*...
gi 98986453 1661 ALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTER 1698
Cdd:pfam07888 362 SRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1384-1940 |
8.67e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1384 TEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKvLAEWKTKCEE 1463
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1464 SQAELEASLKESRSLSTELFKlknayEEALDQLETVKRENKNLEQEIADLTEQI--AENGKTIHELEKS----RKQIELE 1537
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRK-----AEELRKAEDARKAEAARKAEEERKAEEArkAEDAKKAEAVKKAeeakKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1538 KADIQLALEEAEAALEHEEAKILRIQlelTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRS--RNEAIRL 1615
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQ---AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1616 KKKMEgdlnEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRatleQ 1695
Cdd:PTZ00121 1321 KKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK----K 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1696 TERARKLAEQELLDSNErVQLLHTQNTSLIHTKKKLETdlMQLQSEVEDASRDARNAEEKAKKAitDAAMMAEELKKEQD 1775
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1776 TSAHLERMKKNLEQTVKdlqhrLDEAEQLALKGGKK--QIQKLETRIRELEFELEGEQKKNTESVKglRKYERRVKELTY 1853
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAK--KAEEAKKADEAK 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1854 QSEEDRKnvlrLQDLVDKLQVKVKSYKRQAEEAdeqanahltkfrkaqhelEEAEERADIAESQVNKLRAKTRDFTSSRM 1933
Cdd:PTZ00121 1541 KAEEKKK----ADELKKAEELKKAEEKKKAEEA------------------KKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
....*..
gi 98986453 1934 VVHESEE 1940
Cdd:PTZ00121 1599 KLYEEEK 1605
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
915-1141 |
8.99e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDEcselkkdIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLT 994
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 995 REKKALQEAHQQALDDLQaeedKVNSLNKTKSKLEQQ-VEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEND 1073
Cdd:COG4942 97 AELEAQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1074 KQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYA 1141
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
855-1404 |
1.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 855 EEFQKTKDELAKSEAKRKELEekLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER-----AED 929
Cdd:COG4913 262 ERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 930 EEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQ 1006
Cdd:COG4913 340 LEQLEREIERLERELEErerRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1007 ALDDLQAEedkVNSLNKTKSKLEQQVEDLESSLEQEKKLRVD---------------------LER-------------- 1051
Cdd:COG4913 420 ELRELEAE---IASLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlggfaltllvppe 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1052 ---------NKRKLEGDL-----KLAQESILDLENDKQQLDERLKKKDFEY-----CQLQS-----KVEDEQTLGlQFQK 1107
Cdd:COG4913 497 hyaaalrwvNRLHLRGRLvyervRTGLPDPERPRLDPDSLAGKLDFKPHPFrawleAELGRrfdyvCVDSPEELR-RHPR 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1108 KIkelqarieeleeeieaeraTRAKTEKQRSD-YARELEELSERLEEAGGVTSTQIELNKKR----EAEFLKLRRDLEEA 1182
Cdd:COG4913 576 AI-------------------TRAGQVKGNGTrHEKDDRRRIRSRYVLGFDNRAKLAALEAElaelEEELAEAEERLEAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1183 TLQHEAMVAalRKKHADSVAELGEQIDNLQRVK---QKLEKEKSEFKLEIDDLsssmesvskskanlekicRTLEDQLSE 1259
Cdd:COG4913 637 EAELDALQE--RREALQRLAEYSWDEIDVASAEreiAELEAELERLDASSDDL------------------AALEEQLEE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1260 ARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAftQQTEELKRQLEEENKAK--NALAHALQSS 1337
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAveRELRENLEER 774
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1338 RHDCDLLREQYEEEQEGKaeLQRALSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQDSEEQ 1404
Cdd:COG4913 775 IDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
832-1505 |
1.07e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 57.36 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 832 KLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSE--AKRKELEEKLVTLVQEKNDLQLQVQAESENL------LDAE 903
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 904 ERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 976
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 977 KNLTEELSGLDETI----------AKLTREKKALQEAHQQalddLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLR 1046
Cdd:TIGR00606 615 ESKEEQLSSYEDKLfdvcgsqdeeSDLERLKEEIEKSSKQ----RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1047 VDLERNKRKLEGDLKLAQESILDLENDkqqlderLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAE 1126
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESE-------LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1127 RATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELnKKREAEFLKLRRDLEEATLqhEAMVAALRKKHADSVAEL-- 1204
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdt 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1205 -GEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKicrtLEDQLSEargKNEEIQRSLSELTTQKSRLQT 1283
Cdd:TIGR00606 841 vVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ----FEEQLVE---LSTEVQSLIREIKDAKEQDSP 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1284 EAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSrhdCDLLREQYEEEQEGKA----ELQ 1359
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLKQKETELNTVNaqleECE 990
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1360 RALSKANSEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQDSEEQveavnaKCASLEKTKQRLQGEVE 1427
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQM------QVLQMKQEHQKLEENID 1064
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1428 DLMVDVERANSLAAALDKKQRNFDKVLAEWKTK-CEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKN 1505
Cdd:TIGR00606 1065 LIKRNHVLALGRQKGYEKEIKHFKKELREPQFRdAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
863-1039 |
1.07e-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: 54.93 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 863 ELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER-AEDEEEINAELTAKk 941
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 942 rkledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVnsl 1021
Cdd:COG1579 90 -----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL--- 161
|
170
....*....|....*...
gi 98986453 1022 nktKSKLEQQVEDLESSL 1039
Cdd:COG1579 162 ---EAEREELAAKIPPEL 176
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
845-1331 |
1.09e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQlqvQAESENLLDAEERCDQLIKAKFQLEAKIK--- 921
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM---KIINDPVYKNRNYINDYFKYKNDIENKKQils 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 922 ----------EVTERAEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDE 988
Cdd:PRK01156 316 nidaeinkyhAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 989 TIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSL------------------EQEKKLRVDLE 1050
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgeEKSNHIINHYN 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1051 RNKRKLEGDLKLAQESILDLENDKQQL---DERLKKKDF-EYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEeieae 1126
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLkkrKEYLESEEInKSINEYNKIESARADLEDIKIKINELKDKHDKYEE----- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1127 ratrAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATlqheamvaalrkkhadsvaelGE 1206
Cdd:PRK01156 551 ----IKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRL---------------------QE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1207 QIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKnEEIQRSLSELTTQKSRLQTEAG 1286
Cdd:PRK01156 606 IEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDNLK 684
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1287 ELSRQLE-------EKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALA 1331
Cdd:PRK01156 685 KSRKALDdakanraRLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1508 |
1.26e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEfQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLdaEERCDQLIKAKFQLEAKIKEVT 924
Cdd:COG4913 239 RAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 925 ERAEDEEEINAELTAKKRKLE-DECSELKKDIDDLELTLAKVEkekhateNKVKNLTEELSGLDETIAKLTREKKALQEA 1003
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERE-------RRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1004 HQQALDDLQAEEDKvnsLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESIldlendKQQLDERLKK 1083
Cdd:COG4913 389 AAALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL------AEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1084 KDF--EYCQLQSKVED-----EQTLG-------------LQFQKKIKELQarieeleeeieaeRATRAKTEKQRSDYARE 1143
Cdd:COG4913 460 LPFvgELIEVRPEEERwrgaiERVLGgfaltllvppehyAAALRWVNRLH-------------LRGRLVYERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1144 LEELSERLEEAGGVTStqielnkkREAEFlklrRDLEEATLQHEAMVAAlrkkhADSVAElgeqidnLQRVKQKLEKE-- 1221
Cdd:COG4913 527 ERPRLDPDSLAGKLDF--------KPHPF----RAWLEAELGRRFDYVC-----VDSPEE-------LRRHPRAITRAgq 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1222 -KSEFKL-EIDDLSSSMESV------SKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQT---------E 1284
Cdd:COG4913 583 vKGNGTRhEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiD 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1285 AGELSRQLEEKESIVSQLSRSKQAFtqqtEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSK 1364
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1365 ANSEVAQWRTkYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCAS-LEKT----KQRLQGEVEDLMVDVERANSL 1439
Cdd:COG4913 739 AEDLARLELR-ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEeLERAmrafNREWPAETADLDADLESLPEY 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1440 AAALDKKQRNfdkVLAEWKTKCEESQAELeaslkESRSLSTELFKLKNAYEEALDQLETVkreNKNLEQ 1508
Cdd:COG4913 818 LALLDRLEED---GLPEYEERFKELLNEN-----SIEFVADLLSKLRRAIREIKERIDPL---NDSLKR 875
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
841-1078 |
1.41e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLvqeknDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 921 KEVTERAEDEEEINAELTAkkrklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEELSGLdetiakltreKK 998
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 999 ALQEAHQQALDDLQAEedkVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERnkrkLEGDLKLAQESILDLENDKQQLD 1078
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1263-1873 |
2.01e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1263 KNEEIQRSLSELTTQKSRL---QTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRH 1339
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1340 DCDLLREQYEEEQEGKAELQRALSKANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTK 1419
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENK--------KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1420 QRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWkTKCEESQAELEASLKEsrsLSTELFKLKNAYEEALDQLETV 1499
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI-SELKKQNNQLKDNIEK---KQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1500 KRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKilRIQLELTQVKSEID---RK 1576
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK--NQEKKLEEIQNQISqnnKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1577 IAEKDEEIEQLKRNYQrTVETMQSALDAEVRSRNEAIR-LKKKMEGDLNEI---EIQLSHANRQAAETLKHLRSVQGQLK 1652
Cdd:TIGR04523 337 ISQLNEQISQLKKELT-NSESENSEKQRELEEKQNEIEkLKKENQSYKQEIknlESQINDLESKIQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1653 DTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELldsnervQLLHTQNTSLIHTKKKLE 1732
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL-------KVLSRSINKIKQNLEQKQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1733 TDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKeqdtsahLERMKKNLEQTVKDLQHRLDEAEQ-LALKGGKK 1811
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK-------LESEKKEKESKISDLEDELNKDDFeLKKENLEK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1812 QIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQ 1873
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1256-1851 |
2.25e-07 |
|
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: 55.91 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1256 QLSEARGKNEEIqRSLSELT-TQKSRLQTEAGELS-----------------------------------RQLEEKESI- 1298
Cdd:pfam07111 71 QLQELRRLEEEV-RLLRETSlQQKMRLEAQAMELDalavaekagqaeaeglraalagaemvrknleegsqRELEEIQRLh 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1299 VSQLSRSKQAFTQQTEELKRQLEEENKAKNAL-------AHALQSSRHDCDLLREQY---EEEQEGKAELQRALSKANSE 1368
Cdd:pfam07111 150 QEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLsktQEELEAQVTLVESLRKYVGE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1369 VAQWRTKYETDAIQRtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLektKQRLQGEVEDLMVDVERANSLAAALDKKQR 1448
Cdd:pfam07111 230 QVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATVELLQVRVQSL---THMLALQEEELTRKIQPSDSLEPEFPKKCR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1449 NfdkVLAEWKTKCEESQAELEASLKESRSlstelfklknayeealdqletvkrENKNLEQEIADLTEQIAENGKtihele 1528
Cdd:pfam07111 306 S---LLNRWREKVFALMVQLKAQDLEHRD------------------------SVKQLRGQVAELQEQVTSQSQ------ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1529 ksrkqielEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRnYQRTVETMQSALDAEVRS 1608
Cdd:pfam07111 353 --------EQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1609 RNEAIrlkkkmeGDLNEIEIQLSHANRQaAETLKHLRSVQGQLKDTQLHL----DDALRGQEDLKEQLAIVERRANLLQA 1684
Cdd:pfam07111 424 VEQAV-------ARIPSLSNRLSYAVRK-VHTIKGLMARKVALAQLRQEScpppPPAPPVDADLSLELEQLREERNRLDA 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1685 EVeELRATLEQTE--RARKLAEQELLDSNERVQllhtqntslihtkkKLETDLMQLQSEVEDASRDARNAEEKAKKAITD 1762
Cdd:pfam07111 496 EL-QLSAHLIQQEvgRAREQGEAERQQLSEVAQ--------------QLEQELQRAQESLASVGQQLEVARQGQQESTEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1763 AAMMAEELKKEQDTSAH-----LERMKKNLEQTVKDLQHRLDEA--EQLALKGGKKQIQKLETRIRELEFELEGEQKKNT 1835
Cdd:pfam07111 561 AASLRQELTQQQEIYGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHRATQEKERNQELRRLQDEAR 640
|
650
....*....|....*.
gi 98986453 1836 ESVKglRKYERRVKEL 1851
Cdd:pfam07111 641 KEEG--QRLARRVQEL 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1594-1824 |
2.28e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1594 TVETMQSALDAEVRSRNEAIRLKKKMEgDLNEIEiqlshANRQAAETLKHLRSVQGQLKDTqLHLDDALRGQEDLKEQLA 1673
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIE-LLEPIR-----ELAERYAAARERLAELEYLRAA-LRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1674 IVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERvqllhtqntslihTKKKLETDLMQLQSEVEDASRDARNAE 1753
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-------------RLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1754 EKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLETRIRELE 1824
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALR---AEAAALLEALEEELEALEEALAEAEA-ALRDLRRELRELEAEIASLE 432
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1350-1910 |
2.49e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1350 EEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK---------------------KLAQRLQDSEEQVEAV 1408
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieaqrkaiqelqfenekvslKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1409 NAK---CASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEaslkesrslstelFKL 1485
Cdd:pfam05483 151 NATrhlCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH-------------FKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1486 KNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHE----LEKSRKQIEL--EKADIQLALEEAEAALEHEEAKI 1559
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltflLEESRDKANQleEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1560 LR-IQLEL-----TQVKSEIDRKIAEK-------DEEIEQLKRNYQRTVETM-QSALDAEVRSRNEAIRLKK----KMEG 1621
Cdd:pfam05483 298 LEdIKMSLqrsmsTQKALEEDLQIATKticqlteEKEAQMEELNKAKAAHSFvVTEFEATTCSLEELLRTEQqrleKNED 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1622 DLNEIEIQLSHANRQAAETLKHLRSVQGQLKDtqlhLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERark 1701
Cdd:pfam05483 378 QLKIITMELQKKSSELEEMTKFKNNKEVELEE----LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK--- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1702 laeqELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQD----TS 1777
Cdd:pfam05483 451 ----EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEdiinCK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1778 AHLERMKKNLEQTVKDLQHRLDEAEQLAlkggkkqiQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEE 1857
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVR--------EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1858 DRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEER 1910
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
840-1113 |
2.69e-07 |
|
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: 55.89 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 840 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLqlqVQAESENLL---DAEERCDQLikakfql 916
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRavkDIKQERDQL------- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 917 eakIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlteeLSGLDETIAKLTRE 996
Cdd:pfam15921 659 ---LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMG 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 997 KKALQEAHQQALDDLQAE----EDKVNSLNKTKSKLEQQVEDLESSLEQekklrVDLERNkrKLEGDLKLAQESILDLEN 1072
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKiqflEEAMTNANKEKHFLKEEKNKLSQELST-----VATEKN--KMAGELEVLRSQERRLKE 804
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 98986453 1073 DKQQLDERLKKKDFEY--CQ--LQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:pfam15921 805 KVANMEVALDKASLQFaeCQdiIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1346-1583 |
3.29e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1346 EQYEEEQEGKAELQRALSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE 1425
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1426 VEDLMVDVerANSLAAALDKKQRNFDKVLAEwktkcEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKREnkn 1505
Cdd:COG4942 99 LEAQKEEL--AELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE--- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1506 LEQEIADLTEQIAENGKTIHELEKSRKqielEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEE 1583
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
847-1760 |
3.33e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.82 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQlqvqaesenllDAEERCDQLIKAKFQLEAKIKEVTER 926
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK-----------ALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 927 AEDE-EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIakLTREKKALQEAHQ 1005
Cdd:TIGR00606 299 TDEQlNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI--RARDSLIQSLATR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1006 QALDDLQAEEDkvnSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRklegdlkLAQESILDLENDKQQLDERLKKKd 1085
Cdd:TIGR00606 377 LELDGFERGPF---SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKER-------LKQEQADEIRDEKKGLGRTIELK- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1086 feycqlQSKVEDEQTlglQFQKKIKELQARIEELEEEIEAERATRaKTEKQRSDYAReleelserleeaggvtSTQIELN 1165
Cdd:TIGR00606 446 ------KEILEKKQE---ELKFVIKELQQLEGSSDRILELDQELR-KAERELSKAEK----------------NSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1166 KKREAEFLKLRRDLEEaTLQHEAMVAALRKKHADSVaelgEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKAN 1245
Cdd:TIGR00606 500 KKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTR----TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1246 LEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSrSKQAFTQQTEELKRQLEEENK 1325
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-GSQDEESDLERLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1326 AKNALAHALQssrhdcdlLREQYEEEQEGKaelqralSKANSEVAQwrtkyetDAIQRTEELEEAKKKLAQRLQDSEEQV 1405
Cdd:TIGR00606 654 QRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEFISDLQSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1406 EAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELE---ASLKESRSLSTEL 1482
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESAKVCLTDV 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1483 FKLKNAYEEaldqletVKRENKNLEQEIADLteQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRI 1562
Cdd:TIGR00606 792 TIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1563 QLELTQVKSEiDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLK 1642
Cdd:TIGR00606 863 KSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1643 HLRSVQGQLKDTQLHLDDALRGQEDLKE-QLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQN 1721
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNL 1021
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 98986453 1722 TSLIHTK--KKLETDLMQLQSEV-EDASRDARNAEEKAKKAI 1760
Cdd:TIGR00606 1022 TLRKRENelKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1039-1322 |
3.59e-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: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1039 LEQE-KKLRVDLERNkRKLEGDLKLAQESILDLE----NDKQQLderlkKKDFEYCQ------LQSKVEDEQTLGlQFQK 1107
Cdd:pfam09726 400 LEQDiKKLKAELQAS-RQTEQELRSQISSLTSLErslkSELGQL-----RQENDLLQtklhnaVSAKQKDKQTVQ-QLEK 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1108 KIKELQArieeleeeieaeraTRAKTEKQrsdyareleelserleeaggvtstqieLNKKREaeflklRRDLEEATLQHE 1187
Cdd:pfam09726 473 RLKAEQE--------------ARASAEKQ---------------------------LAEEKK------RKKEEEATAARA 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1188 AMVAAlrkkhadsvAELGEQIDNLQRVKQKLEKE----KSEFKL---EIDDLSSSMESVSKSKANlEKICRTLEDQLSEA 1260
Cdd:pfam09726 506 VALAA---------ASRGECTESLKQRKRELESEikklTHDIKLkeeQIRELEIKVQELRKYKES-EKDTEVLMSALSAM 575
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1261 RGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEekesIVSQLSRSKQaftQQTEELKRQLEE 1322
Cdd:pfam09726 576 QDKNQHLENSLSAETRIKLDLFSALGDAKRQLE----IAQGQIYQKD---QEIKDLKQKIAE 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1661-1891 |
3.65e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1661 ALRGQEDLKEQLaivERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQS 1740
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1741 EVEDASRDARNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1814
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1815 KLETRIRELEFELEGEQKK----NTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQA 1890
Cdd:COG4942 171 AERAELEALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 98986453 1891 N 1891
Cdd:COG4942 251 L 251
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1005-1701 |
3.94e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1005 QQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAqesildlENDKQQLDERLKKk 1084
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA-------MDDYNNLKSALNE- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1085 dfeycqlQSKVEDEQTlglQFQKKIKELQARIEELEEEIEAERATRAKTEKqrsdyareleelserleeaggVTSTQIEL 1164
Cdd:PRK01156 244 -------LSSLEDMKN---RYESEIKTAESDLSMELEKNNYYKELEERHMK---------------------IINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1165 NKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKleKEKSEFKLEIDDLSSSMESVSKSKA 1244
Cdd:PRK01156 293 NRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1245 NLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEeen 1324
Cdd:PRK01156 371 SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME--- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1325 kaknalahaLQSSRHDCDLLReqyeeeqegkaelqralskansevaqwrTKYETDAIQR-TEELEEAKKKLAQRLQDSEE 1403
Cdd:PRK01156 448 ---------MLNGQSVCPVCG----------------------------TTLGEEKSNHiINHYNEKKSRLEEKIREIEI 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1404 QVEAVNAKCASLEKTKQRLQG-EVEDLMVDVERANSLAAALdKKQRNFDKVLAEWKTKCEESQAELeaslkesRSLSTEL 1482
Cdd:PRK01156 491 EVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARADL-EDIKIKINELKDKHDKYEEIKNRY-------KSLKLED 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1483 FKLKN-AYEEALDQLETVkrenknleqEIADLTEQIAENGKTIHELEKSRKQIELEKADIqlaleeaeaaleheeakilr 1561
Cdd:PRK01156 563 LDSKRtSWLNALAVISLI---------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD-------------------- 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1562 iqleltqvKSEIDRKIAEKDEEIEQL--KRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANrqaaE 1639
Cdd:PRK01156 614 --------KSYIDKSIREIENEANNLnnKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIE----D 681
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1640 TLKHLRSvqgqlkdtqlHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARK 1701
Cdd:PRK01156 682 NLKKSRK----------ALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1581-1913 |
3.98e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1581 DEEIEQLK--RNYQRTVETMQ--SALDAEVRSRNEAI-RLKKKME----GDLNEIEIQLSHANRQ-AAETLKHLrsvqgq 1650
Cdd:COG3206 84 ETQIEILKsrPVLERVVDKLNldEDPLGEEASREAAIeRLRKNLTvepvKGSNVIEISYTSPDPElAAAVANAL------ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1651 lkdTQLHLDdalrgqEDLKEQLAIVERRANLLQAEVEELRATLEQTERARK--LAEQELLDSNERVQLLHTQNTSlihtk 1728
Cdd:COG3206 158 ---AEAYLE------QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSE----- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1729 kkLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEelkkeqdtSAHLERMKKNLEQTVKDLQhrldeaeQLALKG 1808
Cdd:COG3206 224 --LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELA-------ELSARY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1809 GKK--QIQKLETRIRELEFELEGEQKKNTESVKG-LRKYERRVKELTYQSEEDRKNVLRLQdlvdKLQVKVKSYKRQAEE 1885
Cdd:COG3206 287 TPNhpDVIALRAQIAALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEV 362
|
330 340
....*....|....*....|....*...
gi 98986453 1886 ADEQANAHLTKFRKAQheLEEAEERADI 1913
Cdd:COG3206 363 ARELYESLLQRLEEAR--LAEALTVGNV 388
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
888-1425 |
4.02e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 888 LQLQVQAESENLLDAEERCDQLIKAKFQ-LEAKIKEvterAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVE 966
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKeLEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 967 KEK--HATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQalddlqaeedkvnslnktKSKLEQQVEDLESSLEQEkk 1044
Cdd:COG4717 123 KLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEE------------------LEELEAELAELQEELEEL-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1045 lrvdLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKdfeycqlqskvedeqtlglqfQKKIKELQARIEeleeeie 1124
Cdd:COG4717 183 ----LEQLSLATEEELQDLAEELEELQQRLAELEEELEEA---------------------QEELEELEEELE------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1125 aeratRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELnkkreAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAEL 1204
Cdd:COG4717 231 -----QLENELEAAALEERLKEARLLLLIAAALLALLGLG-----GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1205 GEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQrsLSELTTQKSRLQTE 1284
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1285 AGelSRQLEEKESIVSQLSRsKQAFTQQTEELKRQLEEENKAKNALAHAlqssrHDCDLLREQYEEEQEGKAELQRALSK 1364
Cdd:COG4717 379 AG--VEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELEE 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1365 ANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCAS---LEKTKQRLQGE 1425
Cdd:COG4717 451 LREELA--ELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAlelLEEAREEYREE 512
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1504-1927 |
4.90e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.83 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1504 KNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEH-EEAKILRIQLELTQVK-SEIDRKIAEKD 1581
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1582 EEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKME---GDLNEIEIQLshanrQAAETlkHLRSVQGQLKDTQLHL 1658
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-----LALQT--KLETLTNQNSDCKQHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1659 ddalrgqEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQllhTQNTSLIHTKKKL---ETDL 1735
Cdd:pfam10174 327 -------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS---TLAGEIRDLKDMLdvkERKI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1736 MQLQSEVEDASRDARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EQTVKDLQHRLDEAEQL--A 1805
Cdd:pfam10174 397 NVLQKKIENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1806 LKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDlvdklqvkvKSYKRQAEE 1885
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN---------QLKKAHNAE 547
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 98986453 1886 ADEQANAHLT-KFRKAQHELEEAEERADIAESQVNKLRAKTRD 1927
Cdd:pfam10174 548 EAVRTNPEINdRIRLLEQEVARYKEESGKAQAEVERLLGILRE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1470-1717 |
5.00e-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: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1470 ASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKAdiqlaleeae 1549
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1550 aaleheeakilriqlELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEgdlneieiQ 1629
Cdd:COG4942 87 ---------------ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK--------Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1630 LSHANRQAAETlkhLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLD 1709
Cdd:COG4942 144 LAPARREQAEE---LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
....*...
gi 98986453 1710 SNERVQLL 1717
Cdd:COG4942 221 EAEELEAL 228
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1460-1883 |
6.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1460 KCEESQAELEASLKESRSLSTELFKLKNAYEeALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKA 1539
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1540 DIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLkkkM 1619
Cdd:COG4717 178 ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL---I 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1620 EGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERA 1699
Cdd:COG4717 255 AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1700 RKLAEQELLDSNERVQLLHTQNTSLIH--TKKKLETDLMQLQSEVEDASRDArnAEEKAKKAITDAAMMAEELKKEQDTS 1777
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEE--LRAALEQAEEYQELKEELEELEEQLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1778 AHLERMKKNLEQTVKD-LQHRLDEAEQlALKGGKKQIQKLETRIRELEFELEgEQKKNTESVKGLRKYERRVKELTYQSE 1856
Cdd:COG4717 413 ELLGELEELLEALDEEeLEEELEELEE-ELEELEEELEELREELAELEAELE-QLEEDGELAELLQELEELKAELRELAE 490
|
410 420
....*....|....*....|....*..
gi 98986453 1857 EDRKNVLrLQDLVDKLQVKVKSYKRQA 1883
Cdd:COG4717 491 EWAALKL-ALELLEEAREEYREERLPP 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1502-1725 |
8.01e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1502 ENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEID---RKIA 1578
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelrAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1579 EKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEgdlneieiQLSHANRQAAETLkhlRSVQGQLKDTQLHL 1658
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK--------YLAPARREQAEEL---RADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1659 DDAlrgQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLI 1725
Cdd:COG4942 170 EAE---RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
652-676 |
8.87e-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: 50.81 E-value: 8.87e-07
10 20
....*....|....*....|....*
gi 98986453 652 FRENLNKLMSNLRTTHPHFVRCIIP 676
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1675-1919 |
9.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1675 VERRANLLQAEVEELRATLEQTERARKlaEQELLdsnERVQLLHTQntslihtKKKLETDLMQLqseveDASRDARNAEE 1754
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDARE--QIELL---EPIRELAER-------YAAARERLAEL-----EYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1755 KAKKAitdaAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKn 1834
Cdd:COG4913 286 AQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERR- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1835 tesvkgLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLqvkVKSYKRQAEEADEQANAHLTKFRKAQHELEEAE-ERADI 1913
Cdd:COG4913 361 ------RARLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEaEIASL 431
|
....*.
gi 98986453 1914 AESQVN 1919
Cdd:COG4913 432 ERRKSN 437
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
842-1034 |
1.44e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ------ 915
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 916 -----LEAK-IKEVTERA-------EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE 982
Cdd:COG3883 104 yldvlLGSEsFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 983 LSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVED 1034
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1243-1492 |
1.60e-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: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1243 KANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEE 1322
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1323 EnkaKNALAhalqssrhdcDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKYetdaiqrteeleeakkkLAQRLQDSE 1402
Cdd:COG4942 102 Q---KEELA----------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQY-----------------LKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1403 EQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTEL 1482
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|
gi 98986453 1483 FKLKNAYEEA 1492
Cdd:COG4942 230 ARLEAEAAAA 239
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1304-1910 |
1.67e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1304 RSKQAFTQQTEELKRQLEEenkaknalahaLQSSRHDCDLLREQyEEEQEGKAELQralskansevaqwrtKYETDAIQR 1383
Cdd:pfam07111 56 EGSQALSQQAELISRQLQE-----------LRRLEEEVRLLRET-SLQQKMRLEAQ---------------AMELDALAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1384 TEELEEAKkklAQRLQDSEEQVEAVNakcASLEKTKQRLQGEVEDL----MVDVERANSLA-AALDKKQRNFDKVLAEWK 1458
Cdd:pfam07111 109 AEKAGQAE---AEGLRAALAGAEMVR---KNLEEGSQRELEEIQRLhqeqLSSLTQAHEEAlSSLTSKAEGLEKSLNSLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1459 TKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKnlEQEIADLTEQIAENGKtiHELEKSRKQIELEK 1538
Cdd:pfam07111 183 TKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVG--EQVPPEVHSQTWELER--QELLDTMQHLQEDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1539 ADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIrlkKK 1618
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSV---KQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1619 MEGDLNEIEIQLSHANRQAAETLKHLRSVQGQL-------KDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRA 1691
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVevermsaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1692 TLEQTerarklaeqeLLDSNERVQLLHTQNTSLIHTKKKLET--DLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEE 1769
Cdd:pfam07111 416 WLETT----------MTRVEQAVARIPSLSNRLSYAVRKVHTikGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1770 LKKEQDT-SAHLERMKKNLEQTVKDLQHRlDEAEQLALKGGKKQIQKLETRIRE--------LEFELEGEQkKNTESVKG 1840
Cdd:pfam07111 486 LREERNRlDAELQLSAHLIQQEVGRAREQ-GEAERQQLSEVAQQLEQELQRAQEslasvgqqLEVARQGQQ-ESTEEAAS 563
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1841 LRKYERRVKELTYQSEEDrknvlRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEER 1910
Cdd:pfam07111 564 LRQELTQQQEIYGQALQE-----KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1620-1837 |
1.73e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1620 EGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEqtERA 1699
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1700 RKLAEQELLDSNERVQLLHTQNTSLIhtkkkletDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEqdtsah 1779
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFL--------DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE------ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1780 LERMKKNLEQTVKDLQHRLDEAEQLaLKGGKKQIQKLETRIRELEFELEGEQKKNTES 1837
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
884-1534 |
1.87e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 884 EKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLA 963
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 964 KVEKEKHATENKVKNLTEELSGLDETIAKLTR---EKKALQEAHQQALDDLQAEEDKVNSLnktkSKLEQQVEDLESSLE 1040
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSSledMKNRYESEIKTAESDLSMELEKNNYY----KELEERHMKIINDPV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1041 QEKKLRVdleRNKRKLEGDLKLAQESILDLENDKQQLDERLKkkdfeycqlqsKVEDEQTLGLQFQKKIKELQarieele 1120
Cdd:PRK01156 291 YKNRNYI---NDYFKYKNDIENKKQILSNIDAEINKYHAIIK-----------KLSVLQKDYNDYIKKKSRYD------- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1121 eeieaeratraKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADs 1200
Cdd:PRK01156 350 -----------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVK- 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1201 VAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLsssmesvskskaNLEKICRTLEDQLSEargknEEIQRSLSELTTQKSR 1280
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLDELSRNMEML------------NGQSVCPVCGTTLGE-----EKSNHIINHYNEKKSR 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1281 LQTEAGELSRQLEEKESIVSQLSRSKQAFtqQTEELKRQLEEENKAKNAlAHALQSSRHDCDLLREQYEEEQEGKAELQR 1360
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYL--ESEEINKSINEYNKIESA-RADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1361 A-LSKANSEVAQW------RTKYETDAIQ-RTEELEEAKKKLAQRLQDSEEQVEAVNakcASLEKTKQRLQGEVEDLMVD 1432
Cdd:PRK01156 558 LkLEDLDSKRTSWlnalavISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNK 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1433 VERANSLAAALDK---KQRNFDKVLAEWKTKcEESQAELEASLKESrslSTELFKLKNAYEEALDQLETVKRENKNLEQE 1509
Cdd:PRK01156 635 YNEIQENKILIEKlrgKIDNYKKQIAEIDSI-IPDLKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTR 710
|
650 660
....*....|....*....|....*
gi 98986453 1510 IADLTEQIAENGKTIHELEKSRKQI 1534
Cdd:PRK01156 711 INELSDRINDINETLESMKKIKKAI 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
912-1099 |
2.40e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 912 AKFQLEAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIA 991
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAEL----DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 992 KLTRekkALQEA---------------------HQQALDDL-QAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDL 1049
Cdd:COG3883 90 ERAR---ALYRSggsvsyldvllgsesfsdfldRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 98986453 1050 ERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQ 1099
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1190-1535 |
2.60e-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: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1190 VAALRKKHADSVAELGEQIDNLQRVKQKL-EKEKSEFKLEIDDLSSSMESVSKSKA--NLEKICRTLEDqLSEARGKNEE 1266
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELeELSARESDLEQDYQAASDHLNLVQTAlrQQEKIERYQED-LEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1267 IQRSLSELTTQKSRLQTEAGELSrqlEEKESIVSQLSRSKQAF-TQQTEELKRQleeenKAKNALAHAlqssRHDCDLlr 1345
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLADYQQALdVQQTRAIQYQ-----QAVQALEKA----RALCGL-- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1346 eqyeeeqegkaelqRALSKANseVAQWRTKYETDAIQRTEELEEakkkLAQRLQDSEEQVEAVNAKCASLEKtkqrLQGE 1425
Cdd:COG3096 432 --------------PDLTPEN--AEDYLAAFRAKEQQATEEVLE----LEQKLSVADAARRQFEKAYELVCK----IAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1426 VEDlmvdvERANSLAAALDKKQRNFdKVLAEWKTKCEESQAELE---ASLKESRSLSTELFKLKNAYEEALDQLETVKRE 1502
Cdd:COG3096 488 VER-----SQAWQTARELLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350
....*....|....*....|....*....|...
gi 98986453 1503 nknLEQEIADLTEQIAENGKTIHELEKSRKQIE 1535
Cdd:COG3096 562 ---LEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1747-1933 |
2.95e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1747 RDARNAEE----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLETRIRE 1822
Cdd:COG1196 207 RQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--------AELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1823 LEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQH 1902
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190
....*....|....*....|....*....|.
gi 98986453 1903 ELEEAEERADIAESQVNKLRAKTRDFTSSRM 1933
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1059-1622 |
3.10e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1059 DLKLAQESILDLENDKQQLdERLKKKDFEYCQLQSKVEDEQTLGLQF-----QKKIKELQARIEELEEEIEAERATRAKT 1133
Cdd:COG4913 236 DLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1134 EKQRSDYARELEELSERLEEAGGVTSTQIE-----LNKKRE------AEFLKLRRDLEEATLQHEAMVAALRKKHADSVA 1202
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1203 ELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELttqksrLQ 1282
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL------IE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1283 TEAGELS--------------------RQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDC- 1341
Cdd:COG4913 469 VRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFr 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1342 DLLREQYEEEQ-----EGKAELQRA--------LSKANSEVAQ------WRTKYET--DAIQRTEELEEAKKKLAQRLQD 1400
Cdd:COG4913 549 AWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSRYVLgfDNRAKLAALEAELAELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1401 SEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERAnSLAAALDKKqrnfdkvlaewktkcEESQAELEASLKESRSLST 1480
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAEL---------------EAELERLDASSDDLAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1481 ELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEheeakil 1560
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER------- 765
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1561 RIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGD 1622
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED 827
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1382-1639 |
3.68e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1382 QRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANslaAALDKKQRNFDKVLAewktkc 1461
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERAR------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1462 eesqaeleaSLKESRSLSTELFKLKNA--YEEALDQLETVKRENKNLEQEIADLTEQIAEngktiheLEKSRKQIELEKA 1539
Cdd:COG3883 94 ---------ALYRSGGSVSYLDVLLGSesFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1540 DIQLAleeaeaaleheeakilriQLELTQVKSEIDRKIAEKDEEIEQLKRNyQRTVETMQSALDAEVRSRNEAIRLKKKM 1619
Cdd:COG3883 158 ELEAL------------------KAELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250 260
....*....|....*....|
gi 98986453 1620 EGDLNEIEIQLSHANRQAAE 1639
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1307-1535 |
3.96e-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: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1307 QAFTQQTEELKRQLEEENKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAqwrtKYETDAIQRTEE 1386
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAA-------LKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1387 LEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQR-------LQGEVEDLMVDVERANSLAAALDKKQRNFDKV---LAE 1456
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaeLAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1457 WKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLEtvkRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIE 1535
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1357-1776 |
5.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1357 ELQRALSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKC------ASLEKTKQRLQGEVED 1428
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLLPLYQelealeAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1429 LMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLE- 1507
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEn 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1508 -QEIADLTEQIAENGK------TIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEK 1580
Cdd:COG4717 235 eLEAAALEERLKEARLllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1581 D---EEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAetlkhLRSVQGQLKDTQLH 1657
Cdd:COG4717 315 EleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-----LAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1658 LDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLA--EQELLDSNERVQLLHTQNTSLIHTKKKLETD- 1734
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEelEEELEELEEELEELREELAELEAELEQLEEDg 469
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 98986453 1735 -LMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDT 1776
Cdd:COG4717 470 eLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1465-1696 |
5.69e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1465 QAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENK--NLEQEIADLTEQIAEngktiheLEKSRKQIELEKADIQ 1542
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------LESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1543 LALEEAEAALEHEEAKIlrIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQsALDAEVRSRNEaiRLKKKMEGD 1622
Cdd:COG3206 240 ARLAALRAQLGSGPDAL--PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-ALRAQIAALRA--QLQQEAQRI 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1623 LNEIEIQLSHANRQAAEtlkhLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQT 1696
Cdd:COG3206 315 LASLEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1349-1522 |
6.33e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1349 EEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdsEEQVEavnAKCASLEKTKQRLQGEVED 1428
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLD---RKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1429 lmvdveranslaaaLDKKQRNFDKvlaeWKTKCEESQAELEASLKESRSLSTElfklkNAYEEALDQLEtvkrenKNLEQ 1508
Cdd:PRK12704 119 --------------LEQKQQELEK----KEEELEELIEEQLQELERISGLTAE-----EAKEILLEKVE------EEARH 169
|
170
....*....|....
gi 98986453 1509 EIADLTEQIAENGK 1522
Cdd:PRK12704 170 EAAVLIKEIEEEAK 183
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
855-1086 |
7.14e-06 |
|
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: 51.31 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 855 EEFQKTKDELAKSEAKR----KELEEKLVTLVQEKNDLQLQVQAESEnlldaeercdqlikaKFQLEAKIKEVTERAEDE 930
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKRehleKEVEKKLESKSGNKNKMEAKAQANSQ---------------KDEIFALINKEANRDARA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 931 EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAkLTREKKALQEAHQQALDD 1010
Cdd:pfam18971 675 IAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1011 LQaeedkvNSLNKTKSKLEQQVEDLESSLEQ--------EKKLRVDLERNKRKLEGDLKLAQESILDLEN-DKQQLDERL 1081
Cdd:pfam18971 754 FK------NGKNKDFSKVTQAKSDLENSVKDviinqkvtDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQA 827
|
....*.
gi 98986453 1082 KK-KDF 1086
Cdd:pfam18971 828 QKnEDF 833
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1252-1738 |
7.21e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1252 TLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQ-------LSRSKQAFTQQTEELKRQLEEEN 1324
Cdd:pfam10174 314 TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKktkqlqdLTEEKSTLAGEIRDLKDMLDVKE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1325 KAKNALA---HALQSSRHDCDL----LREQYEEEQEGK-------AELQRALSKANSEVAQWRTKYETDAIQRTEELEEA 1390
Cdd:pfam10174 394 RKINVLQkkiENLQEQLRDKDKqlagLKERVKSLQTDSsntdtalTTLEEALSEKERIIERLKEQREREDRERLEELESL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1391 KKKlaqrLQDSEEQVEAVNAKCASLEKTKQRLQgevedlmvdvERANSLAAALDKKQrnfdkvlaewkTKCEESQAELEA 1470
Cdd:pfam10174 474 KKE----NKDLKEKVSALQPELTEKESSLIDLK----------EHASSLASSGLKKD-----------SKLKSLEIAVEQ 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1471 SLKESRSLSTELFKLKNAYEEALDQLETVKREnKNLEQEIADLTEqiaengktihelEKSRKQIELEkadiqlaleeaea 1550
Cdd:pfam10174 529 KKEECSKLENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARYKE------------ESGKAQAEVE------------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1551 aleheeaKILRIQLELTQVKSEIDRKIAE---------KDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEG 1621
Cdd:pfam10174 583 -------RLLGILREVENEKNDKDKKIAElesltlrqmKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1622 DLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLdDALRgQEDLKEQLAIVERRANLLQAEVEELRAT---LEQTER 1698
Cdd:pfam10174 656 QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHL-TNLR-AERRKQLEEILEMKQEALLAAISEKDANialLELSSS 733
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 98986453 1699 ARKLAEQElldsnerVQLLHTQNTSLIHTKKKLETDLMQL 1738
Cdd:pfam10174 734 KKKKTQEE-------VMALKREKDRLVHQLKQQTQNRMKL 766
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1344-1629 |
7.64e-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: 50.89 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1344 LREQYEE---EQEGKAELQRALSKANSEVAQWRTKY---ETDAIQRTEELEEAkkklaqRLQDSEEQVEAVNAKCASLEK 1417
Cdd:pfam17380 301 LRQEKEEkarEVERRRKLEEAEKARQAEMDRQAAIYaeqERMAMERERELERI------RQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1418 TKQRlqgEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTElfKLKNAYEEALDQLE 1497
Cdd:pfam17380 375 SRMR---ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEERAREME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1498 TVKRENKNLEQEIADLTEQIAENGKTIHELEKS---RKQIELEKADI---QLALEEAEAALEHEEAKILRIQLELTQ--V 1569
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEkrdRKRAEEQRRKIlekELEERKQAMIEEERKRKLLEKEMEERQkaI 529
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1570 KSEIDRKIAEKDEEIEQLKRNYQRTVETMQSAldAEVRSRNEAIRLKKKMEGDLNEIEIQ 1629
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKA 587
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
868-1210 |
8.54e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 868 EAKRKELEEKLVTLVQEKNDLQLQVQAesenlldAEERCDQLiKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEde 947
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEA-------LEAELDAL-QERREALQRLAEYSWDEIDVASAEREIAELEAELE-- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 948 csELKKDIDDLEltlaKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLnkTKSK 1027
Cdd:COG4913 679 --RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1028 LEQQVEDLESSlEQEKKLRVDLERNKRKLEGDLKLAQESILDL--------ENDKQQLDERLKKKDfEYCQLQSKVEDEq 1099
Cdd:COG4913 751 LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLP-EYLALLDRLEED- 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1100 tlGL-QFQKKIKELQARIEELEEEIEAERATRA-KTEKQR----------SDYareleelserleeaGGVTSTQIELNKK 1167
Cdd:COG4913 828 --GLpEYEERFKELLNENSIEFVADLLSKLRRAiREIKERidplndslkrIPF--------------GPGRYLRLEARPR 891
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 98986453 1168 REAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDN 1210
Cdd:COG4913 892 PDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
862-1067 |
8.64e-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: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 862 DELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIkevteraedeEEINAELTAKK 941
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----------AEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 942 RKLEDECSELKK---DIDDLELTLAkvekekhatenkVKNLTEELSGLD--ETIAKLTREKKALQEAHQQALDDLQAE-E 1015
Cdd:COG3883 86 EELGERARALYRsggSVSYLDVLLG------------SESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAElE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1016 DKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESI 1067
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1252-1418 |
8.64e-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: 49.15 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1252 TLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAK--NA 1329
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1330 LAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAqwrtkyetdaiQRTEELEEAKKKLAQRLQDSEEQVEAVN 1409
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA-----------ELEAELEEKKAELDEELAELEAELEELE 162
|
....*....
gi 98986453 1410 AKCASLEKT 1418
Cdd:COG1579 163 AEREELAAK 171
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
854-1091 |
9.85e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.53 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 854 KEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEER--------CDQLIKAKFQLEAKIKEVTE 925
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeiedlrrqLDTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 926 RAEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEELSGL----DETIAKLT------- 994
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLkknhEEEVRELQaqvsdtq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 995 -----------------------------REKKALQEAHQQALDDLQAEEDKVN-SLNKTKSKLEQ---QVEDLESSLEQ 1041
Cdd:pfam00038 156 vnvemdaarkldltsalaeiraqyeeiaaKNREEAEEWYQSKLEELQQAAARNGdALRSAKEEITElrrTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1042 EKKLRVDLERNKRKLE----GDLKLAQESILDLENDKQQLDERLKKKDFEYCQL 1091
Cdd:pfam00038 236 LKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
847-1070 |
1.06e-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: 50.51 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFqktKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER 926
Cdd:pfam05557 15 QNEKKQMELEH---KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 927 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQ 1006
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1007 ---------------------------------ALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLR---VDLE 1050
Cdd:pfam05557 172 ikelefeiqsqeqdseivknskselaripelekELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYReeaATLE 251
|
250 260
....*....|....*....|....
gi 98986453 1051 RNKRKLEGDL----KLAQESILDL 1070
Cdd:pfam05557 252 LEKEKLEQELqswvKLAQDTGLNL 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1566-1940 |
1.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1566 LTQVKSEIDRKIAEKDEEIEQlKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLshanrqaaETLKHLR 1645
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV--------KELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1646 SVQGQLKDTQLHLDDALRGQEDLKEQLaivERRANLLQAEVEELRATLEQTERARKLAEQELldsnervqllhtqntSLI 1725
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIREL---EERIEELKKEIEELEEKVKELKELKEKAEEYI---------------KLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1726 HTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEqTVKDLQHRLDEAEQLA 1805
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1806 LKGGKKQIQKLETRIRELEfelegeqKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQdlvdKLQVKVKSYKRQAEE 1885
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELE-------KAKEEIEEEISKITARIGELKKEIKELKKAIEELK----KAKGKCPVCGRELTE 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1886 AD-----EQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE 1940
Cdd:PRK03918 448 EHrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKE 507
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1219-1376 |
1.48e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1219 EKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESI 1298
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1299 VSQLSRSKQAFTQQTEELKRQLeeenkakNALAHALQSSrhdcdllrEQYEEEQEGKAE-----LQRALSKANSEVAQWR 1373
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQL-------AALEAALDAS--------EKRDRESQAKIAdlgrrLNVALAQRVQELNRYR 196
|
...
gi 98986453 1374 TKY 1376
Cdd:PRK09039 197 SEF 199
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1084 |
1.74e-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: 49.38 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 862 DELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER----AEDEEEINAEL 937
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 938 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQAlddlqaeEDK 1017
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL-------EAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1018 VNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKK 1084
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1759 |
1.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1478 LSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAengKTIHELEKSRKQIELEKADIQlaleeaeaaleheea 1557
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIR--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1558 kilriqlELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSrneairlkkkmeGDLNEIEIQLSHAN-RQ 1636
Cdd:COG4942 73 -------ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL------------GRQPPLALLLSPEDfLD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1637 AAETLKHLRSVQGQLKDTqlhlddalrgQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQL 1716
Cdd:COG4942 134 AVRRLQYLKYLAPARREQ----------AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR 203
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 98986453 1717 LHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKA 1759
Cdd:COG4942 204 LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1334 |
2.28e-05 |
|
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: 49.79 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 853 MKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESE---NLLDAEERCDQLIKAKFQLEAKIKEVTERAED 929
Cdd:pfam01576 550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsNLEKKQKKFDQMLAEEKAISARYAEERDRAEA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 930 E------------------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETI- 990
Cdd:pfam01576 630 EareketralslaraleeaLEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELq 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 991 ----AKLtREKKALQEAHQQALDDLQAEEDKVNslnKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQES 1066
Cdd:pfam01576 710 atedAKL-RLEVNMQALKAQFERDLQARDEQGE---EKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1067 ILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQ-------TLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSD 1139
Cdd:pfam01576 786 IDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDE 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1140 YARELeelserleeAGGVTSTQIELNKKR--EAEFLKLRRDLEEATLQHEAMVAALRK--KHADSV-AELGEQIDNLQRV 1214
Cdd:pfam01576 866 LADEI---------ASGASGKSALQDEKRrlEARIAQLEEELEEEQSNTELLNDRLRKstLQVEQLtTELAAERSTSQKS 936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1215 ---KQKLEKEKSEFKL----------------------EIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQR 1269
Cdd:pfam01576 937 esaRQQLERQNKELKAklqemegtvkskfkssiaaleaKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERR 1016
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1270 SLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHAL 1334
Cdd:pfam01576 1017 HADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
935-1139 |
2.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 935 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAE 1014
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1015 EDKVNSLN------------KTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLK 1082
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1083 KKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSD 1139
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
861-1113 |
2.88e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 861 KDELAKSEAKRKELEEKL---VTLVQEKNDLQLQVQAESENLLDAEERCDQLIKA--KFQLEAKIKEVTERAED-EEEIn 934
Cdd:COG3206 106 DEDPLGEEASREAAIERLrknLTVEPVKGSNVIEISYTSPDPELAAAVANALAEAylEQNLELRREEARKALEFlEEQL- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 935 AELTAKKRKLEDECSELKKD----------------IDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKk 998
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKnglvdlseeaklllqqLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 999 ALQEAHQQaLDDLQAEEDKVNSLNKTKS----KLEQQVEDLESSLEQEkklrvdLERNKRKLEGDLKLAQESILDLENDK 1074
Cdd:COG3206 264 VIQQLRAQ-LAELEAELAELSARYTPNHpdviALRAQIAALRAQLQQE------AQRILASLEAELEALQAREASLQAQL 336
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 98986453 1075 QQLDERLK---KKDFEYCQLQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:COG3206 337 AQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1154-1383 |
3.17e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1154 AGGVTSTQIELNKKREAEFLKLRRDLEEATlQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLS 1233
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELE-KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1234 SSMESVsksKANLEKICRTLEDQLSEA--RGKNEEIQ------------RSLSELTTQKSRLQTEAGELSRQLEEKESIV 1299
Cdd:COG4942 90 KEIAEL---RAELEAQKEELAELLRALyrLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1300 SQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETD 1379
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....
gi 98986453 1380 AIQR 1383
Cdd:COG4942 247 GFAA 250
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
844-1087 |
3.98e-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: 48.35 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 924 TERAE-------DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAK---L 993
Cdd:pfam07888 156 KERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 994 TREKKALQE---AHQQALDDLQAEEDKVNSL-NKTKSKLEQ-QVEDLESSLE------QEKKLRVDLERNKRKLEGDLKL 1062
Cdd:pfam07888 236 LEELRSLQErlnASERKVEGLGEELSSMAAQrDRTQAELHQaRLQAAQLTLQladaslALREGRARWAQERETLQQSAEA 315
|
250 260
....*....|....*....|....*
gi 98986453 1063 AQESILDLENDKQQLDERLKKKDFE 1087
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERME 340
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
890-1513 |
4.07e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 890 LQVQAESENLLDAEERCDQLIKAkfqleakIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEK 969
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFG-------YKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 970 HATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRV-- 1047
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnr 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1048 DLERNKRKL----EGDLKLAQESILDLENDKQQLDERLK--KKDFEYCQLQSKVEDEQTLGLQFQKKIK-ELQARIEELE 1120
Cdd:pfam12128 391 DIAGIKDKLakirEARDRQLAVAEDDLQALESELREQLEagKLEFNEEEYRLKSRLGELKLRLNQATATpELLLQLENFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1121 EEIEAERATRAKTEKQRSDYAreleelsERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEA----MVAALRKK 1196
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQ-------SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtLLHFLRKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1197 HADSVAELGEQIDNLQRVKQKLEKEKSEF----------------KLEIDDLSSSMESVSKSKANLEKICRT-------L 1253
Cdd:pfam12128 544 APDWEQSIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRIDVPEWAASEEELRERLDKAEEALQSarekqaaA 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1254 EDQLSEARGKNEEIQRslsELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKA-KNALAH 1332
Cdd:pfam12128 624 EEQLVQANGELEKASR---EETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQlDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1333 ALQSSRHDCDLLR---EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQ---------------RTEELEEAKKKL 1394
Cdd:pfam12128 701 WLEEQKEQKREARtekQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALEtwykrdlaslgvdpdVIAKLKREIRTL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1395 AQRLQDSEEQVEAV------------------NAKCASLEKTKQRLQGEVEDLMVDVERANS--------------LAAA 1442
Cdd:pfam12128 781 ERKIERIAVRRQEVlryfdwyqetwlqrrprlATQLSNIERAISELQQQLARLIADTKLRRAklemerkasekqqvRLSE 860
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1443 LDKKQRNFDKVLAEWKTKCEESQAELEASlkeSRSLSTELFKLKNAYEEaldqlETVKRENKNLEQEIADL 1513
Cdd:pfam12128 861 NLRGLRCEMSKLATLKEDANSEQAQGSIG---ERLAQLEDLKLKRDYLS-----ESVKKYVEHFKNVIADH 923
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1565-1809 |
4.85e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1565 ELTQVKSEIDRKIAEKDEEIEQLKRNyQRTVETMQSALDAEVRSRNEAIRlkkKMEGDLNEIEIQLSHANRQAAETLKHL 1644
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1645 RSVQGQLKDtQLHLDDALRGQEDLK-----EQLAIVERRANLLQAEVEELRATLEQTERARklaeqelldsnervQLLHT 1719
Cdd:COG4942 100 EAQKEELAE-LLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADL--------------AELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1720 QNTSLIHTKKKLETDLMQLQSEvedasRDARNAEEKAKKAItdAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD 1799
Cdd:COG4942 165 LRAELEAERAELEALLAELEEE-----RAALEALKAERQKL--LARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|
gi 98986453 1800 EAEQLALKGG 1809
Cdd:COG4942 238 AAAERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1728-1927 |
5.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1728 KKKLETDLMQLQSEVEDASRdARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKKNL-----EQTVKDLQHRLD 1799
Cdd:COG4913 220 EPDTFEAADALVEHFDDLER-AHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1800 EAEQlALKGGKKQIQKLETRIRELEFELEG-EQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKS 1878
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 98986453 1879 YKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRD 1927
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1160-1455 |
6.58e-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: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1160 TQIELNKKRE-----AEFLKLRRDLEEATLQHEAMVAALRKkhadsvaelgeqidnlqRVKQKLEKEKSEFKLEIDDlss 1234
Cdd:COG3206 85 TQIEILKSRPvlervVDKLNLDEDPLGEEASREAAIERLRK-----------------NLTVEPVKGSNVIEISYTS--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1235 smESVSKSKANLEKICRTLEDQLSEARgkNEEIQRSLSELTTQKSRLQTEAGELSRQLEE--KESIVSQLSRSKQAFTQQ 1312
Cdd:COG3206 145 --PDPELAAAVANALAEAYLEQNLELR--REEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1313 TEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEE--EQEGKAELQRALSKANSEVAQWRTKYETD--AIQRT-EEL 1387
Cdd:COG3206 221 LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALrAQI 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1388 EEAKKKLAQR----LQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLA 1455
Cdd:COG3206 301 AALRAQLQQEaqriLASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1003 |
8.09e-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: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 845 ETEKEMATMKEEFQKTKDELAKSEAK----RKELEEKLVTLVQEKNDLQLQVQAESENLLDA--------------EERC 906
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkylaparREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 907 DQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEdecselkKDIDDLELTLAKVEKEKHATENKVKNLTEELSGL 986
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
170
....*....|....*..
gi 98986453 987 DETIAKLTREKKALQEA 1003
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
973-1329 |
8.69e-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: 47.64 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 973 ENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTK---------------------SKLEQQ 1031
Cdd:COG5185 172 LNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKakeiinieealkgfqdpeselEDLAQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1032 VEDLESSLEQEKKLRVDLERNKRKLEGDLK-LAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQ-FQKKI 1109
Cdd:COG5185 252 SDKLEKLVEQNTDLRLEKLGENAESSKRLNeNANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1110 KELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREaEFLKLRRDLEEATLQHEAM 1189
Cdd:COG5185 332 RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKE-SLDEIPQNQRGYAQEILAT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1190 VAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQlSEARGKNEEIQR 1269
Cdd:COG5185 411 LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVR-SKKEDLNEELTQ 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1270 SLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQ-QTEELKRQLEEENKAKNA 1329
Cdd:COG5185 490 IESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRaRGYAHILALENLIPASEL 550
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1438-1679 |
9.38e-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: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1438 SLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQI 1517
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1518 AEngktihelekSRKQIELEKADIQLALEEAEAALEHEEAKILriqleltqVKSEIDRKIAEKDEEIEQLKRNYQRTVET 1597
Cdd:COG4942 93 AE----------LRAELEAQKEELAELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1598 MQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVER 1677
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
..
gi 98986453 1678 RA 1679
Cdd:COG4942 235 EA 236
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1187 |
9.47e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESE---NLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipNLQNITVRLQDLTEKLSEAEDMLACE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 924 TERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAtenkvknlteelsgldetiaKLTREKKAL 1000
Cdd:TIGR00618 614 QHALLRKLQPeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHA--------------------LSIRVLPKE 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1001 QEAHQQALddLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLER-------NKRKLEGDLKLAQESILDLEnd 1073
Cdd:TIGR00618 674 LLASRQLA--LQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELM-- 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1074 kQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEE 1153
Cdd:TIGR00618 750 -HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ 828
|
330 340 350
....*....|....*....|....*....|....
gi 98986453 1154 AGGVTSTQIELNKKREAEFLKLRRDLEEATLQHE 1187
Cdd:TIGR00618 829 EEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
890-1053 |
1.11e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 890 LQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLeltlakvE 966
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELL-------E 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 967 KEKHATENKVKNLTEELSGLDETIAKLtrekKALQEAHQQALDD---LQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEK 1043
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEEL----EELIEEQLQELERisgLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEA 182
|
170
....*....|
gi 98986453 1044 KLRVDLERNK 1053
Cdd:PRK12704 183 KEEADKKAKE 192
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1669-1924 |
1.45e-04 |
|
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: 46.97 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1669 KEQLAIVE--RRANLLQAEVEELRATLEQ-------TERaRKLAEQELLDSNE---RVQLLHTQntslihTKKKLETdlM 1736
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--L 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1737 QLQSEVEDASRDARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKL 1816
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1817 ETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLV-------DKLQVKVKSYKRQAEEADEQ 1889
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLeelesklDELAEELAELEEKLEELKEE 352
|
250 260 270
....*....|....*....|....*....|....*
gi 98986453 1890 ANAHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1265-1511 |
1.74e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1265 EEIQRSLSELTTQKSrLQTEAGELSRQLEEKESIVSQLSRSKQaftqQTEELKRQL-----------EEENKAKNALAHA 1333
Cdd:PRK11281 39 ADVQAQLDALNKQKL-LEAEDKLVQQDLEQTLALLDKIDRQKE----ETEQLKQQLaqapaklrqaqAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1334 LQSSRHDCDL--LREQYEEEQEGKAELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKL-AQRLQDSEEQ 1404
Cdd:PRK11281 114 TRETLSTLSLrqLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKGGkVGGKALRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1405 VEAVNAKCASLE-KTKQR---LQGevedlmvdveraNSLAAALDKKQRNFdkvLAEWKTKCEESQAELEASLKESRSLST 1480
Cdd:PRK11281 194 RVLLQAEQALLNaQNDLQrksLEG------------NTQLQDLLQKQRDY---LTARIQRLEHQLQLLQEAINSKRLTLS 258
|
250 260 270
....*....|....*....|....*....|..
gi 98986453 1481 ElfklkNAYEEALDQLETVK-RENKNLEQEIA 1511
Cdd:PRK11281 259 E-----KTVQEAQSQDEAARiQANPLVAQELE 285
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1414-1932 |
1.74e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1414 SLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQ---RNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYE 1490
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNlelENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1491 EALDQLETVKRENKNLEQEIADLTEQIAENGKtIHELEKSRKQIELEKA---------------DIQLALE--EAEAALE 1553
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVyknrnyindyfkyknDIENKKQilSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1554 HEEAKILRIQLELTQVKSEIDRKIAEKDE------EIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIE 1627
Cdd:PRK01156 322 NKYHAIIKKLSVLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1628 IQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRAnllQAEVEELRATLEQTERARKLAEQEL 1707
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQS---VCPVCGTTLGEEKSNHIINHYNEKK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1708 LDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELK---------KEQDTSA 1778
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdkhdkyeeiKNRYKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1779 HLERMKKNLEQTVKDLQHRLD---EAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESvkgLRKYERRVKELTYQS 1855
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISLidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS---IREIENEANNLNNKY 635
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1856 EEDRKNvlrlQDLVDKLQVKVKSYKRQAEEADEQanahltkfrkaQHELEEAEERADIAESQVNKLRAKTRDFTSSR 1932
Cdd:PRK01156 636 NEIQEN----KILIEKLRGKIDNYKKQIAEIDSI-----------IPDLKEITSRINDIEDNLKKSRKALDDAKANR 697
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1347-1539 |
1.77e-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: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1347 QYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEV 1426
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1427 EDLMVDVER-------------ANSLAAALDK---------KQRNFDKVLAEWKTKCEESQAELEASLKEsrslsteLFK 1484
Cdd:COG3883 89 GERARALYRsggsvsyldvllgSESFSDFLDRlsalskiadADADLLEELKADKAELEAKKAELEAKLAE-------LEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1485 LKNAYEEALDQLETVKRENKN----LEQEIADLTEQIAENGKTIHELEKSRKQIELEKA 1539
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEAllaqLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1644-1933 |
1.83e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1644 LRSVQGQLKDTQ---LHLDDA-LRGQEDLKEQLAivERRAnlLQAEVEELRATLEQTERARKLAEQElldsNERVQLLHT 1719
Cdd:PLN02939 130 LEDLVGMIQNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQE----KIHVEILEE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1720 QntsLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQH 1796
Cdd:PLN02939 202 Q---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELES 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1797 RLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKY---ERRVKELTYQSEEdrKNVLRLQ-DLVDKL 1872
Cdd:PLN02939 279 KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELL 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1873 QVKVKSYKRQAEEADEQANAHLTKFrkaQHELEEAEeraDIAESQVNKLRAKTRDFTSSRM 1933
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHSYIQLY---QESIKEFQ---DTLSKLKEESKKRSLEHPADDM 411
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1254-1447 |
1.93e-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: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1254 EDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHA 1333
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1334 LQSSRHDCDLL---------------REQYEEEQEGKAELQRALSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRL 1398
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 98986453 1399 QDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQ 1447
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1161-1367 |
2.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1161 QIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVS 1240
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1241 KS----KANLEKICRTLE--DQLSEARGKN-EEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQaftqQT 1313
Cdd:COG4942 122 LAlllsPEDFLDAVRRLQylKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1314 EELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANS 1367
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
844-968 |
2.09e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKL--VTLVQEKNDLQLQVQAESENLLDAEercDQLIKAKFQLEAKIK 921
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRRISDLE---DEILELMERIEELEE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 98986453 922 EVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE 968
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1265-1885 |
2.20e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1265 EEIQRSLSELTTQKSRLQTEAGELSRQLE---EKESIVSQLSRSKQAFTQQTEELkrqlEEENKAKNALAHALQSSRhdc 1341
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNwltRLDELQQEASRRQQALQQALAAE----EKAQPQLAALSLAQPARQ--- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1342 dlLREQYEEEQEGKAELQRALSKANS------EVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSE------EQVEAVN 1409
Cdd:PRK10246 292 --LRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDrfrqwnNELAGWR 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1410 AKCASLEKTKQRLQGEVEDLMVDVERANSLAAALdkkqrnfdkvlaewKTKCEESQAELEASLKESRSLSTELFKLKNAY 1489
Cdd:PRK10246 370 AQFSQQTSDREQLRQWQQQLTHAEQKLNALPAIT--------------LTLTADEVAAALAQHAEQRPLRQRLVALHGQI 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1490 EEALDQLETVKRENKNLEQEIADLTEQIAE-------------NGKTIHELEKSRKQIELEKADIQL------------- 1543
Cdd:PRK10246 436 VPQQKRLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqlaDVKTICEQEARIKDLEAQRAQLQAgqpcplcgstshp 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1544 -ALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRN---YQRTVETMQsALDAEVRSRNEAIRLKKKM 1619
Cdd:PRK10246 516 aVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDeseAQSLRQEEQ-ALTQQWQAVCASLNITLQP 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1620 EGDLN-------EIEIQLSHANR------QAAETLKHLRSVQGQLKDTQLHLDDALRG-------QEDLKEQLAIVERRA 1679
Cdd:PRK10246 595 QDDIQpwldaqeEHERQLRLLSQrhelqgQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqEDEEASWLATRQQEA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1680 NLLQAEVEELRATLEQTERARKL-----AEQELLDSNERVQL-----LHTQNTSL---IHTKKKLETDLMQLQSEVEDAS 1746
Cdd:PRK10246 675 QSWQQRQNELTALQNRIQQLTPLletlpQSDDLPHSEETVALdnwrqVHEQCLSLhsqLQTLQQQDVLEAQRLQKAQAQF 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1747 RDARNAEEKAKKAITDAAMMAEElkkeqdTSAHLERMKKNLEQtvkdlqhRLDEAEQLALKGGKKQIQKLETRIRELEFE 1826
Cdd:PRK10246 755 DTALQASVFDDQQAFLAALLDEE------TLTQLEQLKQNLEN-------QRQQAQTLVTQTAQALAQHQQHRPDGLDLT 821
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1827 LEGE--QKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDklqvKVKSYKRQAEE 1885
Cdd:PRK10246 822 VTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQ----QIAQATQQVED 878
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
981-1397 |
2.43e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 981 EELSGLDETIAKLTREK---KALQEAHQQALDDLQAEEDkvnSLNKTKSKLEQQVEDLESSL----------EQEKKLRV 1047
Cdd:PRK04863 279 NERRVHLEEALELRRELytsRRQLAAEQYRLVEMARELA---ELNEAESDLEQDYQAASDHLnlvqtalrqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1048 DLERNKRKLEGDL---KLAQESILDLENDKQQLDE---RLKKKDFEYcqlQSKVEDEQTLGLQFQKKIKELQarieelee 1121
Cdd:PRK04863 356 DLEELEERLEEQNevvEEADEQQEENEARAEAAEEevdELKSQLADY---QQALDVQQTRAIQYQQAVQALE-------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1122 eieaeratRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKReaeflKLrRDLEEATLQHEAMVAALRKkhadsv 1201
Cdd:PRK04863 425 --------RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQ-----KL-SVAQAAHSQFEQAYQLVRK------ 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1202 aeLGEQID--NLQRVKQKLEKEKSEFKLEIDDLSSsmesvskskanlekicrtLEDQLSEARGKNEE---IQRSLSELTT 1276
Cdd:PRK04863 485 --IAGEVSrsEAWDVARELLRRLREQRHLAEQLQQ------------------LRMRLSELEQRLRQqqrAERLLAEFCK 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1277 QKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEE------ENKAKNALAHALQSSrhdCDLLREQYEE 1350
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqRLAARAPAWLAAQDA---LARLREQSGE 621
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1351 EQEGK----------AELQRALSKANSEVAqwrtkyetdaiQRTEELEEAKKKLAQR 1397
Cdd:PRK04863 622 EFEDSqdvteymqqlLERERELTVERDELA-----------ARKQALDEEIERLSQP 667
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
949-1079 |
2.85e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 949 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDL----------------- 1011
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1012 ---------------QAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEN---- 1072
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
....*..
gi 98986453 1073 DKQQLDE 1079
Cdd:PRK11637 231 DQQQLSE 237
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
848-1112 |
3.30e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENL------LDAEERCDQLIKAKFQLEAKIK 921
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 922 EVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKEKH 970
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 971 ATENKVKNLTEELSGLDETI----AKLTREKKALQ------------EAHQQALDDL-QAEEDKVnsLNKTKSKLEQQVE 1033
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKLsvaqAAHSQFEQAYQlvrkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMRLS 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1034 DLESSLEQEKklrvDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKEL 1112
Cdd:PRK04863 524 ELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
842-1087 |
3.30e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIK-------AKF 914
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkeERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 QLEAKIKEVTERAEDEEEINAELTAKKRKLEdecsELKKDIDDLE-----------------LTLAKVEKEKHATE---- 973
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEwrqqtevlspeeekelvEKIKELEKELEKAKkale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 974 --NKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLER 1051
Cdd:COG1340 158 knEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQK 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 98986453 1052 NKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFE 1087
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
847-1037 |
3.77e-04 |
|
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: 45.60 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 847 EKEMATMKEEFQKTKDEL-AKSEAKRKELEE----KLVTLVQEKNDLQLQVQAESENLldaEERCDQLIKAK-------F 914
Cdd:pfam12128 695 DKKHQAWLEEQKEQKREArTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKAL---ETWYKRDLASLgvdpdviA 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 QLEAKIKEVTERAEDEEEINAE------------------LTAKKRKLEDECSELKKD----IDDLELTLAKVEKEKHAT 972
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQQQlarlIADTKLRRAKLEMERKAS 851
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 973 ENKVKNLTEELSGLDETIAKLT--REKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLES 1037
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLAtlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1274-1528 |
3.80e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1274 LTTQKSRLQTEAgelsRQLEEKESivSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQE 1353
Cdd:pfam00038 23 LEQQNKLLETKI----SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1354 GKAELQ---RALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQ 1423
Cdd:pfam00038 97 LRTSAEndlVGLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1424 GEVEDLMvdveranslaaaldkkQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKREN 1503
Cdd:pfam00038 177 AQYEEIA----------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260
....*....|....*....|....*....
gi 98986453 1504 KNLEQEIADLTE----QIAENGKTIHELE 1528
Cdd:pfam00038 241 ASLERQLAETEEryelQLADYQELISELE 269
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
956-1368 |
4.17e-04 |
|
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: 45.60 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 956 DDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLnktKSKLEQQVEDL 1035
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSE---KDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1036 ESSLEQEkklRVDLERNKRKLEGDLKLAQESILD--LENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:pfam12128 677 KDSANER---LNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1114 ARIEELEEEIEAERATRAKTEKQRSDYareleelserleeaggvtSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAAL 1193
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTL------------------ERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQ 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1194 RKKHADSVAELGEQIDNLQR-VKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSE-ARGKNEEIQRSL 1271
Cdd:pfam12128 816 LSNIERAISELQQQLARLIAdTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEqAQGSIGERLAQL 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1272 SELttqKSRLQTEAGELSRQLEEKESIVSQLSRSkqAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEE 1351
Cdd:pfam12128 896 EDL---KLKRDYLSESVKKYVEHFKNVIADHSGS--GLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQS 970
|
410
....*....|....*..
gi 98986453 1352 QEGKAELQRALSKANSE 1368
Cdd:pfam12128 971 IMVLREQVSILGVDLTE 987
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
970-1224 |
4.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 970 HATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSL----EQEKKL 1045
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1046 RVDLERNKRKLEGDLKLAQES-------ILDLENDKQQLDERLKKkdfeycqLQSKVEDEQTLGLQFQKKIKELQARIEE 1118
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplaLLLSPEDFLDAVRRLQY-------LKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1119 leeeieaerATRAKTEKQRSdyareleelserleeaggvtstqielnkkrEAEFLKLRRDLEEATLQHEAMVAALRKK-- 1196
Cdd:COG4942 169 ---------LEAERAELEAL------------------------------LAELEEERAALEALKAERQKLLARLEKEla 209
|
250 260
....*....|....*....|....*....
gi 98986453 1197 -HADSVAELGEQIDNLQRVKQKLEKEKSE 1224
Cdd:COG4942 210 eLAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
911-1073 |
4.59e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 911 KAKFQLEAKIKEVTERAEDEEEIN-AELTAKKRKLEDECSELKKDIDDLELTLAKvekekhatenkvknlteelsgLDET 989
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELEAELEE---------------------KDER 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 990 IAKLTRE-KKALQEAHQQALDD--LQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNK----RKLEgdlKL 1062
Cdd:COG2433 443 IERLERElSEARSEERREIRKDreISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGElvpvKVVE---KF 519
|
170
....*....|.
gi 98986453 1063 AQESILDLEND 1073
Cdd:COG2433 520 TKEAIRRLEEE 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1063-1291 |
4.70e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1063 AQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRsdyAR 1142
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1143 ELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEAtLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEK 1222
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1223 SEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQ 1291
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1462-1618 |
4.85e-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: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1462 EESQAELEASLKEsrsLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE------NGKTIHELEKSRKQIE 1535
Cdd:COG1579 23 EHRLKELPAELAE---LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1536 LEKADIQL---ALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTV---ETMQSALDAEVRSR 1609
Cdd:COG1579 100 SLKRRISDledEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaerEELAAKIPPELLAL 179
|
....*....
gi 98986453 1610 NEAIRLKKK 1618
Cdd:COG1579 180 YERIRKRKN 188
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1395-1748 |
5.57e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1395 AQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdkvLAEWKTKCEESQAELEASLKE 1474
Cdd:PLN02939 63 SKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ------QTNSKDGEQLSDFQLEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEH 1554
Cdd:PLN02939 137 IQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGAT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1555 EEAKILRIQLELTQVKSEidrKIAEKDeEIEQLKRNYQRTVETMQSALDAEvrsrneaiRLKKKMEGDLNEIEIQLSHAN 1634
Cdd:PLN02939 217 EGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAETEERVFKLE--------KERSLLDASLRELESKFIVAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1635 rqaAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERAR------KLAEQELL 1708
Cdd:PLN02939 285 ---EDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKfssykvELLQQKLK 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 98986453 1709 DSNERVQLLHTQNTSLI----HTKKKLETDLMQLQSEVEDASRD 1748
Cdd:PLN02939 362 LLEERLQASDHEIHSYIqlyqESIKEFQDTLSKLKEESKKRSLE 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1473-1911 |
5.92e-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: 44.96 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1473 KESRSLSTELFKLKNAYE----EALDQLETVKRENKNLEQEIADLTEQIAENGKTiheLEKSRKQIELEKADIQLALEEA 1548
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHLREALQQTQQS---HAYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1549 EAALEHEEAKILRIQLELTQVKSEIDRK---IAEKDEEIEQLKRNYQRTVETMQSALDAEVRSR-NEAIRLKKKMEGDLN 1624
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLmKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1625 EIEIQLSHA----NRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEV-----EELRATLEQ 1695
Cdd:TIGR00618 344 RRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQatidtRTSAFRDLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1696 TERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLE-TDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQ 1774
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1775 dtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQK-------KNTESVKGLRKYERR 1847
Cdd:TIGR00618 504 -----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKqraslkeQMQEIQQSFSILTQC 578
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1848 VKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERA 1911
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1169-1338 |
5.93e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1169 EAEFLKLRRDLEEAtlqhEAMVAALRKKHADSVAELGEQIDNlqRVKQKLEKEKSEFKLEIDDLSSSMesvsksKANLEK 1248
Cdd:COG3206 225 ESQLAEARAELAEA----EARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARY------TPNHPD 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1249 IcRTLEDQLSEARGK-NEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKqaftQQTEELKRQLEEENKAK 1327
Cdd:COG3206 293 V-IALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE----AELRRLEREVEVARELY 367
|
170
....*....|.
gi 98986453 1328 NALAHALQSSR 1338
Cdd:COG3206 368 ESLLQRLEEAR 378
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
912-1084 |
6.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 912 AKFQLEAKIKEVTERAE---DEEEINAELTAKKRKLEdecseLKKDIDDLEltlAKVEKEKHATENKVKNLteelsglde 988
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-----AKEEIHKLR---NEFEKELRERRNELQKL--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 989 tiakltrEKKALQeaHQQALDDlqaeedKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEgdLKLAQESIL 1068
Cdd:PRK12704 88 -------EKRLLQ--KEENLDR------KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL--QELERISGL 150
|
170
....*....|....*.
gi 98986453 1069 DLENDKQQLDERLKKK 1084
Cdd:PRK12704 151 TAEEAKEILLEKVEEE 166
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
1415-1599 |
6.14e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 44.55 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1415 LEKTKQRLQGEVEDLMVDVE-RANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTElfklknAYEEAL 1493
Cdd:COG4487 24 VKQRRAEFEKELAERLADAAkREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKKALAVAE------EKEKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1494 DQLETVKRENknlEQEIADLTEQIAENGKTIHELE--KSRKQIELEKADIQLALEEAEAALEHEEAKilriQLELTQVK- 1570
Cdd:COG4487 98 AALQEALAEK---DAKLAELQAKELELLKKERELEdaKREAELTVEKERDEELDELKEKLKKEEEEK----QLAEKSLKv 170
|
170 180
....*....|....*....|....*....
gi 98986453 1571 SEIDRKIAEKDEEIEQLKRNYQRTVETMQ 1599
Cdd:COG4487 171 AEYEKQLKDMQEQIEELKRKKEQGSTQLQ 199
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1187-1429 |
7.40e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1187 EAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKekseFKLEIDDLSSSMESVSKSKAN-LEKICRTLEDQLSEARGKNE 1265
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQ----AKEGLSALNRLLPRLNLLADEtLADRVEEIREQLDEAEEAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1266 EIQR---SLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQ---AFTQ--------QTEELKRQLEEENKAKNALA 1331
Cdd:PRK04863 912 FVQQhgnALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEvvqrrahfSYEDAAEMLAKNSDLNEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1332 HALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEvaqWRTKYET--DAIQRTEEL-----EEAKKKLAQRLQDSEEQ 1404
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDELHAR 1068
|
250 260
....*....|....*....|....*
gi 98986453 1405 VEAVNAKCASLEKTKQRLQGEVEDL 1429
Cdd:PRK04863 1069 LSANRSRRNQLEKQLTFCEAEMDNL 1093
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
926-1051 |
7.48e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 926 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETI-AKLTREKKALQeah 1004
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIA--- 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 98986453 1005 QQALDDLQAEEDKVN-----SLNKTKSKLEQQVEDLESSLEQEKKLRVDLER 1051
Cdd:cd22656 178 RKEIKDLQKELEKLNeeyaaKLKAKIDELKALIADDEAKLAAALRLIADLTA 229
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
915-1067 |
7.49e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE---------ELSG 985
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 986 LDETIAKLTREKKALQEAHQQALDDLQAEEDKvnsLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQE 1065
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEE---LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
..
gi 98986453 1066 SI 1067
Cdd:COG1579 171 KI 172
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1923 |
7.51e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1254 EDQLSEARGKNEEIQRSLSELTtqkSRLQTEAGELSRQLEekesivsqlsrskqaftQQTEELKRQLEEENKAKNALAHA 1333
Cdd:NF041483 592 EEALADARAEAERIRREAAEET---ERLRTEAAERIRTLQ-----------------AQAEQEAERLRTEAAADASAARA 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1334 lQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiqrTEELEEAKKKLAQRLQDSEEQVEAVNAKcA 1413
Cdd:NF041483 652 -EGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEA---AEALAAAQEEAARRRREAEETLGSARAE-A 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1414 SLEKTKQRLQGEvedlmvdveranslaaaldkkqrnfdKVLAEWKTKCEESQAELEASLKESRSLSTELfkLKNAYEEAL 1493
Cdd:NF041483 727 DQERERAREQSE--------------------------ELLASARKRVEEAQAEAQRLVEEADRRATEL--VSAAEQTAQ 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1494 DQLETVKRENKNLEQEIADLtEQIAEngktiHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQV-KSE 1572
Cdd:NF041483 779 QVRDSVAGLQEQAEEEIAGL-RSAAE-----HAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAaKAL 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1573 IDRKIAEKDEEIEQLKRNYQRTVETMQS-ALDAEVRSRNEAIRLKKKMEGDLNEI--------EIQLSHANRQAAETLKH 1643
Cdd:NF041483 853 AERTVSEAIAEAERLRSDASEYAQRVRTeASDTLASAEQDAARTRADAREDANRIrsdaaaqaDRLIGEATSEAERLTAE 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1644 LRSVQGQLKDTQLHLDDALRGqedlkEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTS 1723
Cdd:NF041483 933 ARAEAERLRDEARAEAERVRA-----DAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAE 1007
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1724 LIHTKKKLETDLMqLQSEVEDASRDARNAEEKAKKAITDAAMMAEEL---------KKEQDTSAHLERM----KKNLEQT 1790
Cdd:NF041483 1008 RLRTEAREEADRT-LDEARKDANKRRSEAAEQADTLITEAAAEADQLtakaqeealRTTTEAEAQADTMvgaaRKEAERI 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1791 VKDL---------QHRLDEAEQLAlkGGKKQIQKLETRIRELEFELEGE-----QKKNTESVKGLRKYERRVKELTYQSE 1856
Cdd:NF041483 1087 VAEAtvegnslveKARTDADELLV--GARRDATAIRERAEELRDRITGEieelhERARRESAEQMKSAGERCDALVKAAE 1164
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1857 EDRKnvlrlqdlvdklQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRA 1923
Cdd:NF041483 1165 EQLA------------EAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKA 1219
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1000-1539 |
8.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1000 LQEAHQQALDDLQAEEDKVNSLNKTKSK-LEQQVEDLESSLEQEKKLRVDLERNKRKLEgdlklaqesilDLENDKQQLD 1078
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAELQEELEELEEELE-----------ELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1079 ERLKKKDfeycQLQSKVEDEQTLGlQFQKKIKELQARIEELEEEIEAERATRAKTEkqrsdyareleelserleeaggvt 1158
Cdd:COG4717 116 EELEKLE----KLLQLLPLYQELE-ALEAELAELPERLEELEERLEELRELEEELE------------------------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1159 stqielnkKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMES 1238
Cdd:COG4717 167 --------ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1239 VskskANLEKICRTLEDQLSEARgkneeIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKR 1318
Cdd:COG4717 239 A----ALEERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1319 QLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdaIQRTEELEEAKKKLAQRL 1398
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE---------LQLEELEQEIAALLAEAG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1399 QDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNfdKVLAEWKTKCEESQAELEASLKESRSL 1478
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAEL 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1479 STELFKLKN--AYEEALDQLETVKRENKNLEQEIA--DLTEQIAEngKTIHELEKSRKQIELEKA 1539
Cdd:COG4717 459 EAELEQLEEdgELAELLQELEELKAELRELAEEWAalKLALELLE--EAREEYREERLPPVLERA 521
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1682-1765 |
8.78e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1682 LQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARnaeEKAKKAIT 1761
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK---QKRKEITD 223
|
....
gi 98986453 1762 DAAM 1765
Cdd:PRK11448 224 QAAK 227
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1161-1425 |
8.85e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1161 QIELNKKREAEFLKLRRDLEEATLQHEAMV---AALRKKHADSVAELGEQIDNLQRVKQKLEKEK---SEFKLEIDDLSS 1234
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMdrqAAIYAEQERMAMERERELERIRQEERKRELERirqEEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1235 SMESVSKSKANLEKICRTLEdQLSEARGKNEEIQRSLSELTTQKSRLQTEAG-----ELSRQLEEKESIVSQLSRSKQAF 1309
Cdd:pfam17380 380 LERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1310 TQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE-----------LQRALSKANSEVAQWRTKYET 1378
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREA 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 98986453 1379 DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE 1425
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
818-1656 |
9.40e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 818 NIRSFMNVKHWPWMKLFFKIKPLLKSAETEKemaTMKEEFQKT----KDELAK--SEAKRKELEEKLVTLVQEKNDLQLQ 891
Cdd:TIGR01612 932 SIEKFHNKQNILKEILNKNIDTIKESNLIEK---SYKDKFDNTlidkINELDKafKDASLNDYEAKNNELIKYFNDLKAN 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 892 VQAESENLL----DAEERCDQLIKAKFQ------------LEAKIKEVTERAEDEEEINAELTAKK--RKLEDECSELKK 953
Cdd:TIGR01612 1009 LGKNKENMLyhqfDEKEKATNDIEQKIEdanknipnieiaIHTSIYNIIDEIEKEIGKNIELLNKEilEEAEINITNFNE 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 954 DIDDLEL----TLAKVEKEKHATE-NKVKNlteELSGLDETIAKLTREKKALQEAHQQALDDLQAEedkVNSLNKTKSKL 1028
Cdd:TIGR01612 1089 IKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQ---INDLEDVADKA 1162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1029 EQQvEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQEsILDLENDKQQLdERLKKKDFEYcqlqskvedEQTLGLQFQKK 1108
Cdd:TIGR01612 1163 ISN-DDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKTSL-EEVKGINLSY---------GKNLGKLFLEK 1230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1109 IKElqarieeleeEIEAERATRAKTEKQRSDYARELEELSERLEEAGgvtstqIELNKKREAEFLKLRRDLEE----ATL 1184
Cdd:TIGR01612 1231 IDE----------EKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMG------IEMDIKAEMETFNISHDDDKdhhiISK 1294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1185 QHEAMVAALRKKHADSVAELGEQiDNLQRVKQKLEKEKSEFK-------------------LEIDDLSSSMESVSKSKAN 1245
Cdd:TIGR01612 1295 KHDENISDIREKSLKIIEDFSEE-SDINDIKKELQKNLLDAQkhnsdinlylneianiyniLKLNKIKKIIDEVKEYTKE 1373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1246 LEKICRTLEDQLSEARGKNEEIQRSLSeLTTQKSRLQTEA------GELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQ 1319
Cdd:TIGR01612 1374 IEENNKNIKDELDKSEKLIKKIKDDIN-LEECKSKIESTLddkdidECIKKIKELKNHILSEESNIDTYFKNADENNENV 1452
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1320 LEEENK---AKNALAHALQ------SSRHDCDL--LREQYEEEQEGKAELQR--ALSKANSEVAQWRTKYETDAIQRTEE 1386
Cdd:TIGR01612 1453 LLLFKNiemADNKSQHILKikkdnaTNDHDFNIneLKEHIDKSKGCKDEADKnaKAIEKNKELFEQYKKDVTELLNKYSA 1532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1387 LEeAKKKLAQRLQDSE----EQVEAVNAKCASLEKTKQRL------QGEVEDLMVDVERANSLAAALDKKQRNFDKVLae 1456
Cdd:TIGR01612 1533 LA-IKNKFAKTKKDSEiiikEIKDAHKKFILEAEKSEQKIkeikkeKFRIEDDAAKNDKSNKAAIDIQLSLENFENKF-- 1609
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1457 wkTKCEESQAELEASLKESRSLSTELFKLknayeeALDQLETVKRENKNLEQEIADLTEQIAENGKTIHEleksrKQIEL 1536
Cdd:TIGR01612 1610 --LKISDIKKKINDCLKETESIEKKISSF------SIDSQDTELKENGDNLNSLQEFLESLKDQKKNIED-----KKKEL 1676
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1537 EKADiqlaleeaeaaleheeAKILRIQLELTQVKSEIDRKIAEK--------DEEIEQLKRNYQRTVETMQSAL---DAE 1605
Cdd:TIGR01612 1677 DELD----------------SEIEKIEIDVDQHKKNYEIGIIEKikeiaianKEEIESIKELIEPTIENLISSFntnDLE 1740
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 98986453 1606 VRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQL 1656
Cdd:TIGR01612 1741 GIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRI 1791
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1404-1597 |
9.44e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1404 QVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAA-LDKKQRNFDKVLAE---WKTKCEESQAELEASLKESRSLS 1479
Cdd:PHA02562 175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEaktIKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1480 TELFKLKNAYEEALDQLETVKRENK-------------NLEQE---IADLTEQIAENGKTIHELEKSR---KQIELEKAD 1540
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqQISEGpdrITKIKDKLKELQHSLEKLDTAIdelEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1541 IQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAE---KDEEIEQLKRNYQRTVET 1597
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKLQDELDKIVKT 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1565-1778 |
9.68e-04 |
|
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: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1565 ELTQVKSEIDRKIAEKDEEIEQLKRNYQRtvetmqsaLDAEVRSRNEAIrlkKKMEGDLNEIEIQLSHANRQAAETLKHL 1644
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1645 rsvqgQLKDTQLHLDDALRGQEDLKEQLaiveRRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSL 1724
Cdd:COG3883 96 -----YRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1725 IHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSA 1778
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1745-1915 |
1.11e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1745 ASRDARNAEEKAKKAITDAAMMAEELKKEqdtsahlermkKNLEqtVKDLQHRL-DEAEQlALKGGKKQIQKLETRIREL 1823
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKE-----------ALLE--AKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1824 EFELEgeqkkntesvKGLRKYERRVKELtyqsEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQAnAHLTKFRKAQHE 1903
Cdd:PRK12704 95 EENLD----------RKLELLEKREEEL----EKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEIL 159
|
170
....*....|....
gi 98986453 1904 LEEAEE--RADIAE 1915
Cdd:PRK12704 160 LEKVEEeaRHEAAV 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1288-1539 |
1.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1288 LSRQLEEKesiVSQLSRSKQAFTQQTEELKRQLEEenkAKNALAHALQssRHDCDLLREQYEEEQEGKAELQRALSKANS 1367
Cdd:COG3206 162 LEQNLELR---REEARKALEFLEEQLPELRKELEE---AEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1368 EVAQWRTKYetDAIQRteELEEAKKKLAQRLQDSEEQveavnakcaSLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQ 1447
Cdd:COG3206 234 ELAEAEARL--AALRA--QLGSGPDALPELLQSPVIQ---------QLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1448 RNFDKVLaewktkceesQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHEL 1527
Cdd:COG3206 301 AALRAQL----------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|..
gi 98986453 1528 EKSRKQIELEKA 1539
Cdd:COG3206 371 LQRLEEARLAEA 382
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
857-1080 |
1.36e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 857 FQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIK-----------AKFQLEAKIKEVTE 925
Cdd:PRK04778 100 FRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKsllanrfsfgpALDELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 926 RAEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----LTEELSGLDETiaKLTRE 996
Cdd:PRK04778 180 EFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHLDHL--DIEKE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 997 KKALQEAHQQALDDLQAEE-DKVNSLNKtksKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQ 1075
Cdd:PRK04778 258 IQDLKEQIDENLALLEELDlDEAEEKNE---EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID 334
|
....*
gi 98986453 1076 QLDER 1080
Cdd:PRK04778 335 RVKQS 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1713-1894 |
1.40e-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: 42.22 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1713 RVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEQ--T 1790
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNvrN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1791 VKDLQHRLDEAEQLalkggKKQIQKLETRIRELEFELEGEQKKntesvkgLRKYERRVKELTYQSEEDRKnvlRLQDLVD 1870
Cdd:COG1579 88 NKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEE-------LAELEAELAELEAELEEKKA---ELDEELA 152
|
170 180
....*....|....*....|....
gi 98986453 1871 KLQVKVKSYKRQAEEADEQANAHL 1894
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
842-1395 |
1.44e-03 |
|
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: 43.67 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 842 KSAETEKEMATMKEEFQKTKDELAKSEA-KRKELEEKLVTLVQEKNDLQlQVQAESENL---LDAEERCDQLIKAKFQ-L 916
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDqHGAFLDADIETAAADQEQLP-SWQSELENLeerLKALTGKHQDVTAKYNrR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 917 EAKIKEvtERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLakvekeKHATENKVKNLTEELSGLDETIAKLtre 996
Cdd:pfam12128 381 RSKIKE--QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLKSRLGEL--- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 997 kKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQ 1076
Cdd:pfam12128 450 -KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1077 LD---------------------------ERLKKKDFEYCQLQSKVEDEQTLG---LQFQK--------KIKELQARIEE 1118
Cdd:pfam12128 529 LFpqagtllhflrkeapdweqsigkvispELLHRTDLDPEVWDGSVGGELNLYgvkLDLKRidvpewaaSEEELRERLDK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1119 LEEEIEAERATRAKTEKQRSDYARELEELSERLEEAG----GVTSTQIELNKKREAEFLKLRRDLEEAT----------- 1183
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERKdsanerlnsle 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1184 -------LQHEAMVAALR--------KKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSK----- 1243
Cdd:pfam12128 689 aqlkqldKKHQAWLEEQKeqkreartEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpd 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1244 --ANLEKICRTLEDQLSEARGKNEEIqrsLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLE 1321
Cdd:pfam12128 769 viAKLKREIRTLERKIERIAVRRQEV---LRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLE 845
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 1322 EENKAKNALAHALQSSRHDCDLLREQYEE--EQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLA 1395
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATlkEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIA 921
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
872-1224 |
1.45e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 872 KELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSEL 951
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 952 KKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQ 1031
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1032 VEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKE 1111
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1112 LQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVA 1191
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 98986453 1192 ALRKKHADSVAELGEQIDNLQRVKQKLEKEKSE 1224
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1674-1828 |
1.47e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1674 IVERRANLLQAEVEELratLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETdlmqlqsEVEDASRDARNAE 1753
Cdd:pfam04012 1 IFKRLGRLVRANIHEG---LDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLER-------RLEQQTEQAKKLE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1754 EKAKKAITDAAmmaEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLETRIRELEFELE 1828
Cdd:pfam04012 71 EKAQAALTKGN---EELARE------ALAEKKSLEKQAEALETQLAQQRSAVEQL-RKQLAALETKIQQLKAKKN 135
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
865-1048 |
1.50e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.32 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 865 AKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINA---ELTAKK 941
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 942 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEElsglDETIAKLTREKkalqEAHQQALDDLQAEEDKVNSL 1021
Cdd:PRK00106 104 SRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIIL 175
|
170 180
....*....|....*....|....*..
gi 98986453 1022 NKTKSKLEQQVEDLESSLEQEKKLRVD 1048
Cdd:PRK00106 176 AETENKLTHEIATRIREAEREVKDRSD 202
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1456-1709 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1456 EWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALD--QLETVKRENKNLEQEiadlteQIAENGKTIHELEksRKQ 1533
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELERIRQE------EIAMEISRMRELE--RLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1534 IELEkadiQLALEEAEAALEHEEAKILriqleltqvKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAI 1613
Cdd:pfam17380 385 MERQ----QKNERVRQELEAARKVKIL---------EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1614 RLKkkmegdlnEIEIQlshanrqaaETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQlaiverRANLLQAEVEELRATL 1693
Cdd:pfam17380 452 RLE--------EQERQ---------QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAM 508
|
250
....*....|....*.
gi 98986453 1694 EQTERARKLAEQELLD 1709
Cdd:pfam17380 509 IEEERKRKLLEKEMEE 524
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1674-1824 |
1.56e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1674 IVERRANLLQAEVEELratLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDAsrdarnaE 1753
Cdd:COG1842 2 IFKRLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------E 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1754 EKAKKAitdaammaeeLKKEQDTSAH--LERmKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLETRIRELE 1824
Cdd:COG1842 72 EKARLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELK 132
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1251-1520 |
1.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1251 RTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNAL 1330
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1331 AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNA 1410
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1411 KcASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYE 1490
Cdd:COG4372 208 L-IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270
....*....|....*....|....*....|
gi 98986453 1491 EALDQLETVKRENKNLEQEIADLTEQIAEN 1520
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1251-1537 |
1.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1251 RTLEDQLSEARGkneEIQRSLSELTTQKSRLqteaGELSRQLEEkesivsqLSRSKQAFTQQTEELKRQLeeeNKAKNAL 1330
Cdd:PRK04863 282 RVHLEEALELRR---ELYTSRRQLAAEQYRL----VEMARELAE-------LNEAESDLEQDYQAASDHL---NLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1331 AHALQSSRHDCDL------LREQ---YEEEQEGKAELQRALSKANSEVAQWRTKY----------ETDAIQ--------- 1382
Cdd:PRK04863 345 RQQEKIERYQADLeeleerLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldvqQTRAIQyqqavqale 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1383 ------------------RTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDlmVDVERANSLAAALD 1444
Cdd:PRK04863 425 rakqlcglpdltadnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGE--VSRSEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1445 KKQRNfDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTI 1524
Cdd:PRK04863 503 RRLRE-QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR 581
|
330
....*....|...
gi 98986453 1525 HELEKSRKQIELE 1537
Cdd:PRK04863 582 MALRQQLEQLQAR 594
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
841-971 |
1.77e-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: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVqaesenlldaeERCDQLIKakfQLEAKI 920
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----------EEKDERIE---RLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 921 KEVTERAEDEEEINAELTAKKRK---LEDECSELKKDIDDLEltlAKVEKEKHA 971
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREierLERELEEERERIEELK---RKLERLKEL 501
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1254-1737 |
1.79e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1254 EDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHA 1333
Cdd:COG5185 155 EVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1334 LQSsrhdcdllREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEavnakca 1413
Cdd:COG5185 235 LKG--------FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIA------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1414 slEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSlstelfklknayeeal 1493
Cdd:COG5185 300 --EYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKE---------------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1494 dqletvKRENKNLEQEIADLTEQIAENGKTIhelEKSRKQIELEKADIQLALEEAEAAleheeakilriqleLTQVKSEI 1573
Cdd:COG5185 362 ------EIENIVGEVELSKSSEELDSFKDTI---ESTKESLDEIPQNQRGYAQEILAT--------------LEDTLKAA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1574 DRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAI-RLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLK 1652
Cdd:COG5185 419 DRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADeESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1653 DTQLHLDDALRGQ-EDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKL 1731
Cdd:COG5185 499 ATLEKLRAKLERQlEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLS 578
|
....*.
gi 98986453 1732 ETDLMQ 1737
Cdd:COG5185 579 TIESQQ 584
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1668-1836 |
1.85e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.94 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1668 LKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASR 1747
Cdd:pfam00261 48 LEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1748 DARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE-------RMKKNLEQTVKDLQHRLDEAEQLALKgGKKQIQKLETRI 1820
Cdd:pfam00261 128 DLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekasEREDKYEEQIRFLTEKLKEAETRAEF-AERSVQKLEKEV 206
|
170
....*....|....*.
gi 98986453 1821 RELEFELEGEQKKNTE 1836
Cdd:pfam00261 207 DRLEDELEAEKEKYKA 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1228-1417 |
1.90e-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: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1228 EIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQ 1307
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1308 --------------------------AFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRA 1361
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 1362 LSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEK 1417
Cdd:COG3883 177 QAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1572-1940 |
1.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1572 EIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQL 1651
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1652 KDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKL 1731
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1732 ETDLMQLQSEVEdaSRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKK 1811
Cdd:COG4372 163 QEELAALEQELQ--ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1812 QIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQAN 1891
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 98986453 1892 AHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE 1940
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
836-1051 |
1.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ 915
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 916 LEAKIKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEELSGLDETIAKLTR 995
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELEAEFDEARI 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 996 EKkaLQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLER 1051
Cdd:PRK02224 649 EE--AREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1373-1506 |
2.00e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 43.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1373 RTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdK 1452
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 98986453 1453 VLAEWKTKCEESQAELEASLKESRSLSTELFKlknayeeALDQLETVKRENKNL 1506
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQ-------VLDKVQEIHEDCSVL 131
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
836-1094 |
2.01e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEeRCDQLIKAKF- 914
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELT-RVNELLKAKFs 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 915 ------QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKD-------IDDLELTLAKVEKEKHATENKVKNLTE 981
Cdd:pfam15905 147 edgtqkKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNlehskgkVAQLEEKLVSTEKEKIEEKSETEKLLE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 982 ELSGLDETIAKLTREKKALQeahqQALDDLQAEEDKVNSLnktKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLegdLK 1061
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDIA----QLEELLKEKNDEIESL---KQSLEEKEQELSKQIKDLNEKCKLLESEKEEL---LR 296
|
250 260 270
....*....|....*....|....*....|...
gi 98986453 1062 LAQESILDLENDKQQLDERLKKKDFEYCQLQSK 1094
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
855-1111 |
2.07e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 855 EEFQKTKDELAKSEAKR-KELEEKLvtlvQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEI 933
Cdd:pfam02029 59 DEEEAFLDRTAKREERRqKRLQEAL----ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 934 NAELTAKKRKLEDECSELK---KDIDDLELTLAKVEKEKHATEN-KVKNLTEELSGLDETIAKLTREKKALQEAHQQALD 1009
Cdd:pfam02029 135 IREKEYQENKWSTEVRQAEeegEEEEDKSEEAEEVPTENFAKEEvKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1010 DLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKL----RVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKD 1085
Cdd:pfam02029 215 EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLeelrRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLE 294
|
250 260
....*....|....*....|....*.
gi 98986453 1086 FEYCQLQSKVEDEQTLGLQFQKKIKE 1111
Cdd:pfam02029 295 EEEQRRKQEEAERKLREEEEKRRMKE 320
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
872-1097 |
2.18e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 872 KELEEKLVTLVQEKNDLQ---LQVQAESENLLDAEERcdqLIKAKFQLEaKIKEVteraedeeeINAELTAKKRKLEDEC 948
Cdd:PRK05771 15 KSYKDEVLEALHELGVVHiedLKEELSNERLRKLRSL---LTKLSEALD-KLRSY---------LPKLNPLREEKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 949 SELKKDIDDLELTLAKVEKEkhatenkVKNLTEELSGLDETIAKLTREKKALQ--EAHQQALDDLQAEED---KVNSLNK 1023
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1024 TK-SKLEQQVEDLESSLEQEKKLR-----VDLERNKRKLEGDLKLAQESILDLENDKqQLDERLKKKDFEYCQLQSKVED 1097
Cdd:PRK05771 155 DKlEELKLESDVENVEYISTDKGYvyvvvVVLKELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1003 |
2.19e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 839 PLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEA 918
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 919 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE---LT----LAKVEKEKHATENKVKNLTEELSGLDETIA 991
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaieeYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 98986453 992 KLTREKK-ALQEA 1003
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
844-1113 |
2.22e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 924 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEA 1003
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1004 HQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKK 1083
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270
....*....|....*....|....*....|
gi 98986453 1084 KDFEYCQLQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELK 296
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1341-1541 |
2.24e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1341 CDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQ 1420
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1421 RLQGEVEDLM------VDVERAN---SLAAALDKKQRNFDKVLaewKTKCEESQAELEASLKE--------SRSLSTELF 1483
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLLLgfkYVSVFVGTVPEDKLEEL---KLESDVENVEYISTDKGyvyvvvvvLKELSDEVE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 98986453 1484 KL-----------------KNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELeksrKQIELEKADI 1541
Cdd:PRK05771 195 EElkklgferleleeegtpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY----LEIELERAEA 265
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
903-1044 |
2.62e-03 |
|
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: 41.93 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 903 EERCDQLIKAKFQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 981
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 98986453 982 ELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKK 1044
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1315-1474 |
3.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1315 ELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKyetdaiqrteeLEEAKKKL 1394
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-----------IKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1395 AQrlQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKE 1474
Cdd:COG1579 83 GN--VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1570-1916 |
3.15e-03 |
|
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: 42.65 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1570 KSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRsvqg 1649
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD---- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1650 QLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKK 1729
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1730 KLETDLMQLQSEVEDASRDARNA----EEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNLEQTVKDLQHRLDEAEQLA 1805
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEK-LQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1806 LKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEE 1885
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350
....*....|....*....|....*....|.
gi 98986453 1886 adEQANAHLTKFRKAQHELEEAEERADIAES 1916
Cdd:pfam02463 470 --SEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
848-1044 |
3.39e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQ--------------AESENLLDAEERCDQLIKAK 913
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleeelerteerlaEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 914 FQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKL 993
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 994 -TREKKALQ------EAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKK 1044
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
949-1267 |
3.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 949 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKL 1028
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1029 EQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKK 1108
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1109 IKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEA 1188
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1189 MVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEI 1267
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
981-1085 |
3.56e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 981 EELSGLDETIAKLTREKKAL----QEAHQQALDDLQAEEDKvnslnktkskLEQQVEDLESSLEQEKKLRVDLERNKRKL 1056
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100
....*....|....*....|....*....
gi 98986453 1057 EGDlklaQESILDLENDKQQLDERLKKKD 1085
Cdd:COG0542 481 EQR----YGKIPELEKELAELEEELAELA 505
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
863-999 |
3.65e-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: 41.67 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 863 ELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEE-RCDQLIkakfqLEAKIKEVTERAEdeeEINAELTAKK 941
Cdd:pfam10186 27 DLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRLlKSEVAI-----SNERLNEIKDKLD---QLRREIAEKK 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 942 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKA 999
Cdd:pfam10186 99 KKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
954-1056 |
3.68e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 954 DIDDLELTLAKVEKEKHATENkvknltEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVE 1033
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 98986453 1034 DLESSLEQEKKLRVDLERNKRKL 1056
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1251-1402 |
3.87e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 41.64 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1251 RTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNaL 1330
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV-L 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 98986453 1331 AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKY----ETDAIQRTEELEEAKKKLAQRLQDSE 1402
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENqaevRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1202-1338 |
3.98e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1202 AELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARgKNEEIQRSLSELTTQKSRL 1281
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEALQKEIESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1282 QT---EAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSR 1338
Cdd:COG1579 106 SDledEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1296-1408 |
4.03e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 41.53 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1296 ESIVSQLSRSKQAFTQQTEELKRQLEEENKAKnALAHALqSSRHDCDLLREQYEEEQEGKAELQRALSKANSEvaQWRTK 1375
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 98986453 1376 YEtDAIQRTEELEEAKKKLAQRLQDSEEQVEAV 1408
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
831-1002 |
4.18e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 831 MKLFFKIKPLLKSAETEKEMATMKeeFQKTKDELAKSEAKRKELEEKLVTLVQEKNDlqlqVQAESENLLDAEERCDQLI 910
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGK--LQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE----EKSETEKLLEYITELSCVS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 911 KakfQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDL--ELTLAKVEKEKHATENKVK--NLTEELSGL 986
Cdd:pfam15905 236 E---QVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLneKCKLLESEKEELLREYEEKeqTLNAELEEL 312
|
170
....*....|....*.
gi 98986453 987 DETIAKLTREKKALQE 1002
Cdd:pfam15905 313 KEKLTLEEQEHQKLQQ 328
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1048-1852 |
4.25e-03 |
|
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: 42.02 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1048 DLERNKRKLEGDLKLAQESILDL-----ENDKQQLDERLKKKDFE--------YCQLQSKVEDEQTLGLQFQKKIKELQA 1114
Cdd:pfam05483 27 NLSKNGENIDSDPAFQKLNFLPMleqvaNSGDCHYQEGLKDSDFEnseglsrlYSKLYKEAEKIKKWKVSIEAELKQKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1115 RIEELEEEIEAERATRAKTE--------------KQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLE 1180
Cdd:pfam05483 107 KLQENRKIIEAQRKAIQELQfenekvslkleeeiQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1181 EATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEA 1260
Cdd:pfam05483 187 DLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1261 RGKNEEIQrslselttQKSRLQTEAgelsrqleekesiVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHD 1340
Cdd:pfam05483 267 RDKANQLE--------EKTKLQDEN-------------LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1341 CDLLREQYEEEQEgkaELQRALSKANSEVAQWRTKyetdaiqrTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQ 1420
Cdd:pfam05483 326 ICQLTEEKEAQME---ELNKAKAAHSFVVTEFEAT--------TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1421 RLQGEVEDLMVDVERANSLAAALDK---KQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLE 1497
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1498 TVKREnknLEQEIADLTEQIAENGKTIHEleksrkqielekadiqlaleeaeaaleheeakilriQLELTQVKSEIDRKI 1577
Cdd:pfam05483 475 DLKTE---LEKEKLKNIELTAHCDKLLLE------------------------------------NKELTQEASDMTLEL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1578 AEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKdtqlh 1657
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK----- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1658 lddalrgqedlkeqlaIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQ----NTSLIHTKKKLET 1733
Cdd:pfam05483 591 ----------------ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvnklELELASAKQKFEE 654
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1734 DLMQLQSEVEDASRDARN---AEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNLEQTVKDLQHRLDEaeqLALKG 1808
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKlleEVEKAKAIADEAVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSE---LGLYK 731
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 98986453 1809 GKKQIQK-----LETRIRELEFELEGEQKKNTESVKGLRKYERRVKELT 1852
Cdd:pfam05483 732 NKEQEQSsakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1174-1406 |
4.37e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1174 KLRRDLEEATlqheamvAALRKKHADSVAELGEQIDNLQRVKQKLEKEKsEFKLEIDDLsssmesvskskanlEKICRTL 1253
Cdd:PRK10929 27 QITQELEQAK-------AAKTPAQAEIVEALQSALNWLEERKGSLERAK-QYQQVIDNF--------------PKLSAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1254 EDQLSEARGKNEEIQRSLSELTTQKSRLQTEAG--ELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEE--------- 1322
Cdd:PRK10929 85 RQQLNNERDEPRSVPPNMSTDALEQEILQVSSQllEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEierrlqtlg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1323 -----ENKAKNALAHALQSSRHdcdLLREQYEEEQEgKAELQRALSKANSEVAQWRTKyETDAiqrteELEEAKKKL-AQ 1396
Cdd:PRK10929 165 tpntpLAQAQLTALQAESAALK---ALVDELELAQL-SANNRQELARLRSELAKKRSQ-QLDA-----YLQALRNQLnSQ 234
|
250
....*....|
gi 98986453 1397 RLQDSEEQVE 1406
Cdd:PRK10929 235 RQREAERALE 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-982 |
4.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 844 AETEKEMATMKEEFQKTKDELAKSE---------AKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKF 914
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 915 QLEAKIKEVTERAEDEEEinaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE 982
Cdd:COG4717 178 ELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1338-1620 |
4.98e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.63 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1338 RHDCDLLREQYEEEQEgKAELQRALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQ---RLQDSEEQVEA 1407
Cdd:pfam03528 1 QPDEDLQQRVAELEKE-NAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLkrqnavlQEAQVELDAlqnQLALARAEMEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1408 VNAKCASLEKTKQRLQGEVEDLMVdvERANSLAAALDKKQRNF--------DKVLAEWKTKCEESQAELeASLKESRSLS 1479
Cdd:pfam03528 80 IKAVATVSENTKQEAIDEVKSQWQ--EEVASLQAIMKETVREYevqfhrrlEQERAQWNQYRESAEREI-ADLRRRLSEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1480 TELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQ-----IELEKAdiqlaleeaEAALEH 1554
Cdd:pfam03528 157 QEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKelnhyLEAEKS---------CRTDLE 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1555 EEAKILRIQLELTQVKSEIDRK-IAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKME 1620
Cdd:pfam03528 228 MYVAVLNTQKSVLQEDAEKLRKeLHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRME 294
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1244-1926 |
5.49e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1244 ANLEKICRTLEDQLSEA--------RGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKqafTQQTEE 1315
Cdd:NF041483 364 AQLAKAARTAEEVLTKAsedakattRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAK---TVELQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1316 LKRQLEEENKAKNALAHAlQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQ-RTEELEEA---K 1391
Cdd:NF041483 441 EARRLRGEAEQLRAEAVA-EGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERvRTEAIERAttlR 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1392 KKLAQRLQDSEEQVEAVNAKCASL-EKTKQRLQGEVEDLMVDVERanslaaALDKKQRNFDKVLAEWKTKCEESQAELEA 1470
Cdd:NF041483 520 RQAEETLERTRAEAERLRAEAEEQaEEVRAAAERAARELREETER------AIAARQAEAAEELTRLHTEAEERLTAAEE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1471 SLKESRSLSTELFKlknayeEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQ---LALEE 1547
Cdd:NF041483 594 ALADARAEAERIRR------EAAEETERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRlrsEAAAE 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1548 AEAALEHEEAKILRIQLELT----QVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAE-VRSRNEAIRL----KKK 1618
Cdd:NF041483 668 AERLKSEAQESADRVRAEAAaaaeRVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQErERAREQSEELlasaRKR 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1619 MEGDLNEIEIQLSHANRQAAETL----KHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAivERRANLLQAEVEELRA--- 1691
Cdd:NF041483 748 VEEAQAEAQRLVEEADRRATELVsaaeQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAA--ERTRTEAQEEADRVRSday 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1692 ----------------TLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLmqLQSEVEDASRDARNAEEK 1755
Cdd:NF041483 826 aererasedanrlrreAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDT--LASAEQDAARTRADARED 903
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1756 AKKAITDAAMMAEELKKEQDTSAHLERmkknlEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNT 1835
Cdd:NF041483 904 ANRIRSDAAAQADRLIGEATSEAERLT-----AEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAA 978
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1836 ESVKG-------LRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEAdEQANAHLTKFRKAQHEL---- 1904
Cdd:NF041483 979 ETVGSaqqhaerIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAA-EQADTLITEAAAEADQLtaka 1057
|
730 740
....*....|....*....|...
gi 98986453 1905 -EEAEERADIAESQVNKLRAKTR 1926
Cdd:NF041483 1058 qEEALRTTTEAEAQADTMVGAAR 1080
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1174-1427 |
5.58e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1174 KLRRDLEEATLQHEamvaaLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDlsssmesvsksKANLEKICRTL 1253
Cdd:pfam15905 64 KSQKNLKESKDQKE-----LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVRE-----------KTSLSASVASL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1254 EDQLSEARGKNEEIQRSLSELTTQKsRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHA 1333
Cdd:pfam15905 128 EKQLLELTRVNELLKAKFSEDGTQK-KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1334 LQSSRHDCDLLREQYEEEQEGKAELQ---RALSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNA 1410
Cdd:pfam15905 207 LVSTEKEKIEEKSETEKLLEYITELScvsEQVEKYKLDIAQ----LEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNE 282
|
250
....*....|....*..
gi 98986453 1411 KCASLEKTKQRLQGEVE 1427
Cdd:pfam15905 283 KCKLLESEKEELLREYE 299
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1464-1707 |
6.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1464 SQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKsrkqielekadiql 1543
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1544 aleeaeaaleheeakilriqleltqvkseidrKIAEKDEEIEQLKRNYQRTVETMqSALDAEVRSRNeairlkkkmEGDL 1623
Cdd:COG3883 80 --------------------------------EIEERREELGERARALYRSGGSV-SYLDVLLGSES---------FSDF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1624 NEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLA 1703
Cdd:COG3883 118 LDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
....
gi 98986453 1704 EQEL 1707
Cdd:COG3883 198 LAEL 201
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1328-1533 |
6.59e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1328 NALAHALQSSRHDCDLLREQyeeeqegkaelqraLSKANSEVAQWRTKYETDAIQRTEELEEAKkklaQRLQDSEEQVEA 1407
Cdd:pfam09787 43 TALTLELEELRQERDLLREE--------------IQKLRGQIQQLRTELQELEAQQQEEAESSR----EQLQELEEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1408 VNAKCASLEKTKQRLQGEVEDLMVDVERA-NSLAAALDKKQRNFDKVLAEWKTKC--EESQAELEASLKE-SRSL---ST 1480
Cdd:pfam09787 105 ERSARREAEAELERLQEELRYLEEELRRSkATLQSRIKDREAEIEKLRNQLTSKSqsSSSQSELENRLHQlTETLiqkQT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 98986453 1481 ELFKLKNAYEEALDQLETVKRENKNLEQEIADlteQIAENGKTIHELEKSRKQ 1533
Cdd:pfam09787 185 MLEALSTEKNSLVLQLERMEQQIKELQGEGSN---GTSINMEGISDGEGTRLR 234
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
982-1136 |
7.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 982 ELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLE--QEKKLRVDLERNKRKLEGD 1059
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 98986453 1060 LKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTlglQFQKKIKELQARIEELEEEIEAERATRAKTEKQ 1136
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
911-1247 |
8.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 911 KAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETI 990
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 991 AKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDL 1070
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1071 ENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSER 1150
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1151 LEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEID 1230
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330
....*....|....*..
gi 98986453 1231 DLSSSMESVSKSKANLE 1247
Cdd:COG4372 330 LALAILLAELADLLQLL 346
|
|
| BAR_SNX7_30 |
cd07624 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ... |
956-1063 |
8.50e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX7, SNX30, and similar proteins. The specific functions of SNX7 and SNX30 have not been elucidated. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153308 Cd Length: 200 Bit Score: 39.67 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 956 DDLELTLAKVEKEKHATENKVKNLTEELsgldetiAKLTREKKALQEAHQQAL---DDLQAE-EDKVNSLNKTKSKLEQQ 1031
Cdd:cd07624 70 PLLEGVSSAVERCTAALEVLLSDHEFVF-------LPPLREYLLYSDAVKDVLkrrDQFQIEyELSVEELNKKRLELLKE 142
|
90 100 110
....*....|....*....|....*....|...
gi 98986453 1032 VEDLESSLE-QEKKLRVDLERNKRKLEGDLKLA 1063
Cdd:cd07624 143 VEKLQDKLEcANADLKADLERWKQNKRQDLKKI 175
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
925-1108 |
8.87e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.74 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 925 ERAEDEEEINAELTAKKRKL------EDECSELKkdiddleltlakvekekhateNKVKNLTEELSGLDETIAKLTREKK 998
Cdd:PRK10361 33 EQLAEREEMVAELSAAKQQItqsehwRAECELLN---------------------NEVRSLQSINTSLEADLREVTTRME 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 999 ALQeahqqalddlQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDlERNKRKLEGDLKLAQESildLENDKQQLD 1078
Cdd:PRK10361 92 AAQ----------QHADDKIRQMINSEQRLSEQFENLANRIFEHSNRRVD-EQNRQSLNSLLSPLREQ---LDGFRRQVQ 157
|
170 180 190
....*....|....*....|....*....|
gi 98986453 1079 ERLKKKDFEYCQLQSKVEDEQTLGLQFQKK 1108
Cdd:PRK10361 158 DSFGKEAQERHTLAHEIRNLQQLNAQMAQE 187
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1683-1910 |
8.91e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1683 QAEVEELRATLEQTERarKLAEQELLDSNERVQLLHTQNTSlihtKKKLETDLMQLQsEVEDASRDARNAEEKAKKAITD 1762
Cdd:pfam05557 1 RAELIESKARLSQLQN--EKKQMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 1763 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-DEAEQLalkggKKQIQKLETRIRELEFELEGEQKKNTESVKGL 1841
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 98986453 1842 RKYERRVKELTYQSEEDRKNVLRLQDLVDKLQvkvkSYKRQAEEAdEQANAHLTKFRKAQHELEEAEER 1910
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ----SQEQDSEIV-KNSKSELARIPELEKELERLREH 212
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
857-1113 |
8.91e-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: 40.99 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 857 FQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIK-----------AKFQLEAKIKEVTE 925
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKtllanrfsygpAIDELEKQLAEIEE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 926 R---------------AEDE-EEINAELTAKKRKLED------ECS-ELKKDIDDLELTLAKVEKEKHA-----TENKVK 977
Cdd:pfam06160 161 EfsqfeeltesgdyleAREVlEKLEEETDALEELMEDipplyeELKtELPDQLEELKEGYREMEEEGYAlehlnVDKEIQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 98986453 978 NLTEELSGLDETIAKLTREK-----KALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLEsslEQEKKLRVDLER- 1051
Cdd:pfam06160 241 QLEEQLEENLALLENLELDEaeealEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAE---EQNKELKEELERv 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 98986453 1052 ------NKRKLEgDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQ 1113
Cdd:pfam06160 318 qqsytlNENELE-RVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFK 384
|
|
| |
