|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1339.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHF 579
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGGKKKGSSFQTVSAVFRENL 659
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 660 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 739
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 124486959 740 IDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-770 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1326.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKE--SGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd01377 159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd01377 239 ILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd01377 319 EQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPtkGKAEAH 578
Cdd:cd01377 399 QEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEAH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 579 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAggkkgGKKKGSSFQTVSAVFREN 658
Cdd:cd01377 477 FILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGK-----KKKKGGSFRTVSQLHKEQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 659 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 738
Cdd:cd01377 552 LNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGF 631
|
650 660 670
....*....|....*....|....*....|..
gi 124486959 739 FIDSKnASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01377 632 DDGKA-ACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1319.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKD-SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd14913 240 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHF 579
Cdd:cd14913 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgdSAGGKKGGKKKGSSFQTVSAVFRENL 659
Cdd:cd14913 480 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--DSGKKKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 660 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 739
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 124486959 740 IDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14913 638 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1226.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEaASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 338
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 498
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 499 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAH 578
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 579 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSAGGKKGGKKKGSSFQTVSAVFREN 658
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEA-EGGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 659 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 738
Cdd:cd14915 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 124486959 739 FIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14915 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1215.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEES-GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd14918 240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14918 320 QQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHF 579
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAggKKGGKKKGSSFQTVSAVFRENL 659
Cdd:cd14918 480 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGA--KKGAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 660 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 739
Cdd:cd14918 558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 124486959 740 IDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14918 638 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1214.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEaTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 338
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 498
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 499 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAH 578
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 579 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSAGGKKGGKKKGSSFQTVSAVFREN 658
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEA-EEGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 659 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 738
Cdd:cd14910 560 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 124486959 739 FIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14910 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1194.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQ-QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEiTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 338
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 498
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 499 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAH 578
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 579 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEA-GDSAGGKKGGKKKGSSFQTVSAVFRE 657
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGaSAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 658 NLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEG 737
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 124486959 738 QFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1178.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGD--KKKEQQPG-KMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 257
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLAtKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 258 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 337
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 338 IDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 417
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 418 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 497
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 498 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKG-KAE 576
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 577 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAE-AGDSAGGKKGGKKKGSSFQTVSAVF 655
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDsTEDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 656 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 735
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 124486959 736 EGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1163.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDK-KKEQQPGKmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRsKKDQTPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 338
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 498
Cdd:cd14917 319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 499 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAH 578
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 579 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgdSAGGKKGGKKKGSSFQTVSAVFREN 658
Cdd:cd14917 479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADA--PIEKGKGKAKKGSSFQTVSALHREN 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 659 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 738
Cdd:cd14917 557 LNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 636
|
650 660 670
....*....|....*....|....*....|..
gi 124486959 739 FIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14917 637 FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1156.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHF 579
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAgGKKGGKKKGSSFQTVSAVFRENL 659
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSG-KGKGGKKKGSSFQTVSALHRENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 660 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 739
Cdd:cd14916 560 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 639
|
650 660 670
....*....|....*....|....*....|.
gi 124486959 740 IDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14916 640 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1058.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQqpgkmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14929 155 LSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd14929 234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14929 314 EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHF 579
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHF 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYagAEAGDSAGGKKGGKKKGSSFQTVSAVFRENL 659
Cdd:cd14929 474 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--ISTDSAIQFGEKKRKKGASFQTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 660 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 739
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKF 631
|
650 660 670
....*....|....*....|....*....|.
gi 124486959 740 IDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14929 632 VSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-770 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1034.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 88 IEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 168 TDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFG 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV-------GRLEEQILQSNPILEAFGNAKTVRNNNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 248 KFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIsTNPFDFPFVSQ-GEVTVASID 326
Cdd:pfam00063 154 KYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 327 DSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRV 406
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 407 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQ-PRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 485
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 486 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNN 564
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 565 FQKPKPtkgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGG--K 642
Cdd:pfam00063 471 FQKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkR 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 643 KKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:pfam00063 548 TKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 124486959 723 KQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:pfam00063 628 VQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 1001.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGdkkKEQQPGKmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG---KQSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 340
Cdd:cd14934 157 AGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 341 LGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 420
Cdd:cd14934 237 LGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 421 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 500
Cdd:cd14934 317 QCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 501 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGK-AEAHF 579
Cdd:cd14934 397 EEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgdsaggkKGGKKKGSSFQTVSAVFRENL 659
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-------SKKQKRGSSFMTVSNFYREQL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 660 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqF 739
Cdd:cd14934 550 NKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-F 628
|
650 660 670
....*....|....*....|....*....|.
gi 124486959 740 IDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14934 629 VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 998.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIavtGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATV---GASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTK-GKAEAH 578
Cdd:cd14909 398 QEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAH 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 579 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGaEAGDSAGGKKGGKKKGSSFQTVSAVFREN 658
Cdd:cd14909 478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-QSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 659 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 738
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE 636
|
650 660 670
....*....|....*....|....*....|..
gi 124486959 739 fiDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14909 637 --DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-782 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 990.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 81 NPPKFDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 161 NAYQFMLTDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKkeqqpgkmqGTLEDQIIQANPLLEAFGNAKTVRN 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---------GSVEDQILESNPILEAFGNAKTLRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 241 DNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTnPFDFPFVSQG-E 319
Cdd:smart00242 152 NNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 320 VTVASIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKAGYLMGLNSAEML 398
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 399 KGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQL 478
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 479 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQ 557
Cdd:smart00242 391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-Q 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 558 HLGKSNNFQKPKPtkgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDsagg 637
Cdd:smart00242 469 HHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSK---- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 638 kkggkkkgSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:smart00242 542 --------KRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486959 718 LYADFKQRYRILNASAIPEGQFiDSKNASEKLLNSIDVDREQFRFGHTKVFFKAGLLGLLEEMRD 782
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-770 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 831.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQ-EAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATIAvtgdKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS----GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELID---LLLISTNPFDFPFVSQGE-VTVASIDDSEELLAT 334
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREelkLELLLSYYYLNDYLNSSGcDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 335 DNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 412
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 413 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 490
Cdd:cd00124 317 ITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 491 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPK 569
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 570 ptkgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSlkllsflfsnyagaeagdsaggkkggkkkgssfq 649
Cdd:cd00124 476 ----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS---------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 650 tvsaVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 729
Cdd:cd00124 518 ----QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 124486959 730 NASAiPEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd00124 594 APGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
38-1229 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 817.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 38 CFAVDDKEMYVKGMIQSRENDKVIVK-TLDDRELTLNS-----DQVFPMNPPKFDKIEDMAMMTHLHEPAVLYNLKERYA 111
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTeEGKKEDGESVSvkkkvLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 112 AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAGKTVNTKR 191
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 192 VIQYFAtiAVTGDKkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLE 271
Cdd:COG5022 172 IMQYLA--SVTSSS------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 272 KSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVT-VASIDDSEELLATDNAIDILGFSPEEKVG 350
Cdd:COG5022 244 KSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 351 IYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALA 430
Cdd:COG5022 323 IFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 431 KAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW 510
Cdd:COG5022 402 KALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 511 EFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSNNFQKPKptkgKAEAHFSLVHYAGT 587
Cdd:COG5022 482 SFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSR----FRDNKFVVKHYAGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 588 VDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEagdsaggkkggkkKGSSFQTVSAVFRENLNKLMTNLR 667
Cdd:COG5022 557 VEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------SKGRFPTLGSRFKESLNSLMSTLN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 668 STHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFI---DSKN 744
Cdd:COG5022 624 STQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKN 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 745 ASEKLLNSIDVDREQFRFGHTKVFFKAGLLGLLEEMRDEKLVTLMTRTQAVCRGYLMRVEFKKMMERRESIFCIQYNVRS 824
Cdd:COG5022 704 AVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 825 FMNVKHWPWMNLFFKIKPLLKSAEAEKEMatmkEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENlmd 904
Cdd:COG5022 784 RRLVDYELKWRLFIKLQPLLSLLGSRKEY----RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLK--- 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 905 AEERCEGLIKSKIQLEAKvkelnerleeeeemnselvAKKRNLEDKCSSLKRDIDDLE-LTLTKVEKEKHATENK---VK 980
Cdd:COG5022 857 AKKRFSLLKKETIYLQSA-------------------QRVELAERQLQELKIDVKSISsLKLVNLELESEIIELKkslSS 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 981 NLSEEMTALEETISKLTKEKKSLQEAHQQTLDdlQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLE 1060
Cdd:COG5022 918 DLIENLEFKTELIARLKKLLNNIDLEEGPSIE--YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELK 995
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1061 G---DLKMSQESIMDLENDTQQLEEKLKKKEFEMSqlQTRIDDEQVLSLQLQKKIKELQaRTEELEEEIEAEHTVRAKIE 1137
Cdd:COG5022 996 NfkkELAELSKQYGALQESTKQLKELPVEVAELQS--ASKIISSESTELSILKPLQKLK-GLLLLENNQLQARYKALKLR 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1138 KQRSDLARELEEISERLE-EASGATSAQIEMNKKRESEFQKLRRDLeeatlqheaTAATLRKKHADTVAELGEQ-IDNLQ 1215
Cdd:COG5022 1073 RENSLLDDKQLYQLESTEnLLKTINVKDLEVTNRNLVKPANVLQFI---------VAQMIKLNLLQEISKFLSQlVNTLE 1143
|
1210
....*....|....
gi 124486959 1216 RVKQKLEKEKSELK 1229
Cdd:COG5022 1144 PVFQKLSVLQLELD 1157
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 777.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAV------TGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 254
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAAskpkgsGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 255 GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVASIDDSEELLAT 334
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 335 DNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 413
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 414 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 492
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 493 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgksNNFQKPKPTK 572
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH----SMHPKFMKTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 573 GKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSlklLSFLFSNYAGAEAGDSAGGKKGGKKKGSS----- 647
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ---DPFVVNIWKDAEIVGMAQQALTDTQFGARtrkgm 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 648 FQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYR 727
Cdd:cd14911 553 FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486959 728 ILNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14911 633 LLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 764.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKD---HNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 496
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 497 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKPTKG 573
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 574 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN------YAGAEAGDSAGGKKGGKKKGSS 647
Cdd:cd14920 474 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrivgLDQVTGMTETAFGSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 648 FQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYR 727
Cdd:cd14920 552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486959 728 ILNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14920 632 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 708.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKM-QGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAI 338
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYSKYR--FLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 417
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 418 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 496
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 497 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKptKG 573
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 574 KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAE--AGDSAGGKKGGKKKGSSF 648
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDkvAGMGESLHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 649 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 728
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486959 729 LNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-770 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 690.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATiaVTGDKKKEQQpgkmqgtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFAT--VGGSSSGETQ-------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNK-KPELIDLLLisTNPFDFPFVSQGE-VTVASIDDSEELLATDN 336
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETRK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 416
Cdd:cd01380 230 ALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 417 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 494
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 495 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNN-FQKPKPTKG 573
Cdd:cd01380 390 VFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 574 KaeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLlsflfsnyagaeagdsaggkkggkkkgssfQTVSA 653
Cdd:cd01380 469 A----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK------------------------------KTVGS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 654 VFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 733
Cdd:cd01380 515 QFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK 594
|
650 660 670
....*....|....*....|....*....|....*..
gi 124486959 734 ipEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01380 595 --EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 687.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTS---ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14921 159 VGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 497
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 498 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPTKGK 574
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 575 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGGKKKGSS------F 648
Cdd:cd14921 475 TE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASktkkgmF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 649 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 728
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486959 729 LNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 670.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14919 156 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYR--FLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 497
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 498 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPTKGK 574
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 575 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGG------KKKGSSF 648
Cdd:cd14919 472 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalpgafKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 649 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 728
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486959 729 LNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14919 630 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-770 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 668.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKM-QGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAI 338
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLrSELLLENYN--NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 497
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 498 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKptKGK 574
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 575 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGG----KKKGSSFQT 650
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMpgafKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 651 VSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILN 730
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486959 731 ASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd15896 637 PNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-770 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 648.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqPGkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKE--PG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEELLATD 335
Cdd:cd14930 159 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------ERELFQETL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 336 NAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 414
Cdd:cd14930 232 ESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 415 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 492
Cdd:cd14930 311 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 493 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPK 569
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 570 PTKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSAGGKKGGKKKG 645
Cdd:cd14930 469 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPGGRPRR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 646 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 725
Cdd:cd14930 547 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124486959 726 YRILNASAIPEGqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14930 627 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-770 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 634.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRgkKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFAtiAVTGDKkkeqqpgkmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLA--ALGGGS----------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTnPFDFPFVSQGE-VTVASIDDSEELLATDNAI 338
Cdd:cd01383 147 ICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 418
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 419 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDT-KQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 497
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 498 LEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFqkpkptKGKAE 576
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 577 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYagAEAGDSAGGKKGGKKKGSSFQTVSAVFR 656
Cdd:cd01383 458 GAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKM--LDASRKALPLTKASGSDSQKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 657 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 736
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSA 615
|
650 660 670
....*....|....*....|....*....|....
gi 124486959 737 GQfiDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01383 616 SQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-770 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 615.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFAtiAVTGDKKKEQQPGKmqgtleDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIA--AVSGGSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 340
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 341 LGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY---VTKGQ 417
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 418 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHhmF 496
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--L 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 497 VL--EQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSNNFQKPKPTK 572
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 573 GKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNyaGAEAGDSAGGKkggkkkgssfqTVS 652
Cdd:cd01378 469 ELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE--GVDLDSKKRPP-----------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 653 AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAS 732
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486959 733 AIPEGQFIDSKNAsEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01378 616 TWPAWDGTWQGGV-ESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-770 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 615.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAIS-----------GQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIsTNPFDFPFVSQGE-VTVASIDDSEELLATDNAID 339
Cdd:cd01381 150 EGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 417
Cdd:cd01381 229 VLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 418 NVQQVTNSVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 493
Cdd:cd01381 309 SAEQALDVRDAFVKGIYGRLFIWIVNKINsaiyKPRGTDSSRTS-IGVLDIFGFENFEVNSFEQLCINFANENLQQFFVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 494 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPkptK 572
Cdd:cd01381 388 HIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP---K 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 573 GKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSAGGKkggkkkgssfQTVS 652
Cdd:cd01381 463 SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS-ETRKKS----------PTLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 653 AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILnAS 732
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 124486959 733 AIPEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-770 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 607.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFAtiAVTGDKKKEQQpgkmqgtledQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTNNHSWVEQ----------QILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK--PELIDLLLIStNPFDFPFVSQ-GEVTVASIDDSEELLATDNA 337
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLG-EPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 338 IDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 416
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 417 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 496
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 497 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPTKGKA 575
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 576 EahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFS---NYAGAEAGDSAGGKKGGKKKGSSFQTVS 652
Cdd:cd14883 467 E--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdLLALTGLSISLGGDTTSRGTSKGKPTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 653 AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNA- 731
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPr 624
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 124486959 732 --SAIPEGQFIDSKNasekLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14883 625 arSADHKETCGAVRA----LMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-770 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 589.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATIAvtgdkKKEQQPGKmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----GRAVTEGR---SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTfQLSS-ERSYHIFYQIMSNKKPELIDLLLISTnPFDFPFVSQGE-VTVASIDDSEELLATDN 336
Cdd:cd01384 153 RISGAAIRTYLLERSRVV-QVSDpERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDILGFSPEEKVGIYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADK--------AGYLMGLNSAEMLKGLCCPRVKV 408
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 409 GNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 488
Cdd:cd01384 306 PDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 489 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQK 567
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 568 PKptkgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSaggkkggkkkgSS 647
Cdd:cd01384 464 PK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSS-----------SK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 648 FQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYR 727
Cdd:cd01384 529 FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486959 728 ILnASAIPEGQFiDSKNASEKLLNSIDVdrEQFRFGHTKVFFK 770
Cdd:cd01384 609 LL-APEVLKGSD-DEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-770 |
2.48e-168 |
|
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: 528.74 E-value: 2.48e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 182 GAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESW-----------GSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 262 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLListnpfdfpfvsqgevTVASIDDSEELLATDNAIDIL 341
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 342 GFSPEEKVGIYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------AGYLMGLNSAEMLKGLCCpRVKVGNEY 412
Cdd:cd01382 217 GLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 413 VTKGQ------NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 486
Cdd:cd01382 291 GAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 487 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksNNF 565
Cdd:cd01382 370 LQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NHF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 566 QKPKPTKGKAEAH--------FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFsnyagaEAGDSAGG 637
Cdd:cd01382 446 RLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------ESSTNNNK 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 638 KKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd01382 520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124486959 718 LYADFKQRYRILNASAIPEgqfIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-770 |
7.00e-168 |
|
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: 527.81 E-value: 7.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-----------GGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNpfdfpFVSQGEVTVASID---DSEELLATD 335
Cdd:cd14903 150 TLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANE-----CAYTGANKTIKIEgmsDRKHFARTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 336 NAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 413
Cdd:cd14903 225 EALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 414 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 493
Cdd:cd14903 305 TVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 494 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKg 573
Cdd:cd14903 385 DVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 574 kaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGGKKKGSSFQTVSA 653
Cdd:cd14903 463 ---TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTTTT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 654 V---FRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILn 730
Cdd:cd14903 540 VgtqFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF- 618
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486959 731 asaIPEGQFIDSKNAS--EKLLNSIDVDR-EQFRFGHTKVFFK 770
Cdd:cd14903 619 ---LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-770 |
1.31e-166 |
|
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: 524.64 E-value: 1.31e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRgKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHF---- 254
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS--------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 255 -----GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMS-----------------------NKKPELIDLLLI- 305
Cdd:cd14888 152 skrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 306 STNPFDFPFVSqGEVTVASIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEV 382
Cdd:cd14888 232 PHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 383 ADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGV 461
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 462 LDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELI-EKPMGIFSILEEEC 540
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 541 MFPKATDTSFKNKLYDQHLGkSNNFQ--KPKPTKgkaeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKL 618
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKG-HKRFDvvKTDPNS------FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 619 LSFLFSNYAGAEAGDSAGGKKggkkkgssFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLR 698
Cdd:cd14888 543 ISNLFSAYLRRGTDGNTKKKK--------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLK 614
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 699 CNGVLEGIRICRKGFPSRILYADFKQRYRILnasaipegqfidsKNASEKLLNSIdvdreqFRFGHTKVFFK 770
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRIL-------------LNGEGKKQLSI------WAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-770 |
6.77e-166 |
|
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: 522.03 E-value: 6.77e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTgdkkkeqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTnpfDFPFVSQGE-VTVASIDDSEELLATDNAI 338
Cdd:cd14872 149 ICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLSGcIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEP----DGTEVADKAGyLMGLNSAEMLKGLCCPRVKVgneyvt 414
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGstvaNRDVLKEVAT-LLGVDAATLEEALTSRLMEI------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 415 KGQNV-------QQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 486
Cdd:cd14872 299 KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 487 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnnF 565
Cdd:cd14872 379 LQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--T 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 566 QKPKPTKGkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEagdsaggkkggkkkG 645
Cdd:cd14872 456 FVYAEVRT-SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQ--------------K 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 646 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 725
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124486959 726 YRILNaSAIPEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14872 601 YRFLV-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-770 |
3.49e-164 |
|
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: 517.79 E-value: 3.49e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAY-QFM---LTDRDNQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 176 LITGESGAGKTVNTKRVIQYFATI-------AVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGK 248
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARItsgfaqgASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 249 FIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIsTNPFDFPFVSQGEVTVASIDDS 328
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL-QTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 329 EELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKAGYLMGLNSAEMLKGLCCPRVK 407
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 408 VGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 487
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 488 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYDQHLGK 561
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 562 SN------------NFQKPKPTKGKaeaHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSflfsnyaga 629
Cdd:cd14890 479 SGsggtrrgssqhpHFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIRE--------- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 630 eagdsaggkkggkkkgssfQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRIC 709
Cdd:cd14890 547 -------------------VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIR 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 710 RKGFPSRILYADFKQRYRILNASAipegqfiDSKNASEKLLNSI-DVDREQFRFGHTKVFFK 770
Cdd:cd14890 608 QQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-768 |
4.92e-160 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 506.25 E-value: 4.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAY------RGKKRQEAPPHIFSISDNAYQFMLTDRD-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 172 --NQSILITGESGAGKTVNTKRVIQYFATIAVtgdKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKF 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS---ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 250 IRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKP-ELIDLLLISTNPFDFPFVSQGEVTVASIDDS 328
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 329 EELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEV-ADKAGYLMGLNSAEMLKGLCCPRVK 407
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 408 VGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQP--RQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 485
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 486 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNN 564
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 565 FQKPKPTKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSflfsnyagaeagdsaggkkggkkk 644
Cdd:cd14901 476 FSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 645 gssfQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 724
Cdd:cd14901 530 ----STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 124486959 725 RYRILNAS------AIPEGQFIDSKNASEKLLNSIDVDReqFRFGHTKVF 768
Cdd:cd14901 606 TYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPP--FQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-770 |
8.53e-160 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 506.91 E-value: 8.53e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 183 AGKTVNTKRVIQYFATIAvtgdkkkeqQPGKMQGTlEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 262
Cdd:cd01385 84 SGKTESTNFLLHHLTALS---------QKGYGSGV-EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 263 ADIETYLLEKSRVTFQLSSERSYHIFYQIMSNkKPELIDLLLISTNPFDFPFVSQGE-VTVASIDDSEELLATDNAIDIL 341
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAG-ASEEERKELHLKQPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 342 GFSPEEKVGIYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 419
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 420 QQVTNSVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 495
Cdd:cd01385 313 PEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 496 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYDQHLGKSNNFQKPKptkgK 574
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----V 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 575 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLK------------------LLSFLFSNYAGAEAG---- 632
Cdd:cd01385 467 MEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAfvreligidpvavfrwavLRAFFRAMAAFREAGrrra 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 633 -----------DSAGGKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNG 701
Cdd:cd01385 547 qrtaghsltlhDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTG 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 702 VLEGIRICRKGFPSRILYADFKQRYRILnasaIPEGQfIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd01385 627 MLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-770 |
2.05e-158 |
|
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: 501.98 E-value: 2.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAvtgdkkkeQQPGKMQgtlEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVN--------QRRNNLV---TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQI---MSNKKPELIDLLlistNPFDFPFVSQG-EVTVASIDDSEELLATDN 336
Cdd:cd01387 150 VGAITSQYLLEKSRIVTQAKNERNYHVFYELlagLPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADKA-----GYLMGLNSAEMLKGLCCPRVKVGNE 411
Cdd:cd01387 226 AMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDAeiqwvAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 412 YVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 491
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 492 NHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKp 570
Cdd:cd01387 384 NKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 571 tKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAgaeagdSAGGKKGGKKKGSSF-- 648
Cdd:cd01387 461 -MPLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR------AQTDKAPPRLGKGRFvt 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 649 -----QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFK 723
Cdd:cd01387 532 mkprtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFI 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 124486959 724 QRYRILNASAIPEGQFIDSKNASEKLLNSIdVDREQFRFGHTKVFFK 770
Cdd:cd01387 612 DRYRCLVALKLPRPAPGDMCVSLLSRLCTV-TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-770 |
3.32e-156 |
|
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: 494.87 E-value: 3.32e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKkkeqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIM----SNKKpeLIDLLLISTNPFDFPFVSQGEVTVASIDDS--EELLA 333
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 334 TDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG 409
Cdd:cd01379 228 IEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 410 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQP---RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 486
Cdd:cd01379 308 GETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSasdEPLSIGILDIFGFENFQKNSFEQLCINIANEQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 487 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgK 561
Cdd:cd01379 388 IQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--K 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 562 SNNFQKPKptkgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSflfsnyagaeagdsaggkkgg 641
Cdd:cd01379 461 SKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR--------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 642 kkkgssfQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd01379 516 -------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFAD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 124486959 722 FKQRYRIL--NASAIPEGqfidSKNASEKLLNSIDVDreQFRFGHTKVFFK 770
Cdd:cd01379 589 FLKRYYFLafKWNEEVVA----NRENCRLILERLKLD--NWALGKTKVFLK 633
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-770 |
1.34e-154 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 491.58 E-value: 1.34e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVAAYRGKKRQEA-----PPHIFSISDNAYQFMLTDR----DNQSI 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 176 LITGESGAGKTVNTKRVIQYFATIAVTG-DKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 254
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAkGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 255 GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpELIDLLLISTNPFDFPFVSQGE-VTVASIDDSEELLA 333
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 334 TDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KAGYLMGLNSAEMLKGLCCpRVKVGne 411
Cdd:cd14892 243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 412 yvTKGQNVQ------QVTNSVGALAKAVYEKMFLWMVTRIN----QQL------DTKQPRQYFIGVLDIAGFEIFDFNSL 475
Cdd:cd14892 320 --ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 476 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNK 553
Cdd:cd14892 398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 554 LYDQHLGKSNNFQKPKptkgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSlkllsflfsnyagaeagd 633
Cdd:cd14892 477 YHQTHLDKHPHYAKPR----FECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 634 saggkkggkkkgssfqtvsaVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGF 713
Cdd:cd14892 535 --------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGF 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 714 PSRILYADFKQRYRILNASAIPEGQFIDSKNASE--KLLNSI---DVDREQFRFGHTKVFFK 770
Cdd:cd14892 595 PIRRQFEEFYEKFWPLARNKAGVAASPDACDATTarKKCEEIvarALERENFQLGRTKVFLR 656
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1927 |
1.71e-154 |
|
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: 505.48 E-value: 1.71e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 850 EKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNER 929
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 930 LEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQ 1009
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1010 TLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEF 1089
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1090 EMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNK 1169
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1170 KRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNM 1249
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKA 1329
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1330 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEENTE 1409
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1410 ASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMR 1489
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1490 NAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLEL 1569
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1570 SQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRT 1649
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1650 VQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLIN 1729
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1730 TKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLAL 1809
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1810 KGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 124486959 1890 EEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAK 1927
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-770 |
1.88e-154 |
|
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: 490.85 E-value: 1.88e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSL---KEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTnPFDFPFVSQ-GEVTVASIDDSEELLATDNAI 338
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADK-----AGYLMGLNSAEMLKGLCCPRVKVGNEYV 413
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 414 TKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 493
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 494 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgkSNN--FQKPKpt 571
Cdd:cd14873 389 HIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPR-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 572 kgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGGKKkgssfQTV 651
Cdd:cd14873 463 --VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR-----PTV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 652 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL-N 730
Cdd:cd14873 536 SSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 124486959 731 ASAIPEgqfiDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14873 616 NLALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-770 |
4.24e-149 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 475.72 E-value: 4.24e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKK-RQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLS-----------PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 261 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVASIDDSEEL----LATDN 336
Cdd:cd14897 152 LGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSEELeyyrQMFHD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDIL---GFSPEEKVGIYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADK-----AGYLMGLNSAEMLKGLCCPRVKV 408
Cdd:cd14897 231 LTNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 409 GNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCINFT 483
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 484 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDqHLGKS 562
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGES 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 563 NNFQKPKptKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYagaeagdsaggkkggk 642
Cdd:cd14897 464 PRYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY---------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 643 kkgssfqtvsavFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14897 524 ------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDF 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 124486959 723 KQRYRILNASAipegqfidSKNASEKLLNSIDV----DREQFRFGHTKVFFK 770
Cdd:cd14897 592 VKRYKEICDFS--------NKVRSDDLGKCQKIlktaGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-729 |
6.97e-143 |
|
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: 458.23 E-value: 6.97e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 167 -LTDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPgKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSR 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMG-KSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 246 FGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMsnkkpelidlllistnpfdfpfvsqgevtvasI 325
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA--------------------------------I 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 326 DDSEELLATDN------AIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKAGYLMGL 392
Cdd:cd14900 210 GASEAARKRDMyrrvmdAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 393 NSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL-----DTKQPRQYFIGVLDIAGF 467
Cdd:cd14900 290 DATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 468 EIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKAT 546
Cdd:cd14900 370 EVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 547 DTSFKNKLYdQHLGKSNNFQKPKPTKGKaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQksslkllsflfsnY 626
Cdd:cd14900 449 DTTLASKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV-------------Y 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 627 AGAeagdsaggkkggkkkgssfqtvsavFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGI 706
Cdd:cd14900 513 GLQ-------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|...
gi 124486959 707 RICRKGFPSRILYADFKQRYRIL 729
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-770 |
1.25e-140 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 453.33 E-value: 1.25e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRG--KKRQEA------PPHIFSISDNAYQFMLTDRDN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 173 QSILITGESGAGKTVNTKRVIQYFATIA--------VTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSS 244
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSqqeqnseeVLTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 245 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELI-DLLLISTNPFDFP-FVSQGE-V 320
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLqQLGLKNQLSGDRYdYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 321 TVASIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAGYLMGLNSAEML 398
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 399 KGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL--------DTKQPRQYFIGVLDIAGFEIF 470
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 471 DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 547
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 548 TSFKNKLYDQHlgksNNFQKPKPTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnya 627
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS--- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 628 gAEAGDSAGGKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIR 707
Cdd:cd14907 555 -GEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486959 708 ICRKGFPSRILYADFKQRYRILNasaipegqfidsknasekllnsidvdrEQFRFGHTKVFFK 770
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-770 |
1.92e-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: 452.44 E-value: 1.92e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFML----TDRDNQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 178 TGESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpgKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgAT 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 258 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQI---MSNKKPELIDLLlistNPFDFPFVSQG---EVTVASIDDSEEL 331
Cdd:cd14889 150 GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGagcKREVQYWKKKYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 332 LAtdNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFkqkqreeqaEPDGTEVA----DKAGYL------MGLNSAEMLKGL 401
Cdd:cd14889 226 VC--NAMDMVGFTEQEEVDMFTILAGILSLGNITF---------EMDDDEALkvenDSNGWLkaaagqFGVSEEDLLKTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 402 CCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLdtkQPRQYF------IGVLDIAGFEIFDFNSL 475
Cdd:cd14889 295 TCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 476 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIEL-IEKPMGIFSILEEECMFPKATDTSFKNKL 554
Cdd:cd14889 372 EQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 555 yDQHLGKSNNFQKPKPTKGKaeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAgAEAGDS 634
Cdd:cd14889 451 -NIHFKGNSYYGKSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATR-SRTGTL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 635 AGGKKGGKKKGSSF-----QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRIC 709
Cdd:cd14889 525 MPRAKLPQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIR 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 710 RKGFPSRILYADFKQRYRILnasaIPEGQFIDSKNASEKLLNSIDVdrEQFRFGHTKVFFK 770
Cdd:cd14889 605 REGFSWRPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-770 |
2.34e-138 |
|
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: 446.70 E-value: 2.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA-----------GGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 337
Cdd:cd14904 150 KLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 338 IDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGyLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 417
Cdd:cd14904 230 LSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQVAK-MLGLPTTRIEEALCNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 418 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 496
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 497 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSNNFQKPKPTKgk 574
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 575 aeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNyagAEAgDSAGGKKGGKKKGSSFQTVSAV 654
Cdd:cd14904 466 --TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---SEA-PSETKEGKSGKGTKAPKSLGSQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 655 FRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAI 734
Cdd:cd14904 540 FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSM 619
|
650 660 670
....*....|....*....|....*....|....*..
gi 124486959 735 PEGqfiDSKNASEKLLNSIDVDRE-QFRFGHTKVFFK 770
Cdd:cd14904 620 HSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-770 |
2.46e-134 |
|
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: 434.86 E-value: 2.46e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNPEVvAAYRGKKRQEAPPHIFSISDNAYQFMLTDRD---NQS 174
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 175 ILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQG-------TLEDQIIQANPLLEAFGNAKTVRNDNSSRFG 247
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 248 KFIRIHFGATG-KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIsTNPFDFPFVSQ-GEVTVASI 325
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 326 DDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKAGYLMGLNSAEMLKGL 401
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 402 CCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFD-FNSLEQLCI 480
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 481 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 559
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 560 GKSNNFQKPKPtKGKAEAhFSLVHYAGTVDYNIAGWLDKNKDPLNEtvvglyqksslkllSFlfsnyagaeagdsaggkk 639
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPE--------------DF------------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 640 ggkkkgSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILY 719
Cdd:cd14891 521 ------EDLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 720 ADFKQRYRILNASAI------PEGQFIdsknasEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14891 595 AELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-726 |
1.44e-133 |
|
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: 435.48 E-value: 1.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYR--------GKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 170 RDNQSILITGESGAGKTVNTKRVIQYFATiaVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKF 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTS--VGRDQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 250 IRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVA-----S 324
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQ-KGGKYELLNSYGPSFArkravA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 325 IDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKAGYLMGLNSAEM 397
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 398 LKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-------TKQPRQYF--IGVLDIAGFE 468
Cdd:cd14902 314 ETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsISDEDEELatIGILDIFGFE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 469 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATD 547
Cdd:cd14902 394 SLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 548 TSFKNKLYDQHLGksnnfqkpkptkgkaEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFS--- 624
Cdd:cd14902 473 QALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAden 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 625 -NYAGAEAGDSAGGKKGGKKKGSsfqtVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVL 703
Cdd:cd14902 538 rDSPGADNGAAGRRRYSMLRAPS----VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660
....*....|....*....|...
gi 124486959 704 EGIRICRKGFPSRILYADFKQRY 726
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELF 636
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
42-829 |
1.78e-130 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 430.22 E-value: 1.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 42 DDKEMYVKGMIQ-SRENDKVIVKTLD---DRELTLNSDQVFPMNPP-KFDKIEDMAMMTHLHEPAVLYNLKERYAAWMIY 116
Cdd:PTZ00014 47 DPDLMFAKCLVLpGSTGEKLTLKQIDpptNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 117 TYSGLFCVTVNPYKWLPVYNPEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAGKTVNTKRVIQY 195
Cdd:PTZ00014 127 TTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 196 FATiAVTGDkkkeqqpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRV 275
Cdd:PTZ00014 207 FAS-SKSGN---------MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 276 TFQLSSERSYHIFYQIMSNKKPELID-LLLISTNpfDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSPEEKVGIYKL 354
Cdd:PTZ00014 277 VTQEDDERSYHIFYQLLKGANDEMKEkYKLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSI 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 355 TGAVMHYGNMKFKQKQREEQAE-----PDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGAL 429
Cdd:PTZ00014 355 LSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 430 AKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIE 509
Cdd:PTZ00014 435 SKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIS 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 510 WEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFqkpKPTKGKAEAHFSLVHYAGTVD 589
Cdd:PTZ00014 515 TEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKY---KPAKVDSNKNFVIKHTIGDIQ 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 590 YNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNyAGAEAGDSAGGkkggkkkgssfQTVSAVFRENLNKLMTNLRST 669
Cdd:PTZ00014 591 YCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG-VEVEKGKLAKG-----------QLIGSQFLNQLDSLMSLINST 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 670 HPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAsAIPEGQFIDSKNASEKL 749
Cdd:PTZ00014 659 EPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKL 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 750 LNSIDVDREQFRFGHTKVFFKAGLLGLLEEMRDEKLVT---LMTRTQAVCRGYLMRvefKKMMERRESIFCIQYNVRSFM 826
Cdd:PTZ00014 738 LERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLRRHL 814
|
...
gi 124486959 827 NVK 829
Cdd:PTZ00014 815 VIA 817
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-736 |
1.23e-129 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 423.17 E-value: 1.23e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 170 RDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKF 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 250 IRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIM------SNKKPELIDLLLISTN-PFDFPFVSQGEV-T 321
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 322 VASIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKAGYLMGLNSAEML 398
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 399 KGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL--DTKQPRQYFIGVLDIAGFEIFDFNSLE 476
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 477 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKL 554
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 555 YDQHLGKSN-----NFQKPKPTKGKAEAHFSLVHYAGTVDYNI-AGWLDKNKDPLNETVVGLYQKSSLkllsflfsnyag 628
Cdd:cd14908 480 YETYLPEKNqthseNTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 629 aeagdsaggkkggkkkgssfqtvsavFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRI 708
Cdd:cd14908 548 --------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660
....*....|....*....|....*...
gi 124486959 709 CRKGFPSRILYADFKQRYRILnASAIPE 736
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-770 |
2.18e-122 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 401.67 E-value: 2.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRG-KKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFATiavtgdkkkeQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS----------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 259 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELID---LLLIStnpfDFPFVSQGEVTVASIDDSEELLATD 335
Cdd:cd14876 151 GIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyhLLGLK----EYKFLNPKCLDVPGIDDVADFEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 336 NAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGN 410
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 411 EYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 490
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 491 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNnfqKPK 569
Cdd:cd14876 387 FIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG---KFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 570 PTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAgAEAGDSAGGkkggkkkgssfQ 649
Cdd:cd14876 462 PAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV-VEKGKIAKG-----------S 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 650 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 729
Cdd:cd14876 530 LIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 124486959 730 NAsAIPEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14876 610 DL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-770 |
2.56e-122 |
|
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: 401.08 E-value: 2.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPgkmqgtlEDQIiqanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgATGK 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQP-------EDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEV-TVASIDDSEELLATDNAI 338
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ-GPETYYYLNQGGAcRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 339 DILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVADKAGYLmgLNSAEMLKGLCCPRVKVGN-EYVT 414
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEIHTAARLL--QVPPERLEGAVTHRVTETPyGRVS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 415 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 492
Cdd:cd14896 306 RPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 493 HHMFVLEQEEYKKEGIEWEFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPK-- 569
Cdd:cd14896 386 QTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQlp 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 570 -PTkgkaeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagaEAGDSAGGKKGGKKKGSSF 648
Cdd:cd14896 464 lPV-------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ-----EAEPQYGLGQGKPTLASRF 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 649 QtvsavfrENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 728
Cdd:cd14896 532 Q-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGA 604
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486959 729 LNASAIPEgqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14896 605 LGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-770 |
3.49e-122 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 402.79 E-value: 3.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNpevVAAYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 170 RDNQSILITGESGAGKTVNTKRVIQYFA-----TIAVTGDKKKEQQPGkmqgtleDQIIQANPLLEAFGNAKTVRNDNSS 244
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISG-------SELLSANPILESFGNARTLRNDNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 245 RFGKFIRIHFG-----ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPE-LIDLLLISTNPFDFPFVSQG 318
Cdd:cd14895 151 RFGKFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 319 EVTVAS--IDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------- 383
Cdd:cd14895 231 QCYQRNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspsslt 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 384 -----DKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQY- 457
Cdd:cd14895 311 vqqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNp 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 458 ----------FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE 527
Cdd:cd14895 391 nkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 528 -KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKptKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNET 606
Cdd:cd14895 470 qRPSGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 607 VVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGGKKKGSSFQTV--SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKT 684
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESA 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 685 PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASaipegQFIDSKNASEkLLNSIDVDreQFRFGH 764
Cdd:cd14895 627 SDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVD--HAELGK 698
|
....*.
gi 124486959 765 TKVFFK 770
Cdd:cd14895 699 TRVFLR 704
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-729 |
1.77e-111 |
|
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: 370.72 E-value: 1.77e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRD--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 178 TGESGAGKTVNTKRVIQYFATIAVTGDKKKEQqpgKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAASPTSWESH---KIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 258 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLisTNPFDFPFVSQGEVTVASiDDSEellATDN 336
Cdd:cd14880 160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHL--PEGAAFSWLPNPERNLEE-DCFE---VTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGneyv 413
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAG---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 414 tKGQNVQQVTNSVG-------ALAKAVYEKMFLWMVTRINQQLDTKQPR-QYFIGVLDIAGFEIFDFNSLEQLCINFTNE 485
Cdd:cd14880 310 -KQQQVFKKPCSRAecdtrrdCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 486 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNN 564
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 565 FQKPKPTKgkaEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagAEAGDSAGGKKGGKKK 644
Cdd:cd14880 468 LGHNKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP----ANPEEKTQEEPSGQSR 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 645 GSSFQTVSAvFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 724
Cdd:cd14880 541 APVLTVVSK-FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
....*
gi 124486959 725 RYRIL 729
Cdd:cd14880 620 RYKLL 624
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-727 |
2.56e-110 |
|
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: 369.42 E-value: 2.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 170 RDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQ------PGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNS 243
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSesisppASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 244 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNK----KPELIDLLLISTNPFDFPFVSQG 318
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 319 EVTVA--SIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 384
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 385 KAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL--------------- 449
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 450 DTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlAACIELIE-K 528
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 529 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVV 608
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 609 GLYQKSSLKLLSFLFSNYAGAEA-GDSAGGKKGGKKKGSSFQTVSAV-----FRENLNKLMTNLRSTHPHFVRCLIPNET 682
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDAnGDSELDGFGGRTRRRAKSAIAAVsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124486959 683 KTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYR 727
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-768 |
3.84e-107 |
|
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: 360.06 E-value: 3.84e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKR-QEAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFatIAVTGDKKKEQQP-GKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT- 257
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNnNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 258 GKLASADIETYLLEKSRVTFQLS-SERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASI----------- 325
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRPDnINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 326 ----DDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKAGYLMGLNSAEML 398
Cdd:cd14906 241 nnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 399 KGLCCPRVKVGNE--YVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQ-----------QLDTKQPRQYFIGVLDIA 465
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 466 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 544
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 545 ATDTSFKNKLYDQHLGKSNNFQKpkpTKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFS 624
Cdd:cd14906 480 GSEQSLLEKYNKQYHNTNQYYQR---TLAKGT--LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 625 NYAGAEAGDSaggkkggkKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLE 704
Cdd:cd14906 555 QQITSTTNTT--------KKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLN 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 705 GIRICRKGFPSRILYADFKQRYRILNAS------------AIPEGQFIDSKNASEKLLNSIDVDREQ-----------FR 761
Cdd:cd14906 627 TIKVRKMGYSYRRDFNQFFSRYKCIVDMynrknnnnpklaSQLILQNIQSKLKTMGISNNKKKNNSNsnsnttndkplFQ 706
|
....*..
gi 124486959 762 FGHTKVF 768
Cdd:cd14906 707 IGKTKIF 713
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-770 |
8.90e-107 |
|
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: 357.20 E-value: 8.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEA-PPHIFSISDNAY-QFMLTDRDNQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFatiavtGDKKKEQQPGKMQGTLEDQIIQ----ANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 254
Cdd:cd14875 83 GESGSGKTENAKMLIAYL------GQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 255 -GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDF-------PFVSQGeVTVASID 326
Cdd:cd14875 157 dPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYkclnggnTFVRRG-VDGKTLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 327 DSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGyLMGLNSAEMLKglcCPRV 406
Cdd:cd14875 236 DAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACR-LLQLDPAKLRE---CFLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 407 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQ----QLDTKQPRqyFIGVLDIAGFEIFDFNSLEQLCINF 482
Cdd:cd14875 312 KSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNAsitpQGDCSGCK--YIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 483 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGK 561
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 562 SNNFQKPKPTkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagAEAGDSAGGkkgg 641
Cdd:cd14875 469 SPYFVLPKST---IPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS----TEKGLARRK---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 642 kkkgssfQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 721
Cdd:cd14875 538 -------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQ 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 124486959 722 F-KQRYRILNASAIPEGQFIDSKNASEKLLNS----IDVDREQFRFGHTKVFFK 770
Cdd:cd14875 611 FcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-770 |
7.09e-105 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 351.50 E-value: 7.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRDNQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATIAVTGDKKkeqqpgkmqgtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD-----------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQI---MSNKKPELIDLLLISTnpfdFPFVSQGEV-TVASIDDSEELLATD 335
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCikgLSPEEKKSLGFKSLES----YNFLNASKCyDAPGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 336 NAIDILgFSPEEKVGIYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 412
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 413 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 492
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 493 HHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyDQHLgKSNNFQkpkPT 571
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSFI---PG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 572 KGkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAgAEAGDsaggkkggkkKGSSFqtV 651
Cdd:cd14886 465 KG-SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIP-NEDGN----------MKGKF--L 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 652 SAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL-- 729
Cdd:cd14886 531 GSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILis 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 124486959 730 -NASAIPEGQfiDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14886 611 hNSSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-770 |
1.98e-102 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 345.45 E-value: 1.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 182 GAGKTVNTKRVIQYFATIAVTGDKKkeQQPGKMQGtledqiiqANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV--LSVEKLNA--------ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 262 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-----IDLLLISTNPFDFPFVSQGEVTvasiDDSEELLATDN 336
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALrtelhLNQLAESNSFGIVPLQKPEDKQ----KAAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDILGFSPEEKVGIYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYV 413
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 414 TKGQNVQQVTNS------------VGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 475
Cdd:cd01386 306 TTSSGQESPARSssggpkltgveaLEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 476 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 540
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 541 MFPKATDTSFKNKLYdQHLGKSNNFQKPKPTKgKAEA--HFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSS 615
Cdd:cd01386 466 LYPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 616 LKLlsflfsnyAGAEAgdsaggkkggkkkgssfQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPN------ETKTPGV-- 687
Cdd:cd01386 544 KET--------AAVKR-----------------KSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPaa 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 688 ----MDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL----NASAIPEGQFIDSKNASEKLLNSIDVDREQ 759
Cdd:cd01386 599 gdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKSS 678
|
730
....*....|.
gi 124486959 760 FRFGHTKVFFK 770
Cdd:cd01386 679 YRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-770 |
7.73e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 313.68 E-value: 7.73e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR---GKKRQEAPPHIFSISDNAYQFMLTDRDNQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 178 TGESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTCRA-----------SSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 258 GK-LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGE----VTVASIDDSEELL 332
Cdd:cd14878 151 KKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 333 ATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 412
Cdd:cd14878 230 VLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 413 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRIN----QQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 488
Cdd:cd14878 310 IIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 489 QFFNHHMFVLEQEEYKKEGIEWEFI-DFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQK 567
Cdd:cd14878 390 HYINEVLFLQEQTECVQEGVTMETAySPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSL-LESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 568 PKPTK-GKAE-------AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFsnyagaeagdsaggkk 639
Cdd:cd14878 469 YSPMKdGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 640 ggkkkGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILY 719
Cdd:cd14878 533 -----QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSF 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 124486959 720 ADFKQRYRILNASAIPEGQfidSKNASEKLLNSIDVDREQ-FRFGHTKVFFK 770
Cdd:cd14878 608 SDFLSRYKPLADTLLGEKK---KQSAEERCRLVLQQCKLQgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-733 |
1.47e-87 |
|
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: 298.73 E-value: 1.47e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvynpEVVAAYRGKKRQE-----APPHIFSISDNAYQFMLTdRDNQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 176 LITGESGAGKTVNTKRVIQYFatiaVTGDKKKEqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFg 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYL----VERTASTT--------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 256 aTGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpelidlLLISTNPFDFPFVSQGEVTVasIDDSEELLATD 335
Cdd:cd14898 140 -DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTC 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 336 NAIDILGFSPEEKvgIYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTK 415
Cdd:cd14898 211 SAMKSLGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 416 GQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 495
Cdd:cd14898 286 FNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 496 FVLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNfqkpkptkgKA 575
Cdd:cd14898 364 FRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGFINT---------KA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 576 EAHFSLVHYAGTVDYNIAGWLDKNKdplnetvvglyQKSSLKLLSFLFSNYAGAEagdsaggkkggkkkgssfQTVSAVF 655
Cdd:cd14898 434 RDKIKVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEGSK------------------EDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 656 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 733
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-770 |
1.54e-87 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 303.11 E-value: 1.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRD 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 172 NQSILITGESGAGKTVNTKRVIQYFATIAvtgdkkkEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIR 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS-------DRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 252 IHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpelidllliSTNPFDfpfVSQGEvtvaSIDDSEEL 331
Cdd:cd14887 154 LHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAV---------AAATQK---SSAGE----GDPESTDL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 332 LATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDG-------------------------------- 379
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKltsvsvgceetaadrshssevkclssglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 380 ------TEVADKAGYLMGLNSAEMLK-GLCCPRVKVGNEYVTkgqnVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTK 452
Cdd:cd14887 298 asrkhlKTVARLLGLPPGVEGEEMLRlALVSRSVRETRSFFD----LDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 453 QPRQY--------------FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI-- 513
Cdd:cd14887 374 AKPSEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcs 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 514 --DFGMDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SNN 564
Cdd:cd14887 454 afPFSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 565 FQKPKPTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLyqksslkllsFLFSNYAGAEAGdsAGGKKGGKKK 644
Cdd:cd14887 534 YKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERL----------FLACSTYTRLVG--SKKNSGVRAI 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 645 GSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 724
Cdd:cd14887 602 SSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWR 681
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 124486959 725 RYRILNASAIPEgqFIDSKNASEKLLNSIDVDREQFRFGHTKVFFK 770
Cdd:cd14887 682 RYETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-770 |
9.37e-87 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 298.08 E-value: 9.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEvvaaYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 182 GAGKTVNTKRVIQYFatiaVTGDKKKEQqpgkMQGTLEDqiiqANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 261
Cdd:cd14937 79 GSGKTEASKLVIKYY----LSGVKEDNE----ISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 262 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPfDFPFVSQGEVTVASIDDSEELLATDNAIDIL 341
Cdd:cd14937 147 SSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 342 GFSPEEKVGIYKLTGAVMhYGNMKFKQ-----KQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 416
Cdd:cd14937 226 NMHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 417 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 496
Cdd:cd14937 305 LSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 497 VLEQEEYKKEGIEWEFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYDQHLGKSNNFQKPKPTKGKAE 576
Cdd:cd14937 385 EKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDIN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 577 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLfsnYAGAEAGDSAGGKkggkkkgssfQTVSAVFR 656
Cdd:cd14937 460 KNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL---YEDVEVSESLGRK----------NLITFKYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 657 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRIcRKGFPSRILYADFKQRYRILNASAIPE 736
Cdd:cd14937 527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKD 605
|
650 660 670
....*....|....*....|....*....|....
gi 124486959 737 GQFIDSKNASEKLLNSIDVDreQFRFGHTKVFFK 770
Cdd:cd14937 606 SSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-769 |
7.79e-81 |
|
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: 280.98 E-value: 7.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 106 LKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNPEVVAAYR-------GKKRQEAPPHIFSISDNAYQFMLTDRDNQSI 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 176 LITGESGAGKTVNTKRVIQYFATIAVTGdkKKEQQpgkmqgtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 255
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHS--KKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 256 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFV--SQGEVTVAS--IDDSE-- 329
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD-DPSDYALLasYGCHPLPLGpgSDDAEgf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 330 ELLATdnAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVK 407
Cdd:cd14879 238 QELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 408 VGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL-DTKQPRQYFIGVLDIAGFEIFD---FNSLEQLCINFT 483
Cdd:cd14879 316 VRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstgGNSLDQFCVNFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 484 NEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFKNKLyDQHLGK 561
Cdd:cd14879 396 NERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLEAL-RKRFGN 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 562 SNNF-QKPKPTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLyqksslkLLSFLFsnyagaeagdsaggkkg 640
Cdd:cd14879 474 HSSFiAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNL-------LRGATQ----------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 641 gkkkgssfqtvsavFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYA 720
Cdd:cd14879 530 --------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHA 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 124486959 721 DFKQRYrilnasaIPEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFF 769
Cdd:cd14879 596 EFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-752 |
8.46e-73 |
|
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: 256.96 E-value: 8.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNPEVVAAYRGKKRQEAPPHIfsISDNAYQFMLTDRDnQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLAPQLLKV--VQEAVRQQSETGYP-QAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 181 SGAGKTVNTKRVIQYFATIAVTG---DKKKeqqpgkmqgtledQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgAT 257
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGGpetDAFK-------------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 258 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKP-ELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDN 336
Cdd:cd14881 143 GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 337 AIDILGFSPEEKVGIYkltGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGyLMGLNSAEMLKGLCCpRVKVgneyvTKG 416
Cdd:cd14881 223 CLGILGIPFLDVVRVL---AAVLLLGNVQFIDGGGLEVDVKGETELKSVAA-LLGVSGAALFRGLTT-RTHN-----ARG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 417 QNVQQVTN------SVGALAKAVYEKMFLWMVTRINQQLD-----TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 485
Cdd:cd14881 293 QLVKSVCDanmsnmTRDALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 486 KLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYDQHlgKSN 563
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--RQN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 564 N-FQKPKPTKGKAeahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSlklLSFLFSNYagaeagdsaggkkggk 642
Cdd:cd14881 449 PrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---CNFGFATH---------------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 643 kkGSSFQTvsavfreNLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 722
Cdd:cd14881 507 --TQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAF 577
|
650 660 670
....*....|....*....|....*....|
gi 124486959 723 KQRYRILnASAIPEGQFIDSKNASEKLLNS 752
Cdd:cd14881 578 NARYRLL-APFRLLRRVEEKALEDCALILQ 606
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-718 |
1.88e-69 |
|
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: 248.67 E-value: 1.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEA-------PPHIFSISDNAYQFMLTDRD 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 172 NQSILITGESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGT-LEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFI 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ-----------TDSQMTeRIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 251 RIHF---------GATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGE-- 319
Cdd:cd14884 150 LLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEsh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 320 ----------VTVASIDDSEELLATD--------NAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQkqreeqaepdgte 381
Cdd:cd14884 230 qkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 382 vadkAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRIN---------QQLDTK 452
Cdd:cd14884 297 ----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDNE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 453 QPRQY---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDfgmdLAACIELIEKP 529
Cdd:cd14884 373 DIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 530 MGIFSILEEECMFP----KATDTSFKNKLYD----QHLGKSNNFQK--PKPTKGKAEAH------FSLVHYAGTVDYNIA 593
Cdd:cd14884 449 AKIFRRLDDITKLKnqgqKKTDDHFFRYLLNnerqQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 594 GWLDKNKDPLNETVVGLYQKSSLKllsFLFSNYAGAEAGDsaggkkggkkkgssFQTVSAVFRENLNKLMTNLRSTHPHF 673
Cdd:cd14884 529 NWIDKNSDKIETSIETLISCSSNR---FLREANNGGNKGN--------------FLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 124486959 674 VRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-770 |
4.55e-65 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 234.38 E-value: 4.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 101 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYrgkkrqeappHIFSISDNAYQFMLTDRDN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 180 ESGAGKTVNTKRVIQYFATiavtgdkkkeqQPGKMQGTLEDQIIQAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS-----------QPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 260 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVASIDDSEELLATDNAID 339
Cdd:cd14874 139 TGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 340 ILGFSPEEKVGIYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKA-----GYLMGLNSAEMLKGLCcPRVKVGNEYvt 414
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFLL-PKSEDGTTI-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 415 kgqNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLdtKQPRQY-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 493
Cdd:cd14874 294 ---DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 494 HMFVLEQEEYKKEGIEwefIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNnFQKp 568
Cdd:cd14874 369 HSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 569 kpTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYaGAEAGDsaggkkggkKKGSSF 648
Cdd:cd14874 444 --ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-SSNTSD---------MIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 649 QTVSAVFRENLNKLmtnlRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 728
Cdd:cd14874 512 QFILRGAQEIADKI----NGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486959 729 LNASAIPEGQfiDSKNASEKLLNSIDVDREQ-FRFGHTKVFFK 770
Cdd:cd14874 588 LLPGDIAMCQ--NEKEIIQDILQGQGVKYENdFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-770 |
3.50e-64 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 232.68 E-value: 3.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 106 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYrgKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 185 KTVNTKRVIQYFATIAVTGDKkkeqqpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASAD 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK-----------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 265 IETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLISTNPFDFpFVSQGEVTVASIDDSEELLATDNAIDILGF 343
Cdd:cd14905 154 LYSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 344 sPEEKVG-IYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKAGYlmglnsAEMLKGLCCPRVKVGNEYVT-KGQNVQQ 421
Cdd:cd14905 233 -PSEKIDlIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISdRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 422 VTNSVGALAKAVYEKMFLWMVTRINQQLdtkQPRQY--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 499
Cdd:cd14905 299 AVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 500 QEEYKKEGIEWEFIDFGMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLydqhlgksNNFQKPKPTKGKAEAHF 579
Cdd:cd14905 376 QREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKPNKF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 580 SLVHYAGTVDYNIAGWLDKNKDP-------------------------LNETVVGLYQ---------KSSLKLLSFLFS- 624
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakntakKSPLSIVKVLLSc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 625 -----------NYAGAEAGDSAGGKKGGKKKGSSFQTVSAVfrenlNKLMTNlRSTHPHFVRCLIPNETKTPGVMDHYLV 693
Cdd:cd14905 525 gsnnpnnvnnpNNNSGGGGGGGNSGGGSGSGGSTYTTYSST-----NKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKSV 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 694 MHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASaipEGQFidsKNASEKLL-NSIDVDR---EQFRFGHTKVFF 769
Cdd:cd14905 599 NEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQN---QRNF---QNLFEKLKeNDINIDSilpPPIQVGNTKIFL 672
|
.
gi 124486959 770 K 770
Cdd:cd14905 673 R 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-769 |
1.10e-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: 232.94 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 103 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQ----------EAPPHIFSISDNAYQFMLTDRDN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 173 QSILITGESGAGKTVNTKRVIQYFATIA--VTGDKKKEQQPGKMQgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFI 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGdeTEPRPDSEGASGVLH-PIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 251 RIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK--PELIDLLLISTNPFDFPFVSQG--EVTVASID 326
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 327 --DSEELLATDNAIDIlgfSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKAGYLMGlNSAEML---K 399
Cdd:cd14893 243 arDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALK-DPAQILlaaK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 400 GLCCPRVKVGNEYVT---------------KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYFIG 460
Cdd:cd14893 319 LLEVEPVVLDNYFRTrqffskdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVIN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 461 -----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLAACIELI 526
Cdd:cd14893 399 sqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 527 E-KPMGIFSILEEECMFPKATDTSFKNKLYDqhlGKSNNFQKPKPTKGKAEAH------------FSLVHYAGTVDYNIA 593
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFS---GNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 594 GWLDKNKDPLNETVVGLYQKSSLKLLSFL-FSNYAGAEAGDSAGGKKGGKKKGSSFQTVSAVFRENLN------------ 660
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVgAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 661 --KLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRilnasaipegQ 738
Cdd:cd14893 636 adALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------N 705
|
730 740 750
....*....|....*....|....*....|....*
gi 124486959 739 FIDSKNASEKLLNSID----VDREQFRFGHTKVFF 769
Cdd:cd14893 706 VCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-770 |
2.48e-62 |
|
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: 226.55 E-value: 2.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 102 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 182 GAGKTVNTKRVIQYFATIavtgdkkkeqqpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYL------------GDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 262 SADIETYLLEKSRVTFQLSSERSYHIFYQIMS--NKKPELIDLLLISTNPFDFPFVSQG-------------EVTVASID 326
Cdd:cd14882 151 GAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 327 DSEELLAtdnaidILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRV 406
Cdd:cd14882 231 EFEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 407 KVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTkqPR-----QYFIGVLDIAGFEIFDFNSLEQLCIN 481
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 482 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYDQHLGK 561
Cdd:cd14882 381 TLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 562 SNNFQKPkptkgkAEAH-FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNyagaeagdsaggkkg 640
Cdd:cd14882 456 HSQFVKK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 641 gkKKGSSFQTVSAVFR----ENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSR 716
Cdd:cd14882 515 --SQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYR 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 124486959 717 ILYADFKQRYRILnasAIPEGQFIDSKNASEKLLnSIDVDREQFRFGHTKVFFK 770
Cdd:cd14882 593 IPFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-252 |
1.26e-61 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 208.35 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 122 FCVTVNPYKWLPVYNPEVV-AAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 201 VTGDKKKEQQ----PGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRI 252
Cdd:cd01363 81 FNGINKGETEgwvyLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-768 |
6.49e-44 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 172.33 E-value: 6.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 100 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYR-GKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 179 GESGAGKTVNTKRVIQYFA------------TIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRF 246
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptnLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 247 GKFIRIHFgATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMsNKKPELIDLLLISTNPFDFPFVSQGEVTVASID 326
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYII-NGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 327 DSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 383
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 384 DKAGYL----MGLNSAEMLKGLCCPRVkVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF- 458
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININt 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 459 --IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM--GIFS 534
Cdd:cd14938 398 nyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 535 ILEEECMfPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAhFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKS 614
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 615 SLKLLSFLFSNYAGAEAGDSAGGKKG----------GKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKT 684
Cdd:cd14938 556 ENEYMRQFCMFYNYDNSGNIVEEKRRysiqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 685 P-GVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAsaipegqfiDSKNASEKLLNSIDVDREQFRFG 763
Cdd:cd14938 636 ElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 124486959 764 HTKVF 768
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1148-1934 |
7.48e-33 |
|
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: 139.81 E-value: 7.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1148 EEISERLEEASGATsaqiemnkkresefqKLRRDLEEATLQHEATAATLrKKHADTVAELGEQIDNLQRVKQKLEK---- 1223
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykel 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1224 -------EKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVE 1296
Cdd:TIGR02168 219 kaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1297 EKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWR 1376
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE-------LEEKLEELKEELESLEAELEELEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1377 TKYETdaiqRTEELEEAKKKLAQRLQEAEENteasNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQrnFDKV 1456
Cdd:TIGR02168 372 SRLEE----LEEQLETLRSKVAQLELQIASL----NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1457 LAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRREN---KNLQEEISDLTEQIAETGKN------- 1526
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKALLKNqsglsgi 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1527 ---LQEVEKTKKQVEQEKS-------------DLQAALEEVEGSLEHEESKilRVQLELSQVKselDRKVTEKDEEIEQI 1590
Cdd:TIGR02168 522 lgvLSELISVDEGYEAAIEaalggrlqavvveNLNAAKKAIAFLKQNELGR--VTFLPLDSIK---GTEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1591 KRNSQ-----------RAVEAMQSVLD--AEIRSRNDALRLKKKM----------------------------------- 1622
Cdd:TIGR02168 597 IEGFLgvakdlvkfdpKLRKALSYLLGgvLVVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggsaktnssilerr 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1623 ------EGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVAL 1696
Cdd:TIGR02168 677 reieelEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1697 EQTERTRRLSEQELLDSSDRVQLLHSQntslintKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKE 1776
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1777 QDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTY 1856
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLA--------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1857 QAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCR-RVQHELEEAEERADIAESQVNKLRAKSRDVGGQ 1934
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
966-1798 |
5.59e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 133.64 E-value: 5.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 966 TKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLD--DLQVEEDKVNGLIKINVKleqqtDDLEGSLE 1043
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELELALLVLRL-----EELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1044 QEKKLRADLERVKRKLEGDLKMSQESIMDLEndtqqleeklkkkeFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELE 1123
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1124 EEIEAEHTVRAKIEKQRSDLAR---ELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKh 1200
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1201 adtVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSnmermcrsvEDQFNEIKAKDDQQTQLIHDLNMQ 1280
Cdd:TIGR02168 388 ---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1281 KARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETK----AKNALAHALQSSRHDcDLLREQYEEEQE 1356
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLSGIL-GVLSELISVDEG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1357 GKAELQRALSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEENTEASNSKCASLEKTK 1422
Cdd:TIGR02168 535 YEAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1423 QRLQGEVDDL---------------MLDLERANTACATLD----------------------KKQRNFDKV---LAEWKQ 1462
Cdd:TIGR02168 612 PKLRKALSYLlggvlvvddldnaleLAKKLRPGYRIVTLDgdlvrpggvitggsaktnssilERRREIEELeekIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1463 KLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKS 1542
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1543 DLQAALEEVEGSLEHEESKILRVQLELSQVKSELDrkvtEKDEEIEQIKRNSQRAVEAMQSV---LDAEIRSRNDALRLK 1619
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1620 KKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQT 1699
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1700 ERTRRLSEQELLdssdrvqllhsQNTSLINTKKKLEADLA-QCQAEVENSIQESRNAEEKAKKAITD------AAMmaEE 1772
Cdd:TIGR02168 928 ELRLEGLEVRID-----------NLQERLSEEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKElgpvnlAAI--EE 994
|
890 900
....*....|....*....|....*.
gi 124486959 1773 LKKEQDTSAHLERMKKNLEQTVKDLQ 1798
Cdd:TIGR02168 995 YEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1274-1832 |
5.18e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.96 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1274 IHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEE 1353
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1354 EQEGKAELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLM 1433
Cdd:COG1196 314 LEERLEELEEELAELEEELEE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1434 LDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEI 1513
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1514 SDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLE-HEESKILRVQLELSQVKSELDRKVTEKDEEIEQIkr 1592
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1593 nsqRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNemEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLK 1672
Cdd:COG1196 544 ---LAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT--FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1673 EQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQES 1752
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1753 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDA 1832
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1134-1913 |
5.81e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.09 E-value: 5.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1134 AKIEKQRsdlaRELEEISERLEEASGATSAQIEMNKKRESE------FQKLRRDLEEAtlqhEATAATLRKKHADTVAEL 1207
Cdd:TIGR02169 170 RKKEKAL----EELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREY----EGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1208 GE-QIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKsksnmeRMCRSVEDQFNEIKAKddqqtqlIHDLNMQKARLQT 1286
Cdd:TIGR02169 242 IErQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEK-------IGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1287 QNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRals 1366
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD--- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1367 kansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATL 1446
Cdd:TIGR02169 386 ----ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1447 DKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKN 1526
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1527 LQEVEKTKKQVEQEKSDLQAA-----LEEVEGS----LEHEESKILRVQLELSQVKSELDRKV--TEKDEEIEQIKR--- 1592
Cdd:TIGR02169 541 IEVAAGNRLNNVVVEDDAVAKeaielLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVdlVEFDPKYEPAFKyvf 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1593 NSQRAVEAMQS-----------VLDAEI-----------RSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTV 1650
Cdd:TIGR02169 621 GDTLVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1651 QGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINT 1730
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1731 KKKLEADLAqcQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLA 1808
Cdd:TIGR02169 781 LNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1809 LKGGKK----QIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKR 1884
Cdd:TIGR02169 859 LNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
810 820
....*....|....*....|....*....
gi 124486959 1885 QAEEAEEQANTQLSrCRRVQHELEEAEER 1913
Cdd:TIGR02169 939 PKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1735 |
1.29e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.92 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 861 ERAKEDLARSEARRKELEEKMVSllqekndLQLQVqsetenlmdaeERCEGLIKSKIQLEAkvkelnerleeeeemnsel 940
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKS-------LERQA-----------EKAERYKELKAELRE------------------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 941 vAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEmtaLEETISKLTKEKKSLQEAhQQTLDDLQVEEDK 1020
Cdd:TIGR02168 225 -LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK---LEELRLEVSELEEEIEEL-QKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1021 VNGLIKInvkLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDD 1100
Cdd:TIGR02168 300 LEQQKQI---LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1101 EQVLSLQLQKKIKELQARteeleeeieaehtvRAKIEKQRSDLARELEEISERLEEASGATSAQIEmnKKRESEFQKLRR 1180
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQ--------------IASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1181 DLEEatlqHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELkmeiddmasniETVSKSKSNMERMCRSVEDQF 1260
Cdd:TIGR02168 441 ELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-----------AQLQARLDSLERLQENLEGFS 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1261 NEIKAKDDQQTQLIHDLNMQKARLQTQNG-ELSHQVEEKESLVSQLTKSKQALTQQLEELKRQ-----------LEEETK 1328
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNelgrvtflpldSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1329 AKNALAHALQSSRHDCDLLREQYEEEQEGKA-------------ELQRALSKANSEVAQWR------------------- 1376
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggvitggs 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1377 TKYETDAIQRTEELEEAKKKLAqrlqEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKV 1456
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1457 LAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAE-------TGKNLQE 1529
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltlLNEEAAN 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1530 VEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDrKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEI 1609
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELS 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1610 RSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDS-QLHLDDAQRSNEDLKEQLAIVERRNGLLQEE 1688
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 124486959 1689 LEEM-KVALEqtertrrlSEQELLDSSDRVQLLHSQNTSLINTKKKLE 1735
Cdd:TIGR02168 981 IKELgPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1312-1927 |
9.92e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 9.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1312 LTQQLEELKRQLEeetKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdAIQRTEELE 1391
Cdd:COG1196 198 LERQLEPLERQAE---KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE--------LEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1392 EAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAEL 1471
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1472 EAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEV 1551
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1552 EGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKkkmegDLNEMEI 1631
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-----LLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1632 QLSHANRQVAEtqkhlrtVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEEL-EEMKVALEQTE--RTRRLSEQ 1708
Cdd:COG1196 502 DYEGFLEGVKA-------ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVvEDDEVAAAAIEylKAAKAGRA 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1709 ELLdSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkk 1788
Cdd:COG1196 575 TFL-PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT--- 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1789 nleqtvkdLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAhkyERKVKEMTYQAEEDRKNILRL 1868
Cdd:COG1196 651 --------LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA---LLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1869 QDLVDKLQAKVKSYKRQAEEAEEQANTQLSrcrRVQHELEEAEERADIAESQVNKLRAK 1927
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLERE 775
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
222-715 |
2.87e-24 |
|
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: 111.37 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 222 IIQANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVTFQL------SSERSYHIFYQ 290
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 291 IMS--NKKPEL----IDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATD--------NAIDILGFSPEEKVGIYKLTG 356
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 357 AVMHYGNMKFKQKQREEQAEPDGT---EVADKAGYLMGLNSAEMLKGLCCPR---VKVGNEYVTKGQNVQQVTNSVGALA 430
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 431 KAVYEKMFLWMVTRINQ--------------QLDTKQPRQYFIGVL---DIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 493
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 494 HMFVLEQEEYKKEGIEWEfidfgmdlAACIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYDQHLGKSNNFQKP 568
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 569 KPTK--GKAEAH---------FSLVHYAGTVDYNIAGWLDKNKDPL-NETVVGLYQKSSLKLLSFLF-SNYAGAEAGDSA 635
Cdd:cd14894 641 EPPRvlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNeSSQLGWSPNTNR 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 636 GGKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPS 715
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSSSS 800
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1632 |
6.63e-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: 110.53 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 847 AEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKEL 926
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 927 NERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEA 1006
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1007 HQQTLDDLQVEEDKVNGLIKINVKL-----EQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQle 1081
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1082 eklkkKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQrsdlarelEEISERLEEASGAT 1161
Cdd:TIGR02168 480 -----AERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD--------EGYEAAIEAALGGR 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1162 SAQIEMNKKRE--SEFQKLRRDLEEATLQHEATAATLRKKHADTvAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNI 1239
Cdd:TIGR02168 547 LQAVVVENLNAakKAIAFLKQNELGRVTFLPLDSIKGTEIQGND-REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1240 eTVSKSKSNMERMCRSVEDQFNEIKAKDDqqtqLIH-DLNMQKARLQTQNGELSHQVEEKEslvsqltkskqaLTQQLEE 1318
Cdd:TIGR02168 626 -LVVDDLDNALELAKKLRPGYRIVTLDGD----LVRpGGVITGGSAKTNSSILERRREIEE------------LEEKIEE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1319 LKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTeELEEAKKKLA 1398
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-ELEAEIEELE 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1399 QRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKES 1478
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1479 RSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHE 1558
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1559 ESKILRVQLELSQVKSELDRKVTEKDEEIEQikrnSQRAVEAMQSVLDAEIRSrndaLRLKKKMEGDLNEMEIQ 1632
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLEEAEA----LENKIEDDEEEARRRLKR----LENKIKELGPVNLAAIE 993
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1596 |
5.41e-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: 107.45 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 845 KSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVK 924
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 925 ELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQ 1004
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1005 EAHQQTldDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKL 1084
Cdd:TIGR02168 428 KKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1085 KKKEFEMSQLQTRIDDEQVLSLQLQ-----KKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASG 1159
Cdd:TIGR02168 506 EGVKALLKNQSGLSGILGVLSELISvdegyEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1160 ATSAQIEMnKKRESEFQKLRRDLEEATLQHE----------------ATAATLRKK---HADTVAELGEQI--------- 1211
Cdd:TIGR02168 586 IQGNDREI-LKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKlrpGYRIVTLDGDLVrpggvitgg 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1212 -DNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGE 1290
Cdd:TIGR02168 665 sAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1291 LSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANS 1370
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1371 EVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQ 1450
Cdd:TIGR02168 825 RLESLERRIA-ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1451 RNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIF----KMRNAY----EEVVDQLETLRRENKNLQEEISDLTEQIAE 1522
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqeRLSEEYsltlEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1523 TGK-NL------QEVEKTKKQVEQEKSDLQAALEEVEGSLEheeskilrvqlelsqvksELDRKVTEK-DEEIEQIKRNS 1594
Cdd:TIGR02168 984 LGPvNLaaieeyEELKERYDFLTAQKEDLTEAKETLEEAIE------------------EIDREARERfKDTFDQVNENF 1045
|
..
gi 124486959 1595 QR 1596
Cdd:TIGR02168 1046 QR 1047
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1807 |
3.37e-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: 104.76 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 861 ERAKEDLARSEARRKELEekmvSLLQEKNDLQLQVQSETENLmdaeERCEGLIKSKIQLEAKVKELNERleeeeemnsEL 940
Cdd:TIGR02169 173 EKALEELEEVEENIERLD----LIIDEKRQQLERLRREREKA----ERYQALLKEKREYEGYELLKEKE---------AL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 941 VAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNL--------SEEMTALEETISKLTKEKKSLQ---EAHQQ 1009
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLErsiAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1010 TLDDLQVEEDKVNGLIKinvKLEQQTDDLEGSLEQEKKLRAdlervkrKLEGDLKMSQESIMDLENDTQQLEEKLKKKEF 1089
Cdd:TIGR02169 316 ELEDAEERLAKLEAEID---KLLAEIEELEREIEEERKRRD-------KLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1090 EMSQLQTRIDDeqvlslqLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEAsgatsaqIEMNK 1169
Cdd:TIGR02169 386 ELKDYREKLEK-------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-------ALEIK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1170 KRESEFQKLRRDLEEATLQHEATAATLRkkhadtvaelgeqidnlqrvkqKLEKEKSELKMEIDDmasnIETVSKSKSNM 1249
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYD----------------------RVEKELSKLQRELAE----AEAQARASEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRSVEDqfnEIKAKDDQQTQLIHDLNMQKARLQTQ-----NGELSHQVEEKESLVS---QLTKSKQALTQQLEELKR 1321
Cdd:TIGR02169 506 VRGGRAVEE---VLKASIQGVHGTVAQLGSVGERYATAievaaGNRLNNVVVEDDAVAKeaiELLKRRKAGRATFLPLNK 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1322 qleeetkaknalahaLQSSRHDCDLLREqyeeeqegKAELQRALskansEVAQWRTKYETD---AIQRT---EELEEAKK 1395
Cdd:TIGR02169 583 ---------------MRDERRDLSILSE--------DGVIGFAV-----DLVEFDPKYEPAfkyVFGDTlvvEDIEAARR 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1396 KLAQ-RLQEAE-ENTEASNS------KCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDES 1467
Cdd:TIGR02169 635 LMGKyRMVTLEgELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 QAELEAAQKEsrslsteifkmrnaYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAA 1547
Cdd:TIGR02169 715 SRKIGEIEKE--------------IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1548 LEEVEGSLEHEESKILRVQL-ELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQsvldaEIRSRNDALRLKKKMEGD- 1625
Cdd:TIGR02169 781 LNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-----ELQEQRIDLKEQIKSIEKe 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1626 LNEMEIQLSHANRQVAETQKHLRTVQGQLKdsqlhldDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRL 1705
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLG-------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1706 SEQELldssdrvqllhsqntslintkKKLEADLAQCQAEVENS-----IQESRNAEEKAKKAITDAAMMA-EELKKEQDT 1779
Cdd:TIGR02169 929 LEEEL---------------------SEIEDPKGEDEEIPEEElsledVQAELQRVEEEIRALEPVNMLAiQEYEEVLKR 987
|
970 980
....*....|....*....|....*...
gi 124486959 1780 SAHLERMKKNLEQTVKDLQHRLDEAEQL 1807
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1261-1930 |
1.20e-21 |
|
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: 102.95 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1261 NEIKAKDDQQTQLIHDLNMQKARLQTQNgELSHQVEEkesLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSS 1340
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQAET-ELCAEAEE---MRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1341 RHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQEAEENTEASNSKCASLEK 1420
Cdd:pfam01576 102 QQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLAEEEEKAKSLSK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1421 TKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLE 1500
Cdd:pfam01576 181 LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1501 TLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKV 1580
Cdd:pfam01576 261 NALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEET 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1581 TEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLH 1660
Cdd:pfam01576 341 RSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQAR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1661 LDDAQRSNEDLKEQLAiverrngLLQEELEEMKVALEQTERTRRLSEQELldSSDRVQLLHSQNTSLINTKKKLEADLAQ 1740
Cdd:pfam01576 421 LSESERQRAELAEKLS-------KLQSELESVSSLLNEAEGKNIKLSKDV--SSLESQLQDTQELLQEETRQKLNLSTRL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1741 CQAEVE-NSIQESRNAEEKAKKAITdaammaeelKKEQDTSAHLERMKKNLEQTVKDLQhrldeaeqlALKGGKKQIQK- 1818
Cdd:pfam01576 492 RQLEDErNSLQEQLEEEEEAKRNVE---------RQLSTLQAQLSDMKKKLEEDAGTLE---------ALEEGKKRLQRe 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1819 LEARVRELESELDAEQKRGaealKGAHKYERKVKEMTYQAEEDRKNILRL---QDLVDKLQAKVKS----YKRQAEEAEE 1891
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLE----KTKNRLQQELDDLLVDLDHQRQLVSNLekkQKKFDQMLAEEKAisarYAEERDRAEA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 124486959 1892 QANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRD 1930
Cdd:pfam01576 630 EAREKETRALSLARALEEALEAKEELERTNKQLRAEMED 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1592 |
1.36e-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: 102.84 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 847 AEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLqlqvqsetenlmdaeERCEGLIKSKIQLEAKVKEL 926
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA---------------ERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 927 NERleeeeemnsELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNL--------SEEMTALEETISKLTK 998
Cdd:TIGR02169 231 EKE---------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 999 EKKSLQ---EAHQQTLDDLQVEEDKVNGLIKinvKLEQQTDDLEGSLEQEKKLRAdlervkrKLEGDLKMSQESIMDLEN 1075
Cdd:TIGR02169 302 EIASLErsiAEKERELEDAEERLAKLEAEID---KLLAEIEELEREIEEERKRRD-------KLTEEYAELKEELEDLRA 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1076 DTQQLEEKLKKKEFEMSQLQTRIDDeqvlslqLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLE 1155
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEK-------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1156 EAsgatsaqIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHaDTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDM 1235
Cdd:TIGR02169 445 DK-------ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE-KELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1236 ASNIE----TVSKSKSNMERMCRSVE----DQFNEIKAKDD----QQTQLIHDLNMQKA------RLQTQNGELSHQVEE 1297
Cdd:TIGR02169 517 KASIQgvhgTVAQLGSVGERYATAIEvaagNRLNNVVVEDDavakEAIELLKRRKAGRAtflplnKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1298 K---------------ESLVSQLTKSKqALTQQLEELKRQ--------LEEE--------TKAKNALAHALQSSRHDCDL 1346
Cdd:TIGR02169 597 GvigfavdlvefdpkyEPAFKYVFGDT-LVVEDIEAARRLmgkyrmvtLEGElfeksgamTGGSRAPRGGILFSRSEPAE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1347 LREQYEEEQEGKAELQRALSKAN---SEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQ 1423
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRrieNRLDELSQELS-DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1424 RLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEwkQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLR 1503
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1504 RENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEK 1583
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
....*....
gi 124486959 1584 DEEIEQIKR 1592
Cdd:TIGR02169 913 EKKRKRLSE 921
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1259-1797 |
1.44e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1259 QFNEIKAKDD--QQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLtkskQALTQQLEELKRQLEEETKAKNALAHA 1336
Cdd:COG1196 214 RYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1337 LQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEENTEASNSKCA 1416
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1417 SLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVV 1496
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1497 DQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLE-HEESKILRVQLELSQVKSE 1575
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1576 LDRKVTEKDEEIE--------QIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHL 1647
Cdd:COG1196 529 LIGVEAAYEAALEaalaaalqNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1648 RTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRR-------LSEQELLDSSDRVQLL 1720
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGsrrellaALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1721 HSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTS--------------AHLERM 1786
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeeealeelpeppdlEELERE 768
|
570
....*....|.
gi 124486959 1787 KKNLEQTVKDL 1797
Cdd:COG1196 769 LERLEREIEAL 779
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1094-1752 |
3.70e-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: 98.27 E-value: 3.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1094 LQTRIDDEQVL----SLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEeasGATSAQIEMNK 1169
Cdd:pfam15921 90 LQRRLNESNELhekqKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE---AAKCLKEDMLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1170 KRESEFQKLRRDLeeatLQHEATAATLRKKHADTVAELGEQI---DNLQ------------RVKQKLEKEKSELKMEIDD 1234
Cdd:pfam15921 167 DSNTQIEQLRKMM----LSHEGVLQEIRSILVDFEEASGKKIyehDSMStmhfrslgsaisKILRELDTEISYLKGRIFP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1235 MASNIETV-SKSKSNMERMCRSVEDQFNEIKAKDD---------------QQTQLIHDLNMQKARLQTQNGELSHQVEEK 1298
Cdd:pfam15921 243 VEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEveitgltekassarsQANSIQSQLEIIQEQARNQNSMYMRQLSDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1299 ESLVSQLT----KSKQALTQQLEELKRQL----EEETKAKNALAHALQSSRHDCD----LLREQYEEEQEGKAELQRALS 1366
Cdd:pfam15921 323 ESTVSQLRselrEAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDqlqkLLADLHKREKELSLEKEQNKR 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1367 KANSEVAQWRT----KYETD----AIQRTEELEEAKKKLAQ--------RLQEAEENTEASNSKCASLEKTKQRLQGEVD 1430
Cdd:pfam15921 403 LWDRDTGNSITidhlRRELDdrnmEVQRLEALLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1431 DLM---LDLERANTA----CATLDKKQRNFDKVLAE---WKQKLDESQAELEAAQKES---RSLSTEIFKMRNAYEEVVD 1497
Cdd:pfam15921 483 ELTakkMTLESSERTvsdlTASLQEKERAIEATNAEitkLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1498 QLETLRrenknlqEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQ-----LELSQV 1572
Cdd:pfam15921 563 VIEILR-------QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdLELEKV 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1573 K-----SELDRKVTEKDEEIEQIKRNSQRAVEAMQSVL-DAEIRSRNdaLRLK-KKMEGDLNEMEIQLSHANRQVAETQK 1645
Cdd:pfam15921 636 KlvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSeDYEVLKRN--FRNKsEEMETTTNKLKMQLKSAQSELEQTRN 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1646 HLRTVQG--------------QLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQ--TERTRRLSEQE 1709
Cdd:pfam15921 714 TLKSMEGsdghamkvamgmqkQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvaTEKNKMAGELE 793
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 124486959 1710 LLDSSDRVQLLHSQNTSLINTKKKLEadLAQCQAEVENSIQES 1752
Cdd:pfam15921 794 VLRSQERRLKEKVANMEVALDKASLQ--FAECQDIIQRQEQES 834
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1139-1735 |
6.27e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1139 QRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADtVAELGEQIDNLQRVK 1218
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1219 QKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEK 1298
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1299 ESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTK 1378
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1379 YETDAIQRTEELEEAKKKLAQR--LQEAEENTEASNS--KCASLEKTKQRLQGEVDDLMLDLERANTACAT-----LDKK 1449
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLllLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1450 QRNFDKVLAEWKQKLDESQ---AELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKN 1526
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1527 LQEVEKTKKQVEQEKSDLQAALEEVEGSleheeskilrvqlelsqvKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLD 1606
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAG------------------GSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1607 AEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQ 1686
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 124486959 1687 EELEEM-KVALeqtertrrLSEQELLDSSDRVQLLHSQNTSLINTKKKLE 1735
Cdd:COG1196 774 REIEALgPVNL--------LAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1222-1915 |
8.08e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.52 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1222 EKEKSELKMEIDDMASNIETVSKSKSnmermCRSVEDQFneiKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEE--KE 1299
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAED-----ARKAEEAR---KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAarKA 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1300 SLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGK-AELQRAlskaNSEVAQWRTK 1378
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEERN----NEEIRKFEEA 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1379 YETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASlEKTKqrlqgeVDDLMLDLERANTAcATLDKKQRNFDKVLA 1458
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE-EKKK------ADEAKKKAEEAKKA-DEAKKKAEEAKKKAD 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1459 EWKQKLDESQAELEAAQKESRSLSTEIfkmrNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVE 1538
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1539 QEKSDLQAALEEVEGSLEHEESKilrvqlelsqvKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRL 1618
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKK-----------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1619 KKKMEGDLNEMEIQLSHANRQVAETQKhlrTVQGQLKDSQLHLDDAQRSNEDLK---EQLAIVERRNGLLQEELEEMKVA 1695
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKA 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1696 LE-QTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAitdaammaEELK 1774
Cdd:PTZ00121 1555 EElKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELK 1626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1775 KEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGG--KKQIQKLEARVRELESElDAEQKRGAEALKGAHKYERKVK 1852
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1853 EMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAE---EQANTQLSRCRRVQHELEEAEERAD 1915
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1447-1928 |
3.09e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1447 DKKQRNFDKVLAEWKQKLDESQAELE--AAQKEsRSLSTeifkmRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETg 1524
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIEryEEQRE-QARET-----RDEADEVLEEHEERREELETLEAEIEDLRETIAET- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1525 knlqevEKTKKQVEQEKSDLQAALEEVEGSLEH--EESKILRVQLE-LSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAM 1601
Cdd:PRK02224 271 ------EREREELAEEVRDLRERLEELEEERDDllAEAGLDDADAEaVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1602 QSVLD--AEIRSRNDALRLK-KKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIV 1678
Cdd:PRK02224 345 ESLREdaDDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1679 ERRNGLLQEELEEMKVALEQTERTRRLS-----EQELLDSSDRVQLLHSQNTslintKKKLEADLAQCQAEVENsiqesr 1753
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGkcpecGQPVEGSPHVETIEEDRER-----VEELEAELEDLEEEVEE------ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1754 nAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELESELDAE 1833
Cdd:PRK02224 494 -VEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRE--------RAEELRERAAELEAEAEEK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1834 QKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDkLQAKVKSYKRQAE----------EAEEQANTQLSRCRRV 1903
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT-LLAAIADAEDEIErlrekrealaELNDERRERLAEKRER 635
|
490 500
....*....|....*....|....*
gi 124486959 1904 QHELEEAEERADIAESQVNKLRAKS 1928
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEE 660
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1553 |
3.63e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 848 EAEKEMatmkedfERAKEDLARSEARRKELEEKMVSllqekndlqLQVQSETenlmdAEERCEglikskIQLEAKVKELN 927
Cdd:COG1196 176 EAERKL-------EATEENLERLEDILGELERQLEP---------LERQAEK-----AERYRE------LKEELKELEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 928 erleeeeemnsELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAH 1007
Cdd:COG1196 229 -----------LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1008 QQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESImdlendtQQLEEKLKKK 1087
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL-------AEAEEALLEA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1088 EFEMSQLQTRIDDEQVLSLQLQKKIKELQARteeleeeieaehtvrakIEKQRSDLARELEEISERLEEASGATSAQIEM 1167
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQ-----------------LEELEEAEEALLERLERLEEELEELEEALAEL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1168 NKKRESEFQKLRRDLEEAtLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKM--EIDDMASNIETVSKS 1245
Cdd:COG1196 434 EEEEEEEEEALEEAAEEE-AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLllEAEADYEGFLEGVKA 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1246 KSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNmqkARLQTQNGELSHQVEEKESLVSQltKSKQALTQQLEELKRQLEE 1325
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA---AALQNIVVEDDEVAAAAIEYLKA--AKAGRATFLPLDKIRARAA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1326 ETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLAQRLQEA 1404
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRaVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1405 EENTEASNSKCASLEKTKQRLQGEVDDLMLDLERAntacatLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTE 1484
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAE------EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1485 IFKMRNAYEEVVDQLETLRRENKnLQEEISDLTEQIAETGK-NL------QEVEKTKKQVEQEKSDLQAALEEVEG 1553
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEE-LERELERLEREIEALGPvNLlaieeyEELEERYDFLSEQREDLEEARETLEE 816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1133-1926 |
1.25e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1133 RAKIEKQRSDLARELEEI-----SERLEEASGATSAQIEMNKKRESEFQKLR--RDLEEATLQHEA-TAATLRKKHADTV 1204
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEArkaedARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1205 AELGEQIDNLQRVKQKLEKEKSElKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTqlIHDLNMQKARL 1284
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1285 QTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHAlQSSRHDCDLLREQYEEEQEGKAELQRA 1364
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1365 LSKANSEVAQWRTKYETDAIQRTEE---LEEAKKKLAQRLQEAEENTEASNSKCASLE-KTKQRLQGEVDDLMLDLERAN 1440
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKK 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1441 TACATldKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQi 1520
Cdd:PTZ00121 1432 KADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA- 1508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1521 AETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSqvKSELDRKVTEKDEEiEQIKRNSQRAVEA 1600
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEE 1585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1601 MQSVLDAEIRSRNDALRLKKKMEGDlnemEIQLSHANRQVAEtqkhlrtvqgQLKDSQlhldDAQRSNEDLKEQLAIVER 1680
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAE----------ELKKAE----EEKKKVEQLKKKEAEEKK 1647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1681 RNGLLQEELEEMKVALEQTERTrrlSEQElldssdrvqllhsqntslintKKKLEadlaqcqaevensiqESRNAEEKAK 1760
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKK---AEED---------------------KKKAE---------------EAKKAEEDEK 1688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1761 KAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAEA 1840
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1841 lkgAHKYERKVKEMTYQAEEDRKNILRLQDlVDKLQAKVKSYKRQAEEAEEQANTQLSRCRrvQHELEEAEERADIAESQ 1920
Cdd:PTZ00121 1769 ---KAEEIRKEKEAVIEEELDEEDEKRRME-VDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSKNMQ 1842
|
....*.
gi 124486959 1921 VNKLRA 1926
Cdd:PTZ00121 1843 LEEADA 1848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
969-1879 |
1.53e-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: 92.82 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 969 EKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTL--DDLQVEEDKVNGLIKIN---------VKLEQQTDD 1037
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEGYELLKekealerqkEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1038 LEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQqleeklkkkefemSQLQTRIDDEQVLSLQLQKKIKELQA 1117
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ-------------LRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1118 RTEELEEEieaehtvRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEAtlqhEATAATLR 1197
Cdd:TIGR02169 316 ELEDAEER-------LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1198 KKHADTVAEL---GEQIDNLQRVKQKLEKEKSELKMEIDDMAsnietvsksksnmermcrsvedqfNEIKAKDDQQTQLI 1274
Cdd:TIGR02169 385 DELKDYREKLeklKREINELKRELDRLQEELQRLSEELADLN------------------------AAIAGIEAKINELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1275 HDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALtQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEE 1354
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1355 QEG-----------KAELQRALSKANSEVAQwRTKYETDAIQRtEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQ 1423
Cdd:TIGR02169 520 IQGvhgtvaqlgsvGERYATAIEVAAGNRLN-NVVVEDDAVAK-EAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDG 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1424 RLQGEVD-------------------DLMLDLERA-----NTACATLD--------------KKQRNFDKVLAEWKQKLD 1465
Cdd:TIGR02169 598 VIGFAVDlvefdpkyepafkyvfgdtLVVEDIEAArrlmgKYRMVTLEgelfeksgamtggsRAPRGGILFSRSEPAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1466 ESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQ 1545
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1546 AALEEVEGSLEHEESKILRVQLELSQVKSELDRkvtekdEEIEQIkRNSQRAVEAMQSVLDAEIRSrndalrlkkkMEGD 1625
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEARLSH------SRIPEI-QAELSKLEEEVSRIEARLRE----------IEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1626 LNEMEIQLSHANRQVAEtqkhlrtvqgqlkdsqlhlddAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTertrrl 1705
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQE---------------------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL------ 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1706 sEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVEnsIQESRNAEEKAKKAItdaamMAEELKkeqdtsaHLER 1785
Cdd:TIGR02169 874 -EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE--KKRKRLSELKAKLEA-----LEEELS-------EIED 938
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1786 MKKNLEQtvkdlqhrlDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMtyqaEEDRKNI 1865
Cdd:TIGR02169 939 PKGEDEE---------IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKL----EEERKAI 1005
|
970
....*....|....
gi 124486959 1866 LRLQDLVDKLQAKV 1879
Cdd:TIGR02169 1006 LERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1594 |
3.82e-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: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 847 AEAEKEmatmKEDFERAKEDLA-RSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKiQLEAKvke 925
Cdd:TIGR02169 247 ASLEEE----LEKLTEEISELEkRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK-ERELE--- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 926 lnerleeeeemnsELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQE 1005
Cdd:TIGR02169 319 -------------DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1006 AHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLK 1085
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1086 KKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRS---DLARELEEISER----LEEAS 1158
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERyataIEVAA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1159 GA------------TSAQIEMNKKRES------EFQKLRRDLEEATLQHEATAAtlrkKHADTVAELGEQIDNLQR---- 1216
Cdd:TIGR02169 546 GNrlnnvvveddavAKEAIELLKRRKAgratflPLNKMRDERRDLSILSEDGVI----GFAVDLVEFDPKYEPAFKyvfg 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1217 ---VKQKLEKEKS--------ELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQ 1285
Cdd:TIGR02169 622 dtlVVEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1286 TQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRAL 1365
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1366 SKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACAT 1445
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1446 LDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGK 1525
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1526 NLQE----------VEKTKKQVEQEKSDLQaALEEVEGSLEHEESKILRVQLELSQVKSELDRK---VTEKDEEIEQIKR 1592
Cdd:TIGR02169 939 PKGEdeeipeeelsLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKR 1017
|
..
gi 124486959 1593 NS 1594
Cdd:TIGR02169 1018 EV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1294-1925 |
3.88e-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: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1294 QVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKnalahalqssrhdcDLLREQYEEEQEGKAELQRALSKANSEVa 1373
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL--------------EKLTEEISELEKRLEEIEQLLEELNKKI- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1374 qwRTKYETDAIQRTEELEEAKKKLAQrlqeAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNF 1453
Cdd:TIGR02169 282 --KDLGEEEQLRVKEKIGELEAEIAS----LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1454 DKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKT 1533
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1534 KKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDR---KVTEKDEEIEQIK------RNSQRAVEAMQSV 1604
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRvekELSKLQRELAEAEaqarasEERVRGGRAVEEV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1605 LDAEIR---------------------------------------------------SRNDALRLKK-----------KM 1622
Cdd:TIGR02169 516 LKASIQgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiellkrrkaGRATFLPLNKmrderrdlsilSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1623 EG------DLNEMEIQLSHANRQV---------AETQKHLR------TVQGQLKDSQLHL----DDAQRSNEDLKEQLAI 1677
Cdd:TIGR02169 596 DGvigfavDLVEFDPKYEPAFKYVfgdtlvvedIEAARRLMgkyrmvTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1678 VERrnglLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEE 1757
Cdd:TIGR02169 676 LQR----LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1758 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQtvKDLQHRLDEAEQLALKgGKKQIQKLEARVRELESELDAEQKRG 1837
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSK-LEEEVSRIEARLREIEQKLNRLTLEK 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1838 AEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIA 1917
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
....*...
gi 124486959 1918 ESQVNKLR 1925
Cdd:TIGR02169 909 EAQIEKKR 916
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1911 |
9.15e-18 |
|
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: 90.41 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1212 DNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNmQKARLQTQNGEL 1291
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1292 SHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEEtkaknALAHALQSSRhdcdllrEQYEEEQEGKAELQRALSKANSE 1371
Cdd:TIGR00618 266 RARIEELRAQEAVLEETQERINRARKAAPLAAHIK-----AVTQIEQQAQ-------RIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1372 VAQwrtkyETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTkQRLQGEVDDLMLDLERANTACATLDKKQR 1451
Cdd:TIGR00618 334 VKQ-----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1452 NFDKVLAEWKQKLDEsQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVE 1531
Cdd:TIGR00618 408 EQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1532 KTKKQVEQEKSDLQAALEEVEGSLEHEE-------------SKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAV 1598
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPLCGSCIHPNparqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1599 EAMQSVLDAEI---RSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQL 1675
Cdd:TIGR00618 567 EIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1676 AIVERRNGLLQEELEemkvalEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNA 1755
Cdd:TIGR00618 647 ALHALQLTLTQERVR------EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1756 EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ---IQKLEARVRELESELDA 1832
Cdd:TIGR00618 721 NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAEIQFFNRLREEDTHL 800
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1833 EQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAE 1911
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1403 |
1.26e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 843 LLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAK 922
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 VKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKS 1002
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1003 LQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEE 1082
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1083 KLKKKEFEMSQLQTRIDDE--QVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGA 1160
Cdd:COG1196 471 EAALLEAALAELLEELAEAaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1161 TSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDnlqRVKQKLEKEKSELKMEIDDMASNIE 1240
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD---LVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1241 TVSKSKSNMERMCRSVEDQFNEIKAKDdqqtqlihDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELK 1320
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGE--------GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1321 RQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQR 1400
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
...
gi 124486959 1401 LQE 1403
Cdd:COG1196 776 IEA 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
943-1589 |
3.15e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 88.15 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 943 KKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLT-KEKKSlqeahQQTLDDLQVEEDKV 1021
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNdKLKKN-----KDKINKLNSDLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1022 NGLIKIN----VKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTR 1097
Cdd:TIGR04523 109 NSEIKNDkeqkNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1098 IDDEQVLSLQLQKKIKELQArteeleeeieaehtvraKIEKQRSdLARELEEISERleeasgatsaqiemNKKRESEFQK 1177
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKK-----------------KIQKNKS-LESQISELKKQ--------------NNQLKDNIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1178 LRRDLEEATlqheataatlrkkhadtvAELGEQIDNLQRVKQKLEKEKSELKmeidDMASNIETVSKSKSNMErmcrsve 1257
Cdd:TIGR04523 237 KQQEINEKT------------------TEISNTQTQLNQLKDEQNKIKKQLS----EKQKELEQNNKKIKELE------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1258 DQFNEIKAKddqqtqlIHDLNMQKAR--LQTQNGELSHQVEEKESLVSQLTKSKQALTQqLEELKRQLEEEtkaknalah 1335
Cdd:TIGR04523 288 KQLNQLKSE-------ISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQ-LNEQISQLKKE--------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1336 aLQSSRHDCDLLREQYEEEQegkaelqRALSKANSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKC 1415
Cdd:TIGR04523 351 -LTNSESENSEKQRELEEKQ-------NEIEKLKKENQSYK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1416 ASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEV 1495
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1496 VDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHE--ESKILRVQLELSQVK 1573
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELK 574
|
650
....*....|....*....
gi 124486959 1574 SE---LDRKVTEKDEEIEQ 1589
Cdd:TIGR04523 575 QTqksLKKKQEEKQELIDQ 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
871-1591 |
4.59e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.77 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 871 EARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERcegliksKIQLEAKVKelnerleeeeemnsELVAKKRNLEDK 950
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEK-------INNSNNKIK--------------ILEQQIKDLNDK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 951 CSSLKRDIDDLELTLTKVEKEkhatenkVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQVEEDKvngLIKINVK 1030
Cdd:TIGR04523 91 LKKNKDKINKLNSDLSKINSE-------IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE---LEKLNNK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1031 LEqqtddlegsleqekklraDLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQ--- 1107
Cdd:TIGR04523 161 YN------------------DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQise 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1108 LQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATL 1187
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1188 QheataatlrkKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNE----- 1262
Cdd:TIGR04523 303 Q----------KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqnei 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1263 --IKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQ---LEEETKAKNALAHAL 1337
Cdd:TIGR04523 373 ekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiikNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1338 QSSRHDCDLLREQYEEEQEgkaELQRALSKANSEVaQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCAS 1417
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLK---VLSRSINKIKQNL-EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1418 LEKTKQRLQGEVDDLMLDLERANTacatlDKKQRNFDKVLAEWKQKLDES---QAELEAAQKESrslsteifkmrnayEE 1494
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEK--------------QE 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1495 VVDQLETlrrENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKS 1574
Cdd:TIGR04523 590 LIDQKEK---EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
730
....*....|....*..
gi 124486959 1575 ELDRKVTEKDEEIEQIK 1591
Cdd:TIGR04523 667 KIKESKTKIDDIIELMK 683
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1314-1918 |
4.81e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.05 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1314 QQLEELKRQLEEETKAKNALAHALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQwrTKYETdAIQRTEELEEA 1393
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1394 KKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGE-VDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELE 1472
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1473 AAQKESRSLSTEIfkmRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAEtgknlqeVEKTKKQVEQEksdLQAALEEVE 1552
Cdd:COG4913 384 ALRAEAAALLEAL---EEELEALEEALAEAEAALRDLRRELRELEAEIAS-------LERRKSNIPAR---LLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1553 GSLEHEESKiLRVQLELSQVKSElDRK-----------------VTEKDEE-----IEQIKrNSQRAV-EAMQSVLDAEI 1609
Cdd:COG4913 451 EALGLDEAE-LPFVGELIEVRPE-EERwrgaiervlggfaltllVPPEHYAaalrwVNRLH-LRGRLVyERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1610 RSRNDALRLKKKMEGDLN------EMEIQlSHANRQVAETQKHLR------TVQGQLKDS-QLH-LDDAQRSNEDL---- 1671
Cdd:COG4913 528 RPRLDPDSLAGKLDFKPHpfrawlEAELG-RRFDYVCVDSPEELRrhpraiTRAGQVKGNgTRHeKDDRRRIRSRYvlgf 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1672 --KEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSqntslintkkklEADLAQCQAEVENsi 1749
Cdd:COG4913 607 dnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD------------EIDVASAEREIAE-- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1750 qesrnaeekakkaitdaamMAEELKKEQDTSAHLERmkknLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELESE 1829
Cdd:COG4913 673 -------------------LEAELERLDASSDDLAA----LEEQLEELEAELEELEE--------ELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1830 L-DAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNIL---RLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRvQH 1905
Cdd:COG4913 722 LeQAEEELDELQDRLEAAEDLARLELRALLEERFAAALgdaVERELRENLEERIDALRARLNRAEEELERAMRAFNR-EW 800
|
650
....*....|...
gi 124486959 1906 ELEEAEERADIAE 1918
Cdd:COG4913 801 PAETADLDADLES 813
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1210-1889 |
1.20e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1210 QIDNLQRVKQKLEKEKSELKMEIDdmasNIETVSKSKSNMERMCRSVEDQF----NEIKAKDDQQTQLIHDLNMQKARLQ 1285
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEKELeevlREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1286 TQNgELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEetkaknalahalqsSRHDCDLLREQYEE--EQEGKAELQR 1363
Cdd:PRK03918 232 ELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--------------LKKEIEELEEKVKElkELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1364 ALSKansevaqWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMldlerantac 1443
Cdd:PRK03918 297 KLSE-------FYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE---------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1444 atldkkqrnfdkVLAEWKQKLDESQAELEAAQKESRSLSTEifkmrnAYEEVVDQLETLRRENKNLQEEISDLTEQIAEt 1523
Cdd:PRK03918 356 ------------ELEERHELYEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1524 gknlqevektkkqVEQEKSDLQAALEEVEG------------SLEHEESKILRVQLELSQVKSELdRKVTEKDEEIEQIK 1591
Cdd:PRK03918 417 -------------LKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKEL 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1592 RNSQRAVEAmqsvlDAEIRSRNDALRLKKKMEGDLNEMEIQ-LSHANRQVAETQKHLRTVQGQLKDsqlhLDDAQRSNED 1670
Cdd:PRK03918 483 RELEKVLKK-----ESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKS----LKKELEKLEE 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1671 LKEQLAIVERRNGLLQEELEEMkvaLEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADlaqcqaevensiq 1750
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAEL---LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE------------- 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1751 esrnaEEKAKKAITDAAMMAEELkkeQDTSAHLERMKKNLEQtvkdLQHRLDEAEQlalKGGKKQIQKLEARVRELESEL 1830
Cdd:PRK03918 618 -----EKELKKLEEELDKAFEEL---AETEKRLEELRKELEE----LEKKYSEEEY---EELREEYLELSRELAGLRAEL 682
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1831 DAEQKRGAEALKGAHKYERKVKEMTyQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1458-1805 |
2.31e-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: 85.89 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1458 AEWKQKLDESQAELEAAQKESRSLSTEIfkmrnayEEVVDQLETLRREnKNLQEEISDLTEQIAETG-----KNLQEVEK 1532
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLII-------DEKRQQLERLRRE-REKAERYQALLKEKREYEgyellKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1533 TKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKvteKDEEIEQIKRNsQRAVEAMQSVLDAEIRSR 1612
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEK-IGELEAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1613 NDALrlkKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEM 1692
Cdd:TIGR02169 314 EREL---EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1693 KVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAitdAAMMAEE 1772
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL---AADLSKY 467
|
330 340 350
....*....|....*....|....*....|...
gi 124486959 1773 LKKEQDTSAHLERMKKNLEQtvkdLQHRLDEAE 1805
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSK----LQRELAEAE 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1246-1909 |
3.23e-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: 85.17 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1246 KSNMERMCRSVEDQFNEIKAKDDQQTQLiHDlnMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLE- 1324
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNEL-HE--KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQn 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1325 ---EETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALskANSEVAQWRTKYETDAIQRT-------------E 1388
Cdd:pfam15921 150 tvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMhfrslgsaiskilR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1389 ELEEAKKKLAQRLQEAEENTEASNSKCAS-LEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNfdkvlaewkqKLDES 1467
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEHEVEITGLTEKASSARS----------QANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 QAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEE-ISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQA 1546
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSQESGNLDD 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1547 ALE---------EVEGSLEHEESKIL-RVQLELSQVKSELDRKVTEKDEEIEQIkrnsQRAVEAMQSVLDAEIRSRNDAL 1616
Cdd:pfam15921 378 QLQklladlhkrEKELSLEKEQNKRLwDRDTGNSITIDHLRRELDDRNMEVQRL----EALLKAMKSECQGQMERQMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1617 RLKkkmegdlNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKeqlaiverrngllqeeleemkVAL 1696
Cdd:pfam15921 454 QGK-------NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLT---------------------ASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1697 EQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAeVENSIQESRNAEEKAKKAITDaamMAEELKKE 1776
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIEN---MTQLVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1777 QDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKqIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTY 1856
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 124486959 1857 QAEEDRKNilrLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEE 1909
Cdd:pfam15921 661 EVKTSRNE---LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
918-1807 |
3.54e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.58 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 918 QLEAKVKELNERLEEEEEMNSELVAKKRNLEDKCSS--LKRDIDDLELTLTKVEKEKHATENKVKnlSEEMTALEEtiSK 995
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKK--AEDARKAEE--AR 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 996 LTKEKKSLQEAHQQTLDDLQVEEDKVNGLIKINV--------KLEQQTDDLEGSLEQEKKLRADLERVK--RKLEGDLKM 1065
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEarkaedakKAEAARKAEEVRKAEELRKAEDARKAEaaRKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1066 SQESIMDLENDTQ--QLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDL 1143
Cdd:PTZ00121 1215 EEARKAEDAKKAEavKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1144 ARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAelgEQIDNLQRVKQKLEK 1223
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA---DEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1224 EKSELKMEIDDMASNIETVSKSksnmermcrsvedqfNEIKAKDDQQTQLIHDLNmQKARLQTQNGELSHQVEEKESlvS 1303
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKA---------------DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKK--A 1433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1304 QLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRhdCDLLREQYEEEQEGKaELQRALSKANSEVAQWRTKYEtdA 1383
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAE--A 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1384 IQRTEELEEA-KKKLAQRLQEAEENTEASNSKCASlEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQ 1462
Cdd:PTZ00121 1509 KKKADEAKKAeEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1463 KLDESQAElEAAQKESRSLSTEIFKMRNAyEEVVDQLETLRREnKNLQEEISDLTEQIAETGKNLQEVEKtkkqvEQEKS 1542
Cdd:PTZ00121 1588 KAEEARIE-EVMKLYEEEKKMKAEEAKKA-EEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKK-----AEEEN 1659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1543 DLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKM 1622
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1623 EGDLNEMEiqlshaNRQVAETQKHlrtvqgqlKDSQLHLDDAQRSNEDLKEQLAIVERRnglLQEELEEMKVALEQTERt 1702
Cdd:PTZ00121 1740 EEDKKKAE------EAKKDEEEKK--------KIAHLKKEEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIK- 1801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1703 rrlseqELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDaammaeELKKEQDTSAH 1782
Cdd:PTZ00121 1802 ------DIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN------ENGEDGNKEAD 1869
|
890 900
....*....|....*....|....*
gi 124486959 1783 LERMKKNLEQTVKDLQHRlDEAEQL 1807
Cdd:PTZ00121 1870 FNKEKDLKEDDEEEIEEA-DEIEKI 1893
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
840-1432 |
5.17e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 840 IKPLLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERceglikskiQL 919
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---------EL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 920 EAKVKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKE 999
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1000 KKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQ 1079
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1080 LEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKiEKQRSDLARELEEISERLEEASG 1159
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1160 ATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRvkQKLEKEKSELKMEIDDMASNI 1239
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA--AKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1240 ETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQL-----IHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQ 1314
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLgrtlvAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1315 QLEELKRQLEEETKAKNALAHALQSSRHdcDLLREQYEEEQEGKAELQRALSKANSEVAQwRTKYETDAIQRTEELEEAK 1394
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEEE 746
|
570 580 590
....*....|....*....|....*....|....*...
gi 124486959 1395 KKLAQRLQEAEENTEAsnskcASLEKTKQRLQGEVDDL 1432
Cdd:COG1196 747 LLEEEALEELPEPPDL-----EELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1212-1893 |
5.26e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1212 DNLQRVKQKLEKEKSELKMEIddmasnietvsKSKSNMERMCRSVEDQF----NEIKAKDDQQTQLIHDLNMQKARLQTQ 1287
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELeevlREINEISSELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1288 NgELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEetkaknalahalqsSRHDCDLLREQYEE--EQEGKAELQRAL 1365
Cdd:PRK03918 234 E-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE--------------LKKEIEELEEKVKElkELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1366 SKansevaqWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMldlerantacat 1445
Cdd:PRK03918 299 SE-------FYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE------------ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1446 ldkkqrnfdkVLAEWKQKLDESQAELEAAQKESRSLSTEifkmrnAYEEVVDQLETLRRENKNLQEEISDLTEQIAEtgk 1525
Cdd:PRK03918 356 ----------ELEERHELYEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGE--- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1526 nlqevektkkqVEQEKSDLQAALEEVEG------------SLEHEESKILRVQLELSQVKSELdRKVTEKDEEIEQIKRN 1593
Cdd:PRK03918 417 -----------LKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKEL-KEIEEKERKLRKELRE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1594 SQRAVEAmqsvlDAEIRSRNDALRLKKKMEGDLNEMEIQ-LSHANRQVAETQKHLRTVQGQLKDsqlhLDDAQRSNEDLK 1672
Cdd:PRK03918 485 LEKVLKK-----ESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKS----LKKELEKLEELK 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1673 EQLAIVERRNGLLQEELEEMkvaLEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADlaqcqaevensiqes 1752
Cdd:PRK03918 556 KKLAELEKKLDELEEELAEL---LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE--------------- 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1753 rnaEEKAKKAITDAAMMAEELkkeQDTSAHLERMKKNLEQtvkdLQHRLDEAEQlalKGGKKQIQKLEARVRELESELDA 1832
Cdd:PRK03918 618 ---EKELKKLEEELDKAFEEL---AETEKRLEELRKELEE----LEKKYSEEEY---EELREEYLELSRELAGLRAELEE 684
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1833 EQKRGAEALKGAHKYERKVKEMTyQAEEDRKNILRLQDLVDKLQAKVKSYKrqaEEAEEQA 1893
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELREKVKKYK---ALLKERA 741
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1542 |
1.38e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 82.76 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 848 EAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLeakvkeln 927
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI-------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 928 erleeeeemNSELVAKKRNLedkcSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAH 1007
Cdd:TIGR04523 109 ---------NSEIKNDKEQK----NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1008 QQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRK---LEGDLKMSQESIMDLENDTQQLEekl 1084
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQ--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1085 kkkefemSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIE----KQRSDLARELEEISERLEEASGA 1160
Cdd:TIGR04523 253 -------TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1161 TSAQIEMNKKRESEF----QKLRRDLEEATLQHEATAATLRKKHadtvaelgEQIDNLQRVKQKLEKEKSELKMEIDDMA 1236
Cdd:TIGR04523 326 IQNQISQNNKIISQLneqiSQLKKELTNSESENSEKQRELEEKQ--------NEIEKLKKENQSYKQEIKNLESQINDLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1237 SNIETVSKSKSNMERMCRSVEDQFNEI-------KAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSK 1309
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1310 QALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRT-E 1388
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1389 ELEEAKKKLAQRLQEAEENTEasnskcaSLEKTKQRLQGEVDDlmldlerantacatLDKKQRNFDKVLAEWKQKLDESQ 1468
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQK-------SLKKKQEEKQELIDQ--------------KEKEKKDLIKEIEEKEKKISSLE 616
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1469 AELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKS 1542
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
857-1538 |
4.57e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 857 KEDFERAKEDLARSEARRKELEEKMVSLLQEKNDL-QLQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNERLEEeee 935
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDArKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE--- 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 936 mnSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALE----ETISKLTKEKKSLQEAHQQTL 1011
Cdd:PTZ00121 1242 --AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAKKADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1012 DDLQVEEDKVNGlIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQEsimdlENDTQQLEEKLKKKEFEM 1091
Cdd:PTZ00121 1320 AKKKAEEAKKKA-DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-----AKKKADAAKKKAEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1092 SQLQTRIDDEQVLSLQLQKKIKElqaRTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKR 1171
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1172 ESEfqKLRRDLEEATLQHEA-TAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKS-ELKMEIDDMASNIETVSKSKSNM 1249
Cdd:PTZ00121 1471 KAD--EAKKKAEEAKKADEAkKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAdEAKKAEEAKKADEAKKAEEKKKA 1548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARlqtqnGELSHQVEEKEsLVSQLTKSKQALTQQLEELKRqlEEETKA 1329
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-----AEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK--AEEAKI 1620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1330 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL----EEAKKKLAQRLQEAE 1405
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKAAEALKKEAE 1699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1406 ENTEASNSKCASLEKTKQRLQgevddlMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEI 1485
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEE------LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 124486959 1486 FKMRNAY--EEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVE 1538
Cdd:PTZ00121 1774 RKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1423-1927 |
6.79e-15 |
|
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: 80.93 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1423 QRLQGEVDDLMLDLERANTACATLDKKQRNF-DKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLET 1501
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1502 LRRENKNLQEEISDLTEQiaetgknLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKIlrVQLELSQVKSELDRKVT 1581
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQ-------LRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSM--STMHFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1582 EKDEEIEQIKrNSQRAVEAMQSVLDAEIRSRNDAL--RLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQl 1659
Cdd:pfam15921 228 ELDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1660 hlDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEqtERTRRLSEQELLDSSDrvqllhsqntslintkkkleadLA 1739
Cdd:pfam15921 306 --EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE--DKIEELEKQLVLANSE----------------------LT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1740 QCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKL 1819
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQRL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1820 EARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKnilRLQDLVDKLQAkvksyKRQAEEAEEQANTQLSR 1899
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTA-----KKMTLESSERTVSDLTA 503
|
490 500
....*....|....*....|....*...
gi 124486959 1900 crrvqhELEEAEERADIAESQVNKLRAK 1927
Cdd:pfam15921 504 ------SLQEKERAIEATNAEITKLRSR 525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-1938 |
7.40e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1612 RNDALRLKKKMEGDLN-------EMEIQLSHANRQVAETQKHlRTVQGQLKDSQ-----LHLDDAQRSNEDLKEQLAIVE 1679
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERY-RELKEELKELEaelllLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1680 RRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKA 1759
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1760 KKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELESELDAEQKRGAE 1839
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1840 ALKGAHKYERkvkemtyQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSrcRRVQHELEEAEERADIAES 1919
Cdd:COG1196 412 LLERLERLEE-------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE--LLAELLEEAALLEAALAEL 482
|
330
....*....|....*....
gi 124486959 1920 QVNKLRAKSRDVGGQKMEE 1938
Cdd:COG1196 483 LEELAEAAARLLLLLEAEA 501
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
851-1774 |
8.51e-15 |
|
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: 80.86 E-value: 8.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 851 KEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKnDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNERL 930
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 931 EEEEEMNSELVAKK--------RNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKS 1002
Cdd:TIGR00606 279 KQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1003 LQEaHQQTLDDLQVEedkvnglikinVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEE 1082
Cdd:TIGR00606 359 HQE-HIRARDSLIQS-----------LATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1083 KLKKKEFEMSQLQTRIDDEQVLslqLQKKIKELQARTEELEeeieaehtvraKIEKQRSDLARELEEISERLEEASGA-T 1161
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAERELSKAeK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1162 SAQIEMNKKRESEFQKLRRDLEEAtlqheataatlRKKHADTVAELGEQIDNLQRVkQKLEKEKSELKMEIDDMASNIET 1241
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRK-----------LRKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1242 VSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTK------SKQALTQQ 1315
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEESD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1316 LEELKRQLEEETKAKNALAHALQssrhdcdlLREQYEEEQEGKaelqralSKANSEVAQwrtkyetDAIQRTEELEEAKK 1395
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1396 KLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELE--- 1472
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtim 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1473 AAQKESRSLSTEIFKMRNAYEEVVD-------------------QLETLRRENKNLQEEISDLTEQIAETGKNLQEVEK- 1532
Cdd:TIGR00606 779 PEEESAKVCLTDVTIMERFQMELKDverkiaqqaaklqgsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEq 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1533 ------TKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQ---LELSQVKSE-------LDRKVTEKDEEI---EQIKRN 1593
Cdd:TIGR00606 859 iqhlksKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQsliREIKDAKEQdspletfLEKDQQEKEELIsskETSNKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1594 SQRAVEAMQSVLDAEIRSRNDALR-LKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLK 1672
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1673 EQLAIVERRNGL--LQEELEEMKVALEQTERTRRLSEQELLDSSDRvqlLHSQNTSLINTKKKlEADLAQCQAEVENSIQ 1750
Cdd:TIGR00606 1019 DNLTLRKRENELkeVEEELKQHLKEMGQMQVLQMKQEHQKLEENID---LIKRNHVLALGRQK-GYEKEIKHFKKELREP 1094
|
970 980
....*....|....*....|....
gi 124486959 1751 ESRNAEEKAKKAITDAAMMAEELK 1774
Cdd:TIGR00606 1095 QFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
846-1607 |
1.52e-14 |
|
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: 79.73 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 846 SAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKE 925
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 926 LNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQE 1005
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1006 AhqqtlddLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLK 1085
Cdd:TIGR02169 449 E-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1086 KKEFEMSQLqTRIDDEQVLSLQ------LQKKIKELQARTEELEEEIEAEHTVRAK---IEKQRSDLaRELEEISErlEE 1156
Cdd:TIGR02169 522 GVHGTVAQL-GSVGERYATAIEvaagnrLNNVVVEDDAVAKEAIELLKRRKAGRATflpLNKMRDER-RDLSILSE--DG 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1157 ASGATSAQIEMNKKRESEFQKLRRD------LEEA----------TLQHE-------ATAATLRKKHADTVA-ELGEQID 1212
Cdd:TIGR02169 598 VIGFAVDLVEFDPKYEPAFKYVFGDtlvvedIEAArrlmgkyrmvTLEGElfeksgaMTGGSRAPRGGILFSrSEPAELQ 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1213 NLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLnmqKARLQtqngELS 1292
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLS----SLE 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1293 HQVEEKESLVSQLTKSKQALTQQLEELKRQLEeetkaknalahalqssrhdcDLLReqyEEEQEGKAELQRALSKANSEV 1372
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALN--------------------DLEA---RLSHSRIPEIQAELSKLEEEV 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1373 AQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRN 1452
Cdd:TIGR02169 808 SRIE--------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1453 FDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETgKNLQEVEK 1532
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE-LSLEDVQA 958
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1533 TKKQVEQEKSDLQ----AALEEVEgsleheeskilRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDA 1607
Cdd:TIGR02169 959 ELQRVEEEIRALEpvnmLAIQEYE-----------EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEA 1026
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1292-1931 |
1.61e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1292 SHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAkNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSE 1371
Cdd:PTZ00121 1023 NFNIEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKA-EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1372 VAQwrtKYETDAIQRTEELEEAKKKL-----AQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATL 1446
Cdd:PTZ00121 1102 EAK---KTETGKAEEARKAEEAKKKAedarkAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1447 DKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFK---------MRNAYEEVVDQLETLRRENKNLQEEISDLT 1517
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKaedakkaeaVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1518 EQIAETGKNLQ---EVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNS 1594
Cdd:PTZ00121 1259 EARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1595 QRAVEAMQSVLDAEIRSRNDALRLKKKMEGD--LNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLK 1672
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1673 E-----QLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDS-------SDRVQLLHSQNTSLINTKKKLE----- 1735
Cdd:PTZ00121 1419 KadeakKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaeeakkADEAKKKAEEAKKADEAKKKAEeakkk 1498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1736 ADLAQCQAEVENSIQESRNAEEKAK---------KAITDAAMMAEELKKEQDTSAhLERMKKNLEQTVKDLQHRLDEAEQ 1806
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKadeakkaeeAKKADEAKKAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEEDKN 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1807 LALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTyQAEEDRKNILRLQDLVDKLQAKVKSYKRQA 1886
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 124486959 1887 EEAE---EQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDV 1931
Cdd:PTZ00121 1657 EENKikaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1281-1908 |
2.17e-14 |
|
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: 79.00 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1281 KARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLRE----------Q 1350
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarsaektkK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1351 YEEEQEGK----AELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQ 1426
Cdd:pfam05483 174 YEYEREETrqvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1427 GEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKE-SRSLSTEifkmrnayeevvdqlETLRRE 1505
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlQRSMSTQ---------------KALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1506 NKNLQEEISDLTEqiaETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKdE 1585
Cdd:pfam05483 319 LQIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-E 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1586 EIEQIKRNSQRAVEAMQSVLDAEIRsrndalrlkkkmegdlnemeiqLSHANRQVAETQKHLrtvQGQLKDSQLHLDDAQ 1665
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEK----------------------LLDEKKQFEKIAEEL---KGKEQELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1666 RSNEDLKEQLAIVERRNGLLQEELEEMKVALEQtertRRLSEQELLDSSDRVQL----LHSQNTSLINTKKKLEADLAQC 1741
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAHCDKLLLenkeLTQEASDMTLELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1742 QAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQD-TSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGG--KKQIQK 1818
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNnlKKQIEN 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1819 LEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKnilRLQDLVDKLQAKVKSYKRQAE---EAEEQANT 1895
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISEEkllEEVEKAKA 682
|
650
....*....|...
gi 124486959 1896 QLSRCRRVQHELE 1908
Cdd:pfam05483 683 IADEAVKLQKEID 695
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
861-1606 |
2.20e-14 |
|
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: 79.39 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 861 ERAKEDLARSEARRKELeekmvsllQEKNDLQLQVQSETENLMDAEERCEGLIK-SKIQLEAKVKELNERLEEEEEMNSE 939
Cdd:pfam15921 121 EMQMERDAMADIRRRES--------QSQEDLRNQLQNTVHELEAAKCLKEDMLEdSNTQIEQLRKMMLSHEGVLQEIRSI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 940 LVakkrNLEDkcSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDL-QVEE 1018
Cdd:pfam15921 193 LV----DFEE--ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLlQQHQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1019 DKVNGLI-KINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENdtqqleeklkkkefEMSQLQTR 1097
Cdd:pfam15921 267 DRIEQLIsEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLES--------------TVSQLRSE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1098 IDDEQVLslqLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKK---RES- 1173
Cdd:pfam15921 333 LREAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlwdRDTg 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1174 ---EFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEK----------EKSELKMEIDDMASNIE 1240
Cdd:pfam15921 410 nsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssltaqlesTKEMLRKVVEELTAKKM 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1241 TVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIH--DLNMQKAR-LQTQNGELSHQVEEKESLVSQLT---KSKQALTQ 1314
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvDLKLQELQhLKNEGDHLRNVQTECEALKLQMAekdKVIEILRQ 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1315 QLEELKRQLEEETKAKNAL---AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELE 1391
Cdd:pfam15921 570 QIENMTQLVGQHGRTAGAMqveKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1392 EAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQgevddlmldlerantacatldKKQRNFDKVLAEWKQKLDESQAEL 1471
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFR---------------------NKSEEMETTTNKLKMQLKSAQSEL 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1472 EAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEV 1551
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM 788
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1552 EGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVE-AMQSVLD 1606
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRlKLQHTLD 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1376-1937 |
2.53e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1376 RTKYETDAIQRTEELE----EAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQgEVDDLMLDLERANTACATLDKKQR 1451
Cdd:PRK03918 177 RIERLEKFIKRTENIEelikEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1452 NFDKVLAEWKQKLDESQAELEAAQKESRSLsTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVE 1531
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1532 KTKKQVEQ---EKSDLQAALEEVEGSLEHEEsKILRVQLELSQVKSELdrkvteKDEEIEQIKRNSQRAVEAMQSVLDaE 1608
Cdd:PRK03918 335 EKEERLEElkkKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRL------TGLTPEKLEKELEELEKAKEEIEE-E 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1609 IRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLrtvqgqlkdsqlhlddaqrSNEDLKEQLAIVERRNGLLQEE 1688
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-------------------TEEHRKELLEEYTAELKRIEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1689 LEEMKVALEQTERTRRLSEQELLDSSdRVQLLHSQNTSLINTKKKLEADLAQcqaEVENSIQESRNAEEKAKKAITDAAM 1768
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1769 MAEELKKEQDtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELES------ELDAEQKRGAEALK 1842
Cdd:PRK03918 544 LKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1843 GAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAK--VKSYKRQAEEAEEQAntqlSRCRRVQHELEEAEERADIAESQ 1920
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELS----RELAGLRAELEELEKRREEIKKT 695
|
570
....*....|....*..
gi 124486959 1921 VNKLRAKSRDVGGQKME 1937
Cdd:PRK03918 696 LEKLKEELEEREKAKKE 712
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
991-1938 |
5.63e-14 |
|
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: 78.16 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 991 ETISKLTKEKKSLQEAHQQTLDDLQVEEDKVnglIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEgDLKMSQESI 1070
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKA---CEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK-EIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1071 MDLENDtqqleeklkkkefeMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEH--TVRAKiEKQRSDLARELE 1148
Cdd:TIGR00606 265 MKLDNE--------------IKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqrTVREK-ERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1149 EISERLEEASgatsaqiemNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELgeqiDNLQRVKQKLEKEKSEL 1228
Cdd:TIGR00606 330 KLNKERRLLN---------QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL----DGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1229 KMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKakdDQQTQLIHDLNMQKARLQTQNGELSHQVEEKeslvsqltks 1308
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR---DEKKGLGRTIELKKEILEKKQEELKFVIKEL---------- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1309 kQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEeeQEGKAELQRALSKANSEVAQWRTKYETdaiqRTE 1388
Cdd:TIGR00606 464 -QQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSL--QNEKADLDRKLRKLDQEMEQLNHHTTT----RTQ 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1389 ELEEAKKKLAQRLQEAEENTEASNSKCA---------SLEKTKQRLQGEVDDLMLDLERANTACATLDKKQ---RNFDKV 1456
Cdd:TIGR00606 537 MEMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELES 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1457 LAEWKQKLDESQAELEAAQKESRSLSteifKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQ 1536
Cdd:TIGR00606 617 KEEQLSSYEDKLFDVCGSQDEESDLE----RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1537 VEQEKSDLQaaleevegsleheeSKILRVQLELSQVKSELDRKVTEKDEEIEQikrnsqraVEAMQSVLD------AEIR 1610
Cdd:TIGR00606 693 LQEFISDLQ--------------SKLRLAPDKLKSTESELKKKEKRRDEMLGL--------APGRQSIIDlkekeiPELR 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1611 SRNDAL-RLKKKMEGDLNEMEIQLSHANRQVaETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLA------IVERRNG 1683
Cdd:TIGR00606 751 NKLQKVnRDIQRLKNDIEEQETLLGTIMPEE-ESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrTVQQVNQ 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1684 LLQEELEEMKVALEQTERTRRLSEqellDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEkAKKAI 1763
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIELNRKLIQ----DQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS-LIREI 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1764 TDaammaeelKKEQDTSahLERMKKNLEQTVKDLQHRLDEAEQLA---LKGGKKQIQKLEARVRELESELdaeqKRGAEA 1840
Cdd:TIGR00606 905 KD--------AKEQDSP--LETFLEKDQQEKEELISSKETSNKKAqdkVNDIKEKVKNIHGYMKDIENKI----QDGKDD 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1841 LKgaHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQaeeaEEQANTQLSRcRRVQHELEEAEERADIAESQ 1920
Cdd:TIGR00606 971 YL--KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ----ERWLQDNLTL-RKRENELKEVEEELKQHLKE 1043
|
970
....*....|....*...
gi 124486959 1921 VNKLRAKSRDVGGQKMEE 1938
Cdd:TIGR00606 1044 MGQMQVLQMKQEHQKLEE 1061
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1409 |
8.90e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 845 KSAEAEKEMATMKEDFERAK--EDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAK 922
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 VKELNERleeeeemnSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETiSKLTKEKKS 1002
Cdd:PTZ00121 1304 ADEAKKK--------AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1003 LQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKK---LRADLERVKRKLEgdLKMSQESIMDLENDTQQ 1079
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKADE--AKKKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1080 LEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHtvRAKIEKQRSDLARELEEISE-----RL 1154
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK--KAAEAKKKADEAKKAEEAKKadeakKA 1530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1155 EEASGATSAQIEMNKKRESEFQKLR--RDLEEATLQHEATAATLRKKHADTVAELGEQIDNlQRVKQKLEKEKSELKMEI 1232
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKA 1609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1233 DDMASNIEtvSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQAL 1312
Cdd:PTZ00121 1610 EEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1313 TQQLEELKRQLEEETKAKNalahalqssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL-- 1390
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEE---------------LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkk 1751
|
570 580
....*....|....*....|
gi 124486959 1391 -EEAKKKLAQRLQEAEENTE 1409
Cdd:PTZ00121 1752 dEEEKKKIAHLKKEEEKKAE 1771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1315-1929 |
1.86e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1315 QLEELKRQLEE-ETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAElqrALSKANSEVAQWRTKYEtdaiqRTEELEEA 1393
Cdd:PRK02224 188 SLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE---TRDEADEVLEEHEERRE-----ELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1394 KKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEA 1473
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1474 AQKESrslsteifkmrnayeevvdqlETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEG 1553
Cdd:PRK02224 340 HNEEA---------------------ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1554 SLEHEESKILRVQLELSQVKSELDRkVTEKDEEIEQIKRNSQRAVEAMQSVLDAeirsrndalrlkkkmeGDLNEMEiql 1633
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDE-LREREAELEATLRTARERVEEAEALLEA----------------GKCPECG--- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1634 shanrQVAETQKHLRTvqgqlkdsqlhLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQelldS 1713
Cdd:PRK02224 459 -----QPVEGSPHVET-----------IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER----R 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1714 SDRVQLLHSQNTSLINTKKKLEaDLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLERMKK---- 1788
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAE-ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElKERIESLERirtl 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1789 -----NLEQTVKDLQHRLdeaEQLALKGG--KKQIQKLEARVRELESELDAEQKRGAEALKG-AHKYERKVKEMTYQAEE 1860
Cdd:PRK02224 598 laaiaDAEDEIERLREKR---EALAELNDerRERLAEKRERKRELEAEFDEARIEEAREDKErAEEYLEQVEEKLDELRE 674
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1861 DRknilrlqdlvDKLQAKVKSYKRQAEEAE---EQANTQLSRCRRVQHELEEAEEradiAESQVNKLRAKSR 1929
Cdd:PRK02224 675 ER----------DDLQAEIGAVENELEELEelrERREALENRVEALEALYDEAEE----LESMYGDLRAELR 732
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1107-1611 |
1.98e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1107 QLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIE-----MNKKRE------SEF 1175
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1176 QKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERmcrs 1255
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA---- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1256 vedqfNEIKAKDdqqtQLIHDLNMQKARLQTQnGELShQVEEKES-----------------LVSQL-----------TK 1307
Cdd:COG4913 441 -----RLLALRD----ALAEALGLDEAELPFV-GELI-EVRPEEErwrgaiervlggfaltlLVPPEhyaaalrwvnrLH 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1308 SKQAL-TQQLEELKRQLEEETKAKNALAHALQSSRHDC-DLLREQYEEEQ-----EGKAELQRA--------LSKANSEV 1372
Cdd:COG4913 510 LRGRLvYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1373 AQ------WRTKYET--DAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQG--EVDDLMLDLERANTA 1442
Cdd:COG4913 590 HEkddrrrIRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAERE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1443 CATLDKKQRNFDK---VLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRR-----ENKNLQEEIS 1514
Cdd:COG4913 670 IAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaEDLARLELRA 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1515 DLTEQIAETG--KNLQEV-EKTKKQVEQEKSDLQAALEEVEGSLE------HEESKILRVQLE-LSQVKSELDRKVTE-- 1582
Cdd:COG4913 750 LLEERFAAALgdAVERELrENLEERIDALRARLNRAEEELERAMRafnrewPAETADLDADLEsLPEYLALLDRLEEDgl 829
|
570 580 590
....*....|....*....|....*....|..
gi 124486959 1583 ---KDEEIEQIKRNSQRAVEAMQSVLDAEIRS 1611
Cdd:COG4913 830 peyEERFKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1388-1922 |
2.74e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1388 EELEEAKKKLAQrLQEAEENTEasnsKCASLEKTKQRLQGEVDdlMLDLERANTACATLDKKQRNFDKVLAEWKQKLDES 1467
Cdd:COG4913 242 EALEDAREQIEL-LEPIRELAE----RYAAARERLAELEYLRA--ALRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 QAELEAAQKESRSLsteifkmRNAYEEV-VDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTkkqVEQEKSDLQA 1546
Cdd:COG4913 315 EARLDALREELDEL-------EAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLP---LPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1547 ALEEVEGSLE--HEESKILRVQL-ELSQVKSELDRKVTEKDEEIEQIKRNsqraveamQSVLDAEirsrndALRLKKKME 1623
Cdd:COG4913 385 LRAEAAALLEalEEELEALEEALaEAEAALRDLRRELRELEAEIASLERR--------KSNIPAR------LLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1624 GDLNEMEIQLSHANR--QVAETQKHLRT-VQGQLKDSQLHL--DDaqrsnEDLKEQLAIVERRNglLQEELeemkvaleQ 1698
Cdd:COG4913 451 EALGLDEAELPFVGEliEVRPEEERWRGaIERVLGGFALTLlvPP-----EHYAAALRWVNRLH--LRGRL--------V 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1699 TERTRRLSEQELLDSSDRVQLLHsqntslintkkKLEADLAQCQAEVENSIQES------RNAEE--KAKKAITDAAMma 1770
Cdd:COG4913 516 YERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEElrRHPRAITRAGQ-- 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1771 eelkkeqdtsahlerMKKNLEQTVKDLQHRLDE--------AEQLALKggKKQIQKLEARVRELESELDAEQKRGAEALK 1842
Cdd:COG4913 583 ---------------VKGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLEALEAELDALQE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1843 GAHKYERkVKEMTY-------------QAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEE 1909
Cdd:COG4913 646 RREALQR-LAEYSWdeidvasaereiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ 724
|
570
....*....|...
gi 124486959 1910 AEERADIAESQVN 1922
Cdd:COG4913 725 AEEELDELQDRLE 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1290-1938 |
3.05e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1290 ELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQssrhdcDLLREQYEEEQEGKAELQRALSKAN 1369
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE------ELNKKIKDLGEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1370 SEVAQWRtkyetDAIqrtEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKK 1449
Cdd:TIGR02169 301 AEIASLE-----RSI---AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1450 QRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMrnayeevVDQLETLRRENKNLQEEISDLTEQIAETGKNLQE 1529
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL-------QEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1530 VEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKdeeieQIKRNSQRAVEAMQSVLDAEI 1609
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA-----RASEERVRGGRAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1610 RSRNDALRlkkkmegDLNEMEiqlshanrqvAETQKHLRTVQGQLKDSQLHLDDAqrsneDLKEQLAIVERRNGLLQEEL 1689
Cdd:TIGR02169 521 QGVHGTVA-------QLGSVG----------ERYATAIEVAAGNRLNNVVVEDDA-----VAKEAIELLKRRKAGRATFL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1690 EEMKVALEQTErTRRLSEQ-------ELLDSSDR--------------VQLLHSQNTSLINTKK-KLEADLAQCQAEVEN 1747
Cdd:TIGR02169 579 PLNKMRDERRD-LSILSEDgvigfavDLVEFDPKyepafkyvfgdtlvVEDIEAARRLMGKYRMvTLEGELFEKSGAMTG 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1748 SIQESRNAEEKAKKAITDAAMMAEELKKeqdtsahLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELE 1827
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1828 SELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKR------------QAEEAEEQANT 1895
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaELSKLEEEVSR 809
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 124486959 1896 QLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKMEE 1938
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1001-1516 |
3.17e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1001 KSLQEAHQQTLDDL--QVEE-------DKVNGLikiNVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEgDLKMSQESIM 1071
Cdd:PRK02224 179 ERVLSDQRGSLDQLkaQIEEkeekdlhERLNGL---ESELAELDEEIERYEEQREQARETRDEADEVLE-EHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1072 DLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEIS 1151
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1152 ERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKhADTVAELGEQI--------------DNLQRV 1217
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIeelrerfgdapvdlGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1218 KQKLEKEKSELKMEIDDMASNIETVSKSKSNMERM-----C----RSVEDqfNEIKAKDDQQTQLIHDLNMQKARLQTQN 1288
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALleagkCpecgQPVEG--SPHVETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1289 GELSHQVEEKESLVSQ------LTKSKQALTQQLEELKRQLEEET-------KAKNALAHALQSSRHDCDLLREQYEEEQ 1355
Cdd:PRK02224 492 EEVEERLERAEDLVEAedrierLEERREDLEELIAERRETIEEKReraeelrERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1356 EGKAELQRALSKANSEVAQWRTKYETDAiqRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLD 1435
Cdd:PRK02224 572 EEVAELNSKLAELKERIESLERIRTLLA--AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1436 LERANTACAtlDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLStEIFKMRNAYEEVVDQLETLRRENKNLQEEISD 1515
Cdd:PRK02224 650 EAREDKERA--EEYLEQVEEKLDELREERDDLQAEIGAVENELEELE-ELRERREALENRVEALEALYDEAEELESMYGD 726
|
.
gi 124486959 1516 L 1516
Cdd:PRK02224 727 L 727
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
852-1776 |
3.26e-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: 75.39 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 852 EMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDlqlqvqSETENLMDAEERCEGLIKSKIQLEAKVKELNERLE 931
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETE------NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 932 EEEEMNSELVAKKRNLEdkcsslKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEahqqtL 1011
Cdd:pfam02463 219 LELEEEYLLYLDYLKLN------EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE-----E 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1012 DDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKklradlervKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEM 1091
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE---------KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1092 SQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKR 1171
Cdd:pfam02463 359 EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1172 EsEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMER 1251
Cdd:pfam02463 439 I-ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1252 MCRSVEDQFNEIKAKdDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKqaltqqleelkrqleeetKAKN 1331
Cdd:pfam02463 518 DGVGGRIISAHGRLG-DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELP------------------LGAR 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1332 ALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEAS 1411
Cdd:pfam02463 579 KLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGL 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1412 NSKC-----ASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIF 1486
Cdd:pfam02463 659 AEKSevkasLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEEL 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1487 KmRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVegslehEESKILRVQ 1566
Cdd:pfam02463 739 K-LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE------LRALEEELK 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1567 LELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKH 1646
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESK 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1647 LRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTS 1726
Cdd:pfam02463 892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEE 971
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 124486959 1727 LINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKE 1776
Cdd:pfam02463 972 LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1537-1926 |
4.42e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1537 VEQEKSDLQAALEEvegsLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKrnsqraveamqsvLDAEIRSRNDAL 1616
Cdd:TIGR02169 165 VAEFDRKKEKALEE----LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-------------LLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1617 RLKKKmegdlNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQL-AIVERRNGLLQEELEEMKVA 1695
Cdd:TIGR02169 228 LLKEK-----EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1696 LEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAmmaEELKK 1775
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE---EVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1776 EQDTSAHLERMKKNLEqtvkDLQHRLDEaeqlalkggkkqIQKLEARVRELESELDAEQKRGAEALKGAhkyERKVKEMT 1855
Cdd:TIGR02169 380 FAETRDELKDYREKLE----KLKREINE------------LKRELDRLQEELQRLSEELADLNAAIAGI---EAKINELE 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1856 YQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRA 1926
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1566-1932 |
7.17e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1566 QLELSQVKSELDR---KVTEKDEEIEQIKRNSQRAVEAMQsvLDAEIRSRNDALRLKKkmegdlnemeiqLSHANRQVAE 1642
Cdd:COG1196 178 ERKLEATEENLERledILGELERQLEPLERQAEKAERYRE--LKEELKELEAELLLLK------------LRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1643 TQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHS 1722
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1723 QntslintKKKLEADLAQCQAEVENSIQESRNAEEKAKKAitdAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD 1802
Cdd:COG1196 324 E-------LAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1803 EAEQLAlkggkKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSY 1882
Cdd:COG1196 394 AAAELA-----AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 124486959 1883 KRQAEEAEEQANTQLSrcrrvqhELEEAEERADIAESQVNKLRAKSRDVG 1932
Cdd:COG1196 469 LEEAALLEAALAELLE-------ELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1030-1764 |
9.72e-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: 73.85 E-value: 9.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1030 KLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQ------TRIDDEQV 1103
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqshaylTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1104 LSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSdlARELEEISERLEeasgatsaqiEMNKKRESEFQKLrrdle 1183
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAVT----------QIEQQAQRIHTEL----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1184 EATLQHEATAATLRKKHADTVAELGEQidnlQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMcrsveDQFNEI 1263
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-----HTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1264 KAKDDQQTQLIHDLNMQKARLQTQngelshqveekeslVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQssrhd 1343
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQAT--------------IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT----- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1344 cdllrEQYEEEQEGKAELQRALSKANSEVAQWRTKYetdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQ 1423
Cdd:TIGR00618 449 -----CTAQCEKLEKIHLQESAQSLKEREQQLQTKE-----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1424 RL------QGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVD 1497
Cdd:TIGR00618 519 DIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1498 QLETLRRENKNLQEEISDLTEQIAETgKNLQEVEKTKKQVEQEKSDLQAALEEVEGSL--EHEESKILRVQLELSQVKSE 1575
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQPE-QDLQDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1576 LDRKVTEKDEEIEQ---IKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRT--- 1649
Cdd:TIGR00618 678 RQLALQKMQSEKEQltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvlk 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1650 --VQGQLKDSQLHLDDAQRSNEdLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSL 1727
Cdd:TIGR00618 758 arTEAHFNNNEEVTAALQTGAE-LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSR 836
|
730 740 750
....*....|....*....|....*....|....*..
gi 124486959 1728 INTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAIT 1764
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1489-1937 |
1.95e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1489 RNAYEEVVDQLEtlRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEheeskilrvqlE 1568
Cdd:PRK02224 186 RGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------E 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1569 LSQVKSELDrKVTEKDEEIEQIKRNSQRAVEAMQSVLDaEIRSRNDALRlkkkMEGDLNEMEIQLSHANRQVAETQKHlr 1648
Cdd:PRK02224 253 LETLEAEIE-DLRETIAETEREREELAEEVRDLRERLE-ELEEERDDLL----AEAGLDDADAEAVEARREELEDRDE-- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1649 TVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELldssdrvqllhsqntsli 1728
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI------------------ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1729 ntkkkleadlaqcqAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNLEQTVKDLQHRLDEAEQLa 1808
Cdd:PRK02224 387 --------------EELEEEIEELRERFGDAPVDLGNAEDFLEELREERD---ELREREAELEATLRTARERVEEAEAL- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1809 LKGGK---------------------KQIQKLEARVRELESELDAEQKRgAEALKGAHKYERKVKemtyqaeedrknilR 1867
Cdd:PRK02224 449 LEAGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEER-LERAEDLVEAEDRIE--------------R 513
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1868 LQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKME 1937
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1202-1744 |
3.37e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1202 DTVAELGEQIDNLQRVKQKLEKEKSELKM--EIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAkdDQQTQLIHDLNM 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1280 QKARLQTQNGELSHQVEEKESLVSQLTKSKQAL-TQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGK 1358
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1359 AELQRALSKANSEVAQWRtkyetdaiqrtEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLER 1438
Cdd:COG4913 383 AALRAEAAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1439 A--------------------------------NTACATLDKKQRNFDKVLaEW-----------KQKLDESQAELEAAQ 1475
Cdd:COG4913 452 AlgldeaelpfvgelievrpeeerwrgaiervlGGFALTLLVPPEHYAAAL-RWvnrlhlrgrlvYERVRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1476 KESRSLSTEI-FKMRNAYEEV------------VDQLETLRRENKNL-------------------------------QE 1511
Cdd:COG4913 531 LDPDSLAGKLdFKPHPFRAWLeaelgrrfdyvcVDSPEELRRHPRAItragqvkgngtrhekddrrrirsryvlgfdnRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1512 EISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESkilrvQLELSQVKSELDrkvtEKDEEIEQIK 1591
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----EIDVASAEREIA----ELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1592 RNSqraveamqsvldaeirsrndalrlkkkmeGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDL 1671
Cdd:COG4913 682 ASS-----------------------------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1672 KEQL-AIVERRNGLLQEELEEMKVALEQTERTRRLSEQelldssdrvqlLHSQNTSLINTKKKLEADLAQCQAE 1744
Cdd:COG4913 733 QDRLeAAEDLARLELRALLEERFAAALGDAVERELREN-----------LEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1587 |
4.04e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 901 NLMDAEERCEGLIKSKIQLEAKVKELNERLeeeeemnselvAKKRNLEDKcsslkrdiddleltLTKVEKEKHATENKVK 980
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEEL--------------IKEKEKELEEVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 981 NLSEEMTALEETISKLTKEKKSLqEAHQQTLDDLQVEEDKVNGLIKinvKLEQQTDDLEGSLEQEKKLRADLERVKRKLE 1060
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1061 gDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDdeqvlslQLQKKIKELqarteeleeeieaehtvrakiekqr 1140
Cdd:PRK03918 287 -ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN-------GIEERIKEL------------------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1141 SDLARELEEISERLEEasgaTSAQIEMNKKRESEFQKLRRDLEEATlqheataaTLRKKHAD-TVAELGEQIDNLQRVKQ 1219
Cdd:PRK03918 334 EEKEERLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEELE--------RLKKRLTGlTPEKLEKELEELEKAKE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1220 KLEKE-------KSELKMEIDDMASNIETVSKSKSNMERMCRSV-EDQFNEIKAKddqQTQLIHDLNMQKARLQTQNGEL 1291
Cdd:PRK03918 402 EIEEEiskitarIGELKKEIKELKKAIEELKKAKGKCPVCGRELtEEHRKELLEE---YTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1292 SHQVEEKESLV---SQLTKSKQaLTQQLEELKRQLE----EETKAKNalahalqssrhdcdllrEQYEEEQEGKAELQRA 1364
Cdd:PRK03918 479 RKELRELEKVLkkeSELIKLKE-LAEQLKELEEKLKkynlEELEKKA-----------------EEYEKLKEKLIKLKGE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1365 LSKANSEVaqwrtKYETDAIQRTEELEEAKKKLAQRLqeAEENTEASNSKCASLEKTKQRLQgEVDDLMLDLERANTACA 1444
Cdd:PRK03918 541 IKSLKKEL-----EKLEELKKKLAELEKKLDELEEEL--AELLKELEELGFESVEELEERLK-ELEPFYNEYLELKDAEK 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1445 TLDKKQRNFDKVlaewKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEvvDQLETLRRENKNLQEEISDLTEQIAETG 1524
Cdd:PRK03918 613 ELEREEKELKKL----EEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELE 686
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486959 1525 KNLQEVEKTKKQVEQEKSDLQAALEEVEgSLEHEESKILRVQLELSQVKSELDRKVTEKDEEI 1587
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
843-1562 |
5.02e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.54 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 843 LLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQE----KNDLQLQVQSET---ENLMDAEERCEGLIKS 915
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHerkQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 916 KIQLEAKVKELNERLEEEEEMNSEL------VAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKvKNLSEEMTAL 989
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLkqlrarIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE-QQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 990 EETISKLTKEKKSLQEAHQQTLdDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVK---RKLEGDLKMS 1066
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHtlqQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1067 Q--ESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSlQLQKKIKELQARTEELEEEIEAEHTVRAKIE-KQRSDL 1143
Cdd:TIGR00618 396 QslCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQ-QRYAELCAAAITCTAQCEKLEKIHLQESAQSlKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1144 ARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHA--DTVAELGEQIDNLQRVKQKL 1221
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1222 EKEKSELKMEiddMASNIETVSKSKSNMERMCRSVEDQFNEikakddqqTQLIHDLNMQKARLQTQNGELSHqvEEKESL 1301
Cdd:TIGR00618 555 RKQRASLKEQ---MQEIQQSFSILTQCDNRSKEDIPNLQNI--------TVRLQDLTEKLSEAEDMLACEQH--ALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1302 VSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQyeeEQEGKAELQRALSKANSEVAQWRTKYET 1381
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL---PKELLASRQLALQKMQSEKEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1382 DAIQRT--EELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEvddlmLDLERANTACATLDKKQRNFDKV--- 1456
Cdd:TIGR00618 699 LAQCQTllRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE-----LMHQARTVLKARTEAHFNNNEEVtaa 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1457 ------LAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVD-QLETLRRENKNLQEEISDLTEQIAETGKNLQE 1529
Cdd:TIGR00618 774 lqtgaeLSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
730 740 750
....*....|....*....|....*....|...
gi 124486959 1530 VEKTKKQVEQeKSDLQAALEEVEGSLEHEESKI 1562
Cdd:TIGR00618 854 YEECSKQLAQ-LTQEQAKIIQLSDKLNGINQIK 885
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
845-1418 |
9.09e-12 |
|
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: 70.59 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 845 KSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEG----LIKSKIQLE 920
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTlqaqLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 921 AKVKELNERLEEEEEMNSELVAKKRNLEDKCSS----------LKRDIDDLELTLTKVEKEKHATENKVKNLsEEMTALE 990
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAydklektknrLQQELDDLLVDLDHQRQLVSNLEKKQKKF-DQMLAEE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 991 ETISKLTKEKKSLQEAHQQTLD--------DLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGD 1062
Cdd:pfam01576 614 KAISARYAEERDRAEAEAREKEtralslarALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQ 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1063 LKMSQESIMDLENDTQQLEEKLKKKEFEMS--------QLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRA 1134
Cdd:pfam01576 694 VEEMKTQLEELEDELQATEDAKLRLEVNMQalkaqferDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKK 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1135 KIEKQRSDLARELEEISERLEEAsgatsaqIEMNKKRESEFQKLRRDLEEATLQHEATAATLR---KKHADTVAE---LG 1208
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEA-------VKQLKKLQAQMKDLQRELEEARASRDEILAQSKeseKKLKNLEAEllqLQ 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1209 EQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNME----RMCRSVEDQFNEIKAKDDQQ---TQLIHDLNMQ- 1280
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEariaQLEEELEEEQSNTELLNDRLrksTLQVEQLTTEl 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1281 -------------KARLQTQNGELSHQVEEKESLV-SQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDL 1346
Cdd:pfam01576 927 aaerstsqksesaRQQLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKE 1006
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1347 LREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASL 1418
Cdd:pfam01576 1007 VLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
851-1599 |
9.57e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 851 KEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNERL 930
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 931 EEEEEMNSELVAKKRNLEDkcsslKRDIDDLEltltKVEKEKHAtenkvknlsEEMTALEETISKLTKEKKSLQEAHQQT 1010
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEE-----ERKAEEAR----KAEDAKKA---------EAVKKAEEAKKDAEEAKKAEEERNNEE 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1011 LDDLQVEEDKVNGLIKINVKLEQ--QTDDLEGSLEQEKKLRADLERVKRKLEgDLKMSQESIMDLENDTQQLEEKLKKKE 1088
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1089 FEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIE--KQRSDLARELEEISERLEEasgaTSAQIE 1166
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEE----DKKKAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1167 MNKKRESEFQK---LRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLE--------KEKSELKMEIDDM 1235
Cdd:PTZ00121 1409 ELKKAAAAKKKadeAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEA 1488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1236 ASNIEtvsKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQ 1315
Cdd:PTZ00121 1489 KKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1316 LEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdaiqrtEELEEAKK 1395
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-----------KAEEEKKK 1634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1396 KLAQRLQEAEENTEASNSKCAslektkqrlqgevddlmldlERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQ 1475
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKA--------------------EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1476 KESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTkkqvEQEKSDLQAALEEVEGSL 1555
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKA 1770
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 124486959 1556 EHEESKILRVQLElsQVKSELDRKVTEKDEEIEQIKRNSQRAVE 1599
Cdd:PTZ00121 1771 EEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
944-1608 |
1.03e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 944 KRNLEDKCSSLKRDidDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAH--QQTLDDLQVEEDKV 1021
Cdd:TIGR00618 195 KAELLTLRSQLLTL--CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1022 NGLIKI----NVKLEQQTDDLEGSLEQEK--KLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQ 1095
Cdd:TIGR00618 273 RAQEAVleetQERINRARKAAPLAAHIKAvtQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1096 TRI---------------------DDEQVLSLQLQKKIKE--LQARTEELEEEIEAEHTVRAKIEKQRS---DLARELEE 1149
Cdd:TIGR00618 353 QEIhirdahevatsireiscqqhtLTQHIHTLQQQKTTLTqkLQSLCKELDILQREQATIDTRTSAFRDlqgQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1150 IS---ERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATlQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKS 1226
Cdd:TIGR00618 433 QElqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1227 ELKMEIDDmasnietVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNmQKARLQTQNGELSHQVEEKESLVSQLT 1306
Cdd:TIGR00618 512 HPNPARQD-------IDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQQSFSILTQCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1307 KSKQALTQQLEELKRQLEEETKAKNALAhalqssrhdcDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQR 1386
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLA----------CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQL 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1387 TEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDdlmlDLERANTACATLDKKQRNFDKVLAEWKQKLDE 1466
Cdd:TIGR00618 654 TLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE----MLAQCQTLLRELETHIEEYDREFNEIENASSS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1467 SQAELEA-------AQKESRSLSTEIFKMR-NAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVE 1538
Cdd:TIGR00618 730 LGSDLAAredalnqSLKELMHQARTVLKARtEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1539 QE-KSDLQAALEEVEGSLEHEESKILRVQlELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAE 1608
Cdd:TIGR00618 810 QEiPSDEDILNLQCETLVQEEEQFLSRLE-EKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1457-1891 |
1.27e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1457 LAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNA--YEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTK 1534
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1535 KQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQsvlDAEIRSRND 1614
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE---AAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1615 ALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKV 1694
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1695 ALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINT------KKKLEADLAQCQA----EVENSIQESRNAEEKAKKAIT 1764
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqleelEQEIAALLAEAGVedeeELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1765 DAAMMAEELKKEQDTSAHLErmKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELESELDAEQKRgaealkga 1844
Cdd:COG4717 407 LEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEE-ELEELREELAELEAELEQLEEDGELAELL-------- 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 124486959 1845 HKYERKVKEMTYQAEEDRKNILrLQDLVDKLQAKVKSYKRQA--EEAEE 1891
Cdd:COG4717 476 QELEELKAELRELAEEWAALKL-ALELLEEAREEYREERLPPvlERASE 523
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
838-1264 |
1.61e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 838 FKIKPLLKSAEAEKEMATMKED---FERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQsETENLMDAEERCEGL-- 912
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLkk 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 913 ---IKSKIQLEAKVKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELT----------LTKVEKEKHATE--N 977
Cdd:PRK03918 380 rltGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEEHRKELLEEytA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 978 KVKNLSEEMTALEETISKLTKEKKSLQEA---------HQQTLDDLQVEEDKVNgliKINV-KLEQQTDDLEGSLEQEKK 1047
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLK---KYNLeELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1048 LRADLERVKRKLegdlkmsqESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSL-QLQKKIKELQARTEELEEEI 1126
Cdd:PRK03918 537 LKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1127 EAEHTVRAKiEKQRSDLARELEEISERLEEasgaTSAQIEMNKKRESEFQKLRRDLEEATLQHEATaaTLRKKHADTVAE 1206
Cdd:PRK03918 609 DAEKELERE-EKELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAE 681
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1207 LGEQIDNLQRVKQKLEKEKSELKmEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIK 1264
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1385-1832 |
2.41e-11 |
|
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: 68.56 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1385 QRTEELE-------EAKKKLAQ---RLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFD 1454
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1455 KVLAEWKQKLDEsqaeLEAAQKESRSLSTEIFKMRNAYEEVVD---QLET----------LRRENKNLQEEISDLTEQIA 1521
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESSDKVKKleaTVETykkkledlgdLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1522 ETGKNLQEVEKTKKQVEQEKSDLQaaleEVEGSLEHEESKILRVQLE-------LSQVKSELDRKVTEKD---EEIEQIK 1591
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEykkleekLEALQKEKERLIIERDtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1592 RNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHlrTVQGQLKDSQLHLDDAQRSNEDL 1671
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1672 KEQLAIVERRNGLLQEELEEMKVALeqtertrrlseqelldssdrvQLLHSQNTSLINTKKKLEADLAQCQaEVENSIQE 1751
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEKLH-EAQSELQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1752 SRNA-EEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLEQ---TVKDLQHRLDEAEQLALKGGKKQIQKLEAR 1822
Cdd:pfam05622 382 KKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKDKK 461
|
490
....*....|
gi 124486959 1823 VRELESELDA 1832
Cdd:pfam05622 462 IEHLERDFEK 471
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1681 |
2.65e-11 |
|
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: 67.48 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1462 QKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEK 1541
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1542 SDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVtekdEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKK 1621
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1622 MEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERR 1681
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
856-1851 |
2.76e-11 |
|
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: 69.31 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 856 MKEDFERAKEDLARSEARRKELEEKMVSLLQEK---NDLQLQVQSETENLMDAEErcegLIKSKIQLEAKVKELNERLEE 932
Cdd:TIGR01612 563 IKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIiyiNKLKLELKEKIKNISDKNE----YIKKAIDLKKIIENNNAYIDE 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 933 EEEMNSELVAKKRNLEDKC-SSLKR--------DIDDLELTLTKVEKEkhateNKVKNlSEEMTALEETISKLTKEKKSL 1003
Cdd:TIGR01612 639 LAKISPYQVPEHLKNKDKIySTIKSelskiyedDIDALYNELSSIVKE-----NAIDN-TEDKAKLDDLKSKIDKEYDKI 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1004 QEAHQQTLD-DLQVEEDKVNGLIKINVkleqqtddlegslEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEE 1082
Cdd:TIGR01612 713 QNMETATVElHLSNIENKKNELLDIIV-------------EIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKD 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1083 KLKKKEFEMSQLQTRIDDEQVLSlqlqkKIKELQArteeleeeieaehtvrakieKQRSDLARE-LEEISERLEEASGAT 1161
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINID-----NIKDEDA--------------------KQNYDKSKEyIKTISIKEDEIFKII 834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1162 SAQIEMNKK---RESEFQKLRRDLEEATLQHEATAATLRKKHADTVAElgeqiDNLQRVKQKLEKEKS---ELKMEIDDM 1235
Cdd:TIGR01612 835 NEMKFMKDDflnKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD-----DKLNDYEKKFNDSKSlinEINKSIEEE 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1236 ASNIETVSKSKSNMeRMCRSVEDQfneIKAKDDQQTQLIHDLNMQKARLQTQNG-ELSHQVEEKESLVSQLTKSKQALTQ 1314
Cdd:TIGR01612 910 YQNINTLKKVDEYI-KICENTKES---IEKFHNKQNILKEILNKNIDTIKESNLiEKSYKDKFDNTLIDKINELDKAFKD 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1315 -QLEELKRQLEEETKAKNALAHALQSSRHDcdLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEA 1393
Cdd:TIGR01612 986 aSLNDYEAKNNELIKYFNDLKANLGKNKEN--MLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKE 1063
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1394 KKKLAQRLQEaeENTEASNSKCASLEKTKQRLQG-EVDDLMldlERANTACATLDKKQRNFDKVLaewKQKLDESQAELE 1472
Cdd:TIGR01612 1064 IGKNIELLNK--EILEEAEINITNFNEIKEKLKHyNFDDFG---KEENIKYADEINKIKDDIKNL---DQKIDHHIKALE 1135
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1473 AAQKESRSLSTEIFKMRNAYEEVVDQleTLRREN-KNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDlQAALEEV 1551
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDLEDVADK--AISNDDpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEV 1212
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1552 EGsleheeskilrvqLELSQVKSeLDRKVTEKdeeIEQIKRNSQRAVEAMQSVLDaeirsrnDALRLKKKMEGDLNEMEI 1631
Cdd:TIGR01612 1213 KG-------------INLSYGKN-LGKLFLEK---IDEEKKKSEHMIKAMEAYIE-------DLDEIKEKSPEIENEMGI 1268
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1632 QLshanrqvaETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEqlaIVERRNGLLQEELEEMKVALEQTERTRRLSEQELL 1711
Cdd:TIGR01612 1269 EM--------DIKAEMETFNISHDDDKDHHIISKKHDENISD---IREKSLKIIEDFSEESDINDIKKELQKNLLDAQKH 1337
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1712 DSSdrVQLLHSQNTSLINTKKkleadLAQCQaEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLE 1791
Cdd:TIGR01612 1338 NSD--INLYLNEIANIYNILK-----LNKIK-KIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIE 1409
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1792 QTVKDlqhrldeaeqlalkggkKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKV 1851
Cdd:TIGR01612 1410 STLDD-----------------KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENV 1452
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1386-1938 |
2.97e-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: 69.05 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1386 RTEELEEAKkklAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNfdkvLAEWKQKLD 1465
Cdd:pfam01576 2 RQEEEMQAK---EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRAR----LAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1466 ESQAELEAAQKESrslsteifkmrnayEEVVDQLETlrrENKNLQEEISDLTEQiaetgknLQEVEKTKKQVEQEKSDLQ 1545
Cdd:pfam01576 75 EILHELESRLEEE--------------EERSQQLQN---EKKKMQQHIQDLEEQ-------LDEEEAARQKLQLEKVTTE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1546 AALEEVEGS---LEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIK--RNSQRAVEA-MQSVLDAEIRSRNDALRLK 1619
Cdd:pfam01576 131 AKIKKLEEDillLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSklKNKHEAMISdLEERLKKEEKGRQELEKAK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1620 KKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQT 1699
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1700 ERTRRLSEQELldSSDRVQLLHSQNTSliNTKKKLEAdlaQCQAEVENsiqesrnaeekAKKAITDAAMMAEelkkeqdt 1779
Cdd:pfam01576 291 EKQRRDLGEEL--EALKTELEDTLDTT--AAQQELRS---KREQEVTE-----------LKKALEEETRSHE-------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1780 sAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEmtyqae 1859
Cdd:pfam01576 345 -AQLQEMRQKHTQALEELTEQLEQAKR-NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE------ 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1860 edrknilrlqdlvdkLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKMEE 1938
Cdd:pfam01576 417 ---------------LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1215-1895 |
3.75e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.51 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1215 QRVKQKLEKEKSELK---MEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNmqkARLQTQNGEL 1291
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN---SDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1292 SHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAhalqSSRHDCDLLREQYEEEQEGKAELQRALSKANSE 1371
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1372 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQR 1451
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1452 NFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEvvDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVE 1531
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1532 KTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEamqsvLDAEIRs 1611
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-----KDEQIK- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1612 rndalrlKKKMEGDLNEMEIQLSHAnrQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEE 1691
Cdd:TIGR04523 416 -------KLQQEKELLEKEIERLKE--TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1692 MKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQaevensiQESRNAEEKAKKaitdaamMAE 1771
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE-------SKISDLEDELNK-------DDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1772 ELKKEQdtsahLERMKKNLEQTVKDLQHrldeaeqlalkggkkQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKV 1851
Cdd:TIGR04523 553 ELKKEN-----LEKEIDEKNKEIEELKQ---------------TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 124486959 1852 KEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANT 1895
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1204-1746 |
4.66e-11 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 67.84 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1204 VAELGEQIDNLQRVKQKLEKE----KSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLihdlnm 1279
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEhkraRIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAEL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1280 qkARLQTQNGE-LSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGK 1358
Cdd:pfam05557 78 --NRLKKKYLEaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1359 AELQRALSKAnsevaqwrtkyeTDAIQRTEELEeakKKLAQRLQEAEEnTEASNSKCAS---LEKTKQRLQGEVDDLmld 1435
Cdd:pfam05557 156 QNLEKQQSSL------------AEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHL--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1436 leRANTACATLDKKQrnfdkvLAEWKQKLD---ESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQL---ETLRRENKNL 1509
Cdd:pfam05557 217 --NENIENKLLLKEE------VEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1510 QEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELD--RKVTEKDEEI 1587
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyRAILESYDKE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1588 EQIKRNSQRAVEAMQSVLDaeirsrndalrLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQG--QLKDSQLHLDDAQ 1665
Cdd:pfam05557 369 LTMSNYSPQLLERIEEAED-----------MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERelQALRQQESLADPS 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1666 RSNED---LKEQLAIVERRNGLLQEELEEMKVALEqtertrRLSEQELLDSSDRVQLLHSQNTSLiNTKKKLEADLAQCQ 1742
Cdd:pfam05557 438 YSKEEvdsLRRKLETLELERQRLREQKNELEMELE------RRCLQGDYDPKKTKVLHLSMNPAA-EAYQQRKNQLEKLQ 510
|
....
gi 124486959 1743 AEVE 1746
Cdd:pfam05557 511 AEIE 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1140-1600 |
5.17e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1140 RSDLARELEEISERLEEASGATSaqiEMNKKresEFQKLRRDLEEATLQHEATAATLRKKHadtvaELGEQIDNLQRVKQ 1219
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKP---ELNLK---ELKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1220 KLEKEKSELKMEIDDmASNIETVSKSKSNMErmcrSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVE--- 1296
Cdd:COG4717 113 ELREELEKLEKLLQL-LPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqls 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1297 -EKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQssRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQW 1375
Cdd:COG4717 188 lATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE--QLENELEAAALEERLKEARLLLLIAAALLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1376 RTKYETD-------------AIQRTEELEEAKKKLAQRLQEAEENTEASNSKcaslektKQRLQGEVDDLMLDLERANTA 1442
Cdd:COG4717 266 GSLLSLIltiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELE-------EEELEELLAALGLPPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1443 CATLDKKQRNFDKVLAEWKQklDESQAELEAAQKESRSLSTEI-FKMRNAYEEVVDQLEtlrrENKNLQEEISDLTEQIA 1521
Cdd:COG4717 339 LLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALLAEAgVEDEEELRAALEQAE----EYQELKEELEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1522 ETGKNLQEVEK--TKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSelDRKVTEKDEEIEQIKRNSQRAVE 1599
Cdd:COG4717 413 ELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAE 490
|
.
gi 124486959 1600 A 1600
Cdd:COG4717 491 E 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1135-1516 |
6.35e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1135 KIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHA------DTVAELG 1208
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienvkSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1209 EQIDNLQRVKQKLEKEKSELKMEIDDmaSNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQN 1288
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1289 GELSHQVEEKEslvsqltKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKA 1368
Cdd:TIGR02169 843 IDLKEQIKSIE-------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1369 NsevaqwrtkyetdaiQRTEELEEAKKKLAQRLQEAEENT---EASNSKCASLEKTKQRLQgEVDDLMLDLERANTacat 1445
Cdd:TIGR02169 916 R---------------KRLSELKAKLEALEEELSEIEDPKgedEEIPEEELSLEDVQAELQ-RVEEEIRALEPVNM---- 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1446 ldKKQRNFDKVLAewkqKLDESQAELEAAQKESRSLsteifkmrnayEEVVDQLETLRRE---------NKNLQEEISDL 1516
Cdd:TIGR02169 976 --LAIQEYEEVLK----RLDELKEKRAKLEEERKAI-----------LERIEEYEKKKREvfmeafeaiNENFNEIFAEL 1038
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
945-1550 |
6.78e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 6.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 945 RNLEDKCSSLKRDIDDLELTLTKVEKEKHATenKVKNLSEEMTALEETISKLTKEKKSLQ---EAHQQTLDDLQVEEDKv 1021
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEarlDALREELDELEAQIRG- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1022 NGLIKINvKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDE 1101
Cdd:COG4913 335 NGGDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1102 QVlslQLQKKIKELQARteeleeeieaehtvRAKIEKQRSDLARELEEISERLEEASGATSAQ-------IEMnKKRESE 1174
Cdd:COG4913 414 LR---DLRRELRELEAE--------------IASLERRKSNIPARLLALRDALAEALGLDEAElpfvgelIEV-RPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1175 FQK--------LRRDL--EEatlQHEATAAT-LRKKHadtvaeLGEQIDnLQRVKQKLEKEKSElKMEIDDMASNIETvs 1243
Cdd:COG4913 476 WRGaiervlggFALTLlvPP---EHYAAALRwVNRLH------LRGRLV-YERVRTGLPDPERP-RLDPDSLAGKLDF-- 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1244 KSKSNMERMCRSVEDQFNEIKAKDDQQTQLiHDLNMQKARLQTQNGEL-------------------SHQVEEKESLVSQ 1304
Cdd:COG4913 543 KPHPFRAWLEAELGRRFDYVCVDSPEELRR-HPRAITRAGQVKGNGTRhekddrrrirsryvlgfdnRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1305 LTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLlrEQYEEEQEGKAELQRALSKANSEVaqwrtkyetdai 1384
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERLDASSDDL------------ 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1385 qrtEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDkkQRNFDKVLAEwkQKL 1464
Cdd:COG4913 688 ---AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAA--ALG 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1465 DESQAELEAAQKESRSLSTEifKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKT----------- 1533
Cdd:COG4913 761 DAVERELRENLEERIDALRA--RLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeerfke 838
|
650
....*....|....*....
gi 124486959 1534 --KKQVEQEKSDLQAALEE 1550
Cdd:COG4913 839 llNENSIEFVADLLSKLRR 857
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1310-1936 |
7.06e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 67.47 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1310 QALTQQLEELKRQLEEetkaknalahaLQSSRHDCDLLREQyEEEQEGKAELQralskansevaqwrtKYETDAIQRTEE 1389
Cdd:pfam07111 59 QALSQQAELISRQLQE-----------LRRLEEEVRLLRET-SLQQKMRLEAQ---------------AMELDALAVAEK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1390 LEEAKkklAQRLQEAEENTEASNSkcaSLEKTKQRLQGEVDDL----MLDLERAN-TACATLDKKQRNFDKVLAEWKQKL 1464
Cdd:pfam07111 112 AGQAE---AEGLRAALAGAEMVRK---NLEEGSQRELEEIQRLhqeqLSSLTQAHeEALSSLTSKAEGLEKSLNSLETKR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1465 DESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRrenKNLQEEI-SDLTEQIAETGKnlQEVEKTKKQVEQEKSD 1543
Cdd:pfam07111 186 AGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLR---KYVGEQVpPEVHSQTWELER--QELLDTMQHLQEDRAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1544 LQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALrlkKKME 1623
Cdd:pfam07111 261 LQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSV---KQLR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1624 GDLNEMEIQLSHANRQVAETQKHLRTVQGQL-------KDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVAL 1696
Cdd:pfam07111 338 GQVAELQEQVTSQSQEQAILQRALQDKAAEVevermsaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1697 EQTERTRRLSEQELLDSSDRVqllhSQNTSLINTKKKLEA---DLAQCQaevensiQESRNAEEKAKKAITDAAMMAEEL 1773
Cdd:pfam07111 418 ETTMTRVEQAVARIPSLSNRL----SYAVRKVHTIKGLMArkvALAQLR-------QESCPPPPPAPPVDADLSLELEQL 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1774 KKEQDtsahleRMKKNLEQTVKDLQHRLDEAEQlalkGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKE 1853
Cdd:pfam07111 487 REERN------RLDAELQLSAHLIQQEVGRARE----QGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1854 MTYQAEEDRKNILRLQDLVDK-LQAKV-----------KSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERadiaESQV 1921
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQaLQEKVaevetrlreqlSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER----NQEL 632
|
650
....*....|....*
gi 124486959 1922 NKLRAKSRDVGGQKM 1936
Cdd:pfam07111 633 RRLQDEARKEEGQRL 647
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
847-1586 |
8.76e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 67.30 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 847 AEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQV---QSETENLMDAEERCEGLIKS----KIQL 919
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKkkaEKELKKEKEEIEELEKELKEleikREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 920 EAKVKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRdidDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKE 999
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK---LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1000 KKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQ---QTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLEND 1076
Cdd:pfam02463 432 LEEEEESIELKQGKLTEEKEELEKQELKLLKDELelkKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1077 TQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEE 1156
Cdd:pfam02463 512 LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1157 ASGAT---------------SAQIEMNKKRESEFQKLRRDLEEATLQ--HEATAATLRKKHADTVAELGEQIDNLQRVKQ 1219
Cdd:pfam02463 592 KSIAVleidpilnlaqldkaTLEADEDDKRAKVVEGILKDTELTKLKesAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1220 KLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKE 1299
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1300 SLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDC----DLLREQYEEEQEGKAELQRALSKANSEVAQW 1375
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkaqeEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1376 RTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRnFDK 1455
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ-KLN 910
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1456 VLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQ-LETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTK 1534
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENnKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1535 KQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEE 1586
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLEL 1042
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
858-1552 |
9.80e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 858 EDFERAKEDLARSearRKELEEKMvsllqekndlqlqvqSETENLMDAEERCEGLIKSKIQLEAKVKELNERLEEEEEMN 937
Cdd:PRK03918 158 DDYENAYKNLGEV---IKEIKRRI---------------ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 938 SELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQVE 1017
Cdd:PRK03918 220 REELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1018 EDKVN---GLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKrKLEGDLKMSQESIMDLENDtQQLEEKLKKKEFEMSQL 1094
Cdd:PRK03918 300 EFYEEyldELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEER-HELYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1095 QTRIDDEQVlsLQLQKKIKELQARTEeleeeieaehTVRAKIEKQRSDLArELEEISERLEEAsgatsaqIEMNKKRESE 1174
Cdd:PRK03918 378 KKRLTGLTP--EKLEKELEELEKAKE----------EIEEEISKITARIG-ELKKEIKELKKA-------IEELKKAKGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1175 FQKLRRDLEEatlqhEATAATLRKKHADtVAELGEQIDNLQRVKQKLEKEKSELKMEIddmaSNIETVSKSKSNMERMcR 1254
Cdd:PRK03918 438 CPVCGRELTE-----EHRKELLEEYTAE-LKRIEKELKEIEEKERKLRKELRELEKVL----KKESELIKLKELAEQL-K 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1255 SVEDQFNEIKAKddqqtqlihdlnmqkarlqtqngELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKaknala 1334
Cdd:PRK03918 507 ELEEKLKKYNLE-----------------------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK------ 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1335 halqssrhdcdllreqyeeeqegKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEakkklaqRLQEAEENTEASNSk 1414
Cdd:PRK03918 558 -----------------------LAELEKKLDELEEELAELLKELEELGFESVEELEE-------RLKELEPFYNEYLE- 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1415 CASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESqaELEAAQKESRSLSTEIFKMRNAYEE 1494
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEE 684
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1495 VVDQLETLRRENKNLQEEISDLTEQIAET---GKNLQEVEKTKKQVEQEKSDL-QAALEEVE 1552
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELeklEKALERVEELREKVKKYKALLkERALSKVG 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1471-1913 |
1.03e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1471 LEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEE 1550
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1551 VEgSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRaVEAMQSVLDAEIRSRndalRLKKKMEGDLNEME 1630
Cdd:PRK03918 240 IE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLS----EFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1631 IQLSHANRQVAETQKhlrtvqgQLKDsqlhLDDAQRSNEDLKEQLAIVERRNGLLQE---ELEEMKVALEQTERTR-RLS 1706
Cdd:PRK03918 314 KRLSRLEEEINGIEE-------RIKE----LEEKEERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKkRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1707 EQELLDSSDRVQLLHSQNTSLINTKKKLEADLaqcqAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERM 1786
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARI----GELKKEIKELKKAIEELKKAKGKCPVCGRELTEE-----HRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1787 KKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELESELDAEQK--RGAEALKGAHKYERKVKEMTYQ-AEEDRK 1863
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEeLEKKAE 525
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 124486959 1864 NILRLQDLVDKLQAKVKSYKRQAEEAEEQANtqlsRCRRVQHELEEAEER 1913
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1312-1701 |
3.23e-10 |
|
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: 64.92 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1312 LTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEqegKAELQRALSKANSEVAQWRtkyetdaiQRTEELE 1391
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQ---RRELESRVAELKEELRQSR--------EKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1392 EAKKKLAQrlqEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDE---SQ 1468
Cdd:pfam07888 101 EKYKELSA---SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1469 AELEAAQKESRSLSTEIFKMRNAYEEVVDQLETlrrenknLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAAL 1548
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1549 EEVEGsleheeskilrvqlelsqVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNE 1628
Cdd:pfam07888 251 RKVEG------------------LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1629 MEIQLSHANRQVAETQKHLRTVQ-------------GQLKDSQL-HLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKV 1694
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQeermereklevelGREKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*..
gi 124486959 1695 ALEQTER 1701
Cdd:pfam07888 393 YIRQLEQ 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1471-1918 |
3.95e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1471 LEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEe 1550
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1551 vegsleheeskilrvQLELSQVKSELDRKVTEKDEEIEQikrnsqraveamqsvLDAEIRSRNDALRLKKKMEGDLNEME 1630
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEE---------------LEERLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1631 IQLSHANRQVAETQKHlrtvqgQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQEL 1710
Cdd:COG4717 177 EELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1711 LDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKK 1788
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1789 NLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRG-----------AEALKGAHKYERKVKEMTYQ 1857
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvedeeelraaLEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486959 1858 AEEDRKNILRLQDLVDK--LQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAE 1918
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
4.17e-10 |
|
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: 56.67 E-value: 4.17e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124486959 33 DSKKACFAVDDKEMYVKGMIQSRENDKVIVKTLDDRELTLNSDQV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1593-1840 |
4.25e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1593 NSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEmeiQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLK 1672
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK---QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1673 EQLAIverrnglLQEELEEMKVALEQTERTRR----LSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQcqaevens 1748
Cdd:COG4942 97 AELEA-------QKEELAELLRALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1749 IQESRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELES 1828
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAA------LEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 124486959 1829 ELDAEQKRGAEA 1840
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1254-1712 |
5.84e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1254 RSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQtqngELSHQVEEKESLVSQLTKSKQA--LTQQLEELKRQLEEETKAKN 1331
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1332 ALAHALQSSRHdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEAS 1411
Cdd:COG4717 150 ELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1412 NSKCASLEKTKQRLQ--GEVDDLMLDLERANTACAtldkkqrnfdkVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMR 1489
Cdd:COG4717 226 EEELEQLENELEAAAleERLKEARLLLLIAAALLA-----------LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1490 NAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGslEHEESKILRVQLEL 1569
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1570 SQVkseLDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKME-GDLNEMEIQLSHANRQVAETQKHLR 1648
Cdd:COG4717 373 AAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaLDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1649 TVQGQLKDSQLHLDDAQRSNE--DLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLD 1712
Cdd:COG4717 450 ELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1617 |
6.73e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1392 EAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAEL 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1472 EAAQKESRSLSTEIFKM-RNAYEEVV----DQLETLRREN--KNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDL 1544
Cdd:COG4942 100 EAQKEELAELLRALYRLgRQPPLALLlspeDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124486959 1545 QAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALR 1617
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1504-1938 |
7.47e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1504 RENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKilrvqlelsqvKSELDRKVTEK 1583
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-----------KAEDARKAEEA 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1584 DEEIEQIKRNSQRAVEAMQSVldAEIRSRNDAlrlkKKMEGDLNEMEIQLSHANRQVAETqkhlRTVQGQLKDSQLHLDD 1663
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAEDARKA--EEARKAEDA----KKAEAARKAEEVRKAEELRKAEDA----RKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1664 AQRSNEDLKEQLAIveRRNGLLQEELEEMKVALEQ--TERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLE----AD 1737
Cdd:PTZ00121 1216 EARKAEDAKKAEAV--KKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekkkAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1738 LAQcQAEVENSIQESRNAEEKAKKAiTDAAMMAEELKKEQDTSAH-LERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQI 1816
Cdd:PTZ00121 1294 EAK-KAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1817 QKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQaKVKSYKRQAEEAE--EQAN 1894
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKkaDEAK 1450
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 124486959 1895 TQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKMEE 1938
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1091-1341 |
1.21e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1091 MSQLQTRIDDEQVLSlQLQKKIKELQARteeleeeieaehtvRAKIEKQRSDLARELEEISERLEeasgATSAQIemnKK 1170
Cdd:COG4942 16 AAQADAAAEAEAELE-QLQQEIAELEKE--------------LAALKKEEKALLKQLAALERRIA----ALARRI---RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1171 RESEFQKLRRDLEEATLQHEAtaatLRKKHADTVAELGEQIDNLQRVKQKlekekSELKM-----EIDDMASNIETVSKS 1245
Cdd:COG4942 74 LEQELAALEAELAELEKEIAE----LRAELEAQKEELAELLRALYRLGRQ-----PPLALllspeDFLDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1246 KSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEE 1325
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*.
gi 124486959 1326 ETKAKNALAHALQSSR 1341
Cdd:COG4942 225 LEALIARLEAEAAAAA 240
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1259-1854 |
1.52e-09 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 63.23 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1259 QFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQV-------EEKESLVSQLTKSKQALTQQLEELKRQLEE-ETKAK 1330
Cdd:pfam07111 71 QLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAvaekagqAEAEGLRAALAGAEMVRKNLEEGSQRELEEiQRLHQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1331 NALAHALQSSRHDCDLLREQYE--EEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE----- 1403
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEglEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKyvgeq 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1404 --AEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEaaqKESRSL 1481
Cdd:pfam07111 231 vpPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFP---KKCRSL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1482 steifkMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAEtgknLQEVEKTKkqvEQEKSDLQAALEEVEGSLEHEESK 1561
Cdd:pfam07111 308 ------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE----LQEQVTSQ---SQEQAILQRALQDKAAEVEVERMS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1562 ILRVQLELSQVKSELDRKVTEKDEEIEQIKrnsqRAVEAMQSVLDaeirsrndalRLKKKMeGDLNEMEIQLSHANRQVA 1641
Cdd:pfam07111 375 AKGLQMELSRAQEARRRQQQQTASAEEQLK----FVVNAMSSTQI----------WLETTM-TRVEQAVARIPSLSNRLS 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1642 ETQKHLRTVQGqLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALE-QTERTRRLSEQELLDSSDRVQLL 1720
Cdd:pfam07111 440 YAVRKVHTIKG-LMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDaELQLSAHLIQQEVGRAREQGEAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1721 HSQntsLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAH-----LERMKKNLEQTVK 1795
Cdd:pfam07111 519 RQQ---LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQalqekVAEVETRLREQLS 595
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1796 DLQHRLDEA--EQLALKGGKKQIQKLEARVRELESELDAEQKRGAEalKGAHKYERKVKEM 1854
Cdd:pfam07111 596 DTKRRLNEArrEQAKAVVSLRQIQHRATQEKERNQELRRLQDEARK--EEGQRLARRVQEL 654
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
961-1925 |
1.64e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 961 LELTLTKVEKEKHATENKVKNLSEEMTALEETISkltkEKKSLQEAHQQTLDDLQVEEDKVNGLIKInvkLEQQTDDLEG 1040
Cdd:PRK04863 263 ITESTNYVAADYMRHANERRVHLEEALELRRELY----TSRRQLAAEQYRLVEMARELAELNEAESD---LEQDYQAASD 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1041 SL----------EQEKKLRADLERVKRKLEGDLKMS---QESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQ 1107
Cdd:PRK04863 336 HLnlvqtalrqqEKIERYQADLEELEERLEEQNEVVeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1108 LQKKIKELQarteeleeeieaehtvRAKIEKQRSDLAreLEEISERLEEAsgATSAQIEMNKKRESEfQKLRrDLEEATL 1187
Cdd:PRK04863 416 YQQAVQALE----------------RAKQLCGLPDLT--ADNAEDWLEEF--QAKEQEATEELLSLE-QKLS-VAQAAHS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1188 QHEATAATLRKKHADTVAElgeqidNLQRVKQKLEKEKSELKMEIDDMA------SNIETVSKSKSNMERMCRSVEDQFN 1261
Cdd:PRK04863 474 QFEQAYQLVRKIAGEVSRS------EAWDVARELLRRLREQRHLAEQLQqlrmrlSELEQRLRQQQRAERLLAEFCKRLG 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1262 -------EIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQA-LTQQ--LEELKRQLEEEtkakn 1331
Cdd:PRK04863 548 knlddedELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwLAAQdaLARLREQSGEE----- 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1332 alahalQSSRHDCDLLREQYeeeqegkAELQRALSKANSEVAQwrtkyetdaiqRTEELEEAKKKLAQRlqEAEENTEas 1411
Cdd:PRK04863 623 ------FEDSQDVTEYMQQL-------LERERELTVERDELAA-----------RKQALDEEIERLSQP--GGSEDPR-- 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1412 nskcasLEKTKQRLQGEV-----DDLML--------------------DLERANTACATLD-----------KKQRNFDK 1455
Cdd:PRK04863 675 ------LNALAERFGGVLlseiyDDVSLedapyfsalygparhaivvpDLSDAAEQLAGLEdcpedlyliegDPDSFDDS 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1456 VLAEWKQKLDESQAELEAAQKESRSLSTEIFKmRNAYEEvvdQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEK--- 1532
Cdd:PRK04863 749 VFSVEELEKAVVVKIADRQWRYSRFPEVPLFG-RAAREK---RIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfig 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1533 TKKQV------EQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDR-----------KVTEKDEEIEQIKRNSQ 1595
Cdd:PRK04863 825 SHLAVafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSAlnrllprlnllADETLADRVEEIREQLD 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1596 RAVEAMQSvldaeIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKD-SQL-----HLDDAQrSNE 1669
Cdd:PRK04863 905 EAEEAKRF-----VQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAlTEVvqrraHFSYED-AAE 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1670 DLKEQLAIVERrnglLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQntslINTKKKLEADLAQcqaEVEN-S 1748
Cdd:PRK04863 979 MLAKNSDLNEK----LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS----YDAKRQMLQELKQ---ELQDlG 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1749 IQESRNAEEKakkaitdAAMMAEELKKEQDTSahleRMKKN-LEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELE 1827
Cdd:PRK04863 1048 VPADSGAEER-------ARARRDELHARLSAN----RSRRNqLEKQLTFCEAEMDNLT--------KKLRKLERDYHEMR 1108
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1828 SELDAEQKRGAEALK--GAHKYERKV--KEMTYQ-AEEDR--------------------KNILRLQDLVDKLQAKVKSY 1882
Cdd:PRK04863 1109 EQVVNAKAGWCAVLRlvKDNGVERRLhrRELAYLsADELRsmsdkalgalrlavadnehlRDVLRLSEDPKRPERKVQFY 1188
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1883 -------KRQAE----------EAEEQANTQLSRCRRvqhELEEAEERADIA-ESQVNKLR 1925
Cdd:PRK04863 1189 iavyqhlRERIRqdiirtddpvEAIEQMEIELSRLTE---ELTSREQKLAISsESVANIIR 1246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1303-1525 |
1.91e-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: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1303 SQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetd 1382
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1383 aiqrtEELEEAKKKLAQRLQEAEENTEASNSKC--------------ASLEKTKQRLQGEVDDLMLDLERANTACATLDK 1448
Cdd:COG4942 97 -----AELEAQKEELAELLRALYRLGRQPPLALllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 1449 KQRNFDKVLAEwkqkLDESQAELEAAQKESRSLSTEIFKMRNAYEEvvdQLETLRRENKNLQEEISDLTEQIAETGK 1525
Cdd:COG4942 172 ERAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1135-1855 |
3.60e-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: 62.05 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1135 KIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHE--------------------ATAA 1194
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKdlikennatrhlcnllketcARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1195 TLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDmaSNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLI 1274
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAEN--ARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1275 HDLNMQKARLQ------TQNGELSHQVEEKESLVS----QLTKSKQALTQQLEELKRQLEEETKAKNALAHALQ-SSRHD 1343
Cdd:pfam05483 247 IQITEKENKMKdltfllEESRDKANQLEEKTKLQDenlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiATKTI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1344 CDLLRE---QYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQ----EAEENTEASNSKCA 1416
Cdd:pfam05483 327 CQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQkkssELEEMTKFKNNKEV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1417 SLEKTKqrlqgevddlmldlerantacatldkkqrnfdKVLAEwKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVV 1496
Cdd:pfam05483 406 ELEELK--------------------------------KILAE-DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEI 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1497 DQLEtlrrenknLQEEISDLTEQiaetgKNLQEVEKTKKQVEQEKsdlqaaLEEVEgsLEHEESKILRVQLELSQVKSEL 1576
Cdd:pfam05483 453 HDLE--------IQLTAIKTSEE-----HYLKEVEDLKTELEKEK------LKNIE--LTAHCDKLLLENKELTQEASDM 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1577 DRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLShanrqvaETQKHLRTVQGQLKD 1656
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-------KSEENARSIEYEVLK 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1657 SQLHLDDAQRSNEDLKEQlaiVERRNGLLQEELEEMKVALEQ-TERTRRLSEQELldSSDRVQLlhsqntSLINTKKKLE 1735
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQ---IENKNKNIEELHQENKALKKKgSAENKQLNAYEI--KVNKLEL------ELASAKQKFE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1736 ADLAQCQAEVE-NSIQESRNAE--EKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNLEQTVKDLQHRLDEaeqLALK 1810
Cdd:pfam05483 654 EIIDNYQKEIEdKKISEEKLLEevEKAKAIADEAVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSE---LGLY 730
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 124486959 1811 GGKKQIQK-----LEARVRELESELDAEQKRGAEALKGAHKYERKVKEMT 1855
Cdd:pfam05483 731 KNKEQEQSsakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1454-1645 |
3.65e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1454 DKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQE---- 1529
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1530 ---------------------------------VEKTKKQVEQEKSDlQAALEEVEGSLEHEESKILRVQLELSQVKSEL 1576
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfldrlsalskiADADADLLEELKAD-KAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1577 DRKVTEKDEEIEQIKRNsQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQK 1645
Cdd:COG3883 174 EAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1360-1793 |
4.06e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1360 ELQRALSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQEAEENTEAsnskcASLEKTKQRLQGEVDDLMLDLE 1437
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1438 RANTACATLDKKQRNfdkvLAEWKQKLDESQAELEAAQKE-SRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDL 1516
Cdd:COG4717 150 ELEERLEELRELEEE----LEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1517 TEQIAETgKNLQEVEKTKKQVEQEKSDLQAA-----LEEVEGSLEHEESKILRVQLELSQV----KSELDRKVTEKDEEI 1587
Cdd:COG4717 226 EEELEQL-ENELEAAALEERLKEARLLLLIAaallaLLGLGGSLLSLILTIAGVLFLVLGLlallFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1588 EQIKRNSQRAVEAMQSvLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRS 1667
Cdd:COG4717 305 EELQALPALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1668 NEDLKEQLAIVERRNGlLQEELEEMKVALEQ--TERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEV 1745
Cdd:COG4717 384 EEELRAALEQAEEYQE-LKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 124486959 1746 EN--SIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQT 1793
Cdd:COG4717 463 EQleEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1107-1541 |
4.93e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1107 QLQKKIKELQARTEELEEEIEaehtvRAKIEKQRSDLARELEEISERLEEASgatsAQIEMNKKRESEFQKLRRDLEEAT 1186
Cdd:COG4717 106 ELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELE----ERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1187 LQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNmERMCRSVEDQFNEIKAK 1266
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLLIA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1267 dDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDL 1346
Cdd:COG4717 256 -AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1347 LREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdaiqrteeLEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQ 1426
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQ-------------LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1427 GEVDDLMLDLERANTACATLDKKQrnfdkVLAEWKQKLDESQAELEAAQKESRSLSTEI--FKMRNAYEEVVDQLETLRR 1504
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEELEELEEELEELREELaeLEAELEQLEEDGELAELLQ 476
|
410 420 430
....*....|....*....|....*....|....*..
gi 124486959 1505 ENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEK 1541
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1193-1552 |
6.72e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.51 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1193 AATLRKKHADTVAELGEQIDNLQRVKQKLEKEK---SELKMEIDDMASNIETVSKSKSNMERMCRSVEDqFNEIKAKDDQ 1269
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSareSDLEQDYQAASDHLNLVQTALRQQEKIERYQED-LEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1270 QTQLIHDLNMQKARLQTQngeLSHQVEEKESLVSQLTKSKQAL-TQQ------------LEELKRQLEE-ETKAKNALAH 1335
Cdd:COG3096 366 QEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLADYQQALdVQQtraiqyqqavqaLEKARALCGLpDLTPENAEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1336 ALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKKLAQ--RLQEAEENT 1408
Cdd:COG3096 443 LAA--------FRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1409 EASNSKCASLEKTKQRLQgevddlmlDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKM 1488
Cdd:COG3096 515 QQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1489 RNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKT-------KKQVEQEKSDLQAALEEVE 1552
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAmqqllerEREATVERDELAARKQALE 657
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1078-1708 |
6.77e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.39 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1078 QQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARteeleeeieaehtvrakiekQRSDLARELEEISERLEEA 1157
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE--------------------LNQLLRTLDDQWKEKRDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1158 SGATSAQIEMNKKRESEFQKLRRDLE-------EATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKM 1230
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGafldadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1231 E-IDDMASNIETVSKSKSNMERMCRSVEDQFneikakDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSK 1309
Cdd:pfam12128 387 QnNRDIAGIKDKLAKIREARDRQLAVAEDDL------QALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1310 QALTQQ---LEELKRQLEEETKAkNALAHALQSSRHDCDLLREQ-----------YEEEQEGKAELQRALSKA------- 1368
Cdd:pfam12128 461 ELLLQLenfDERIERAREEQEAA-NAEVERLQSELRQARKRRDQasealrqasrrLEERQSALDELELQLFPQagtllhf 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1369 -NSEVAQWRTKY----ETDAIQRTE---ELEEAKKK--------------------------LAQRLQEAEENTEASNSK 1414
Cdd:pfam12128 540 lRKEAPDWEQSIgkviSPELLHRTDldpEVWDGSVGgelnlygvkldlkridvpewaaseeeLRERLDKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1415 CASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRslsteifkmrnayEE 1494
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERL-------------NS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1495 VVDQLETLRRENKNLQEEISD-LTEQIAETGKNLQEVEKTKK----QVEQEKSDLQAALEEVEGSLEHEESKILRVQLEL 1569
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDaqlaLLKAAIAARRSGAKAELKALETWYKRDLASLGVD 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1570 SQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQsVLDAEIRSRNDALRLKK-KMEGDLNEMEIQLShanRQVAETQ---K 1645
Cdd:pfam12128 767 PDVIAKLKREIRTLERKIERIAVRRQEVLRYFD-WYQETWLQRRPRLATQLsNIERAISELQQQLA---RLIADTKlrrA 842
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1646 HLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIV--ERRNGLLQEELEEMKVALEQTERTR-RLSEQ 1708
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSKLATLkeDANSEQAQGSIGERLAQLEDLKLKRdYLSES 908
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1052-1592 |
8.49e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1052 LERVKRKLEGDLKMSQESIMD---LENDTQqleeklkKKEFEMSQLQTRIDDEQVLSLQLQKKIKEL----QARTEELEE 1124
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNidyLEEKLK-------SSNLELENIKKQIADDEKSHSITLKEIERLsieyNNAMDDYNN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1125 EIEAEHTVRA----------KIEKQRSDLARELEE---ISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEA 1191
Cdd:PRK01156 237 LKSALNELSSledmknryesEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1192 TAATLRKKHADTVAELGEQIDNLQRVKQKleKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQT 1271
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1272 QLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQY 1351
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1352 EEEQEGKAE----LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ-------------RLQEAEENTEASNSK 1414
Cdd:PRK01156 475 NEKKSRLEEkireIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledikikinELKDKHDKYEEIKNR 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1415 CASLEKTKQRlQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEE 1494
Cdd:PRK01156 555 YKSLKLEDLD-SKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1495 VVDQLETLRRENKNLQEEISDLTEQIAEtgknLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLE---LSQ 1571
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTieiLRT 709
|
570 580
....*....|....*....|.
gi 124486959 1572 VKSELDRKVTEKDEEIEQIKR 1592
Cdd:PRK01156 710 RINELSDRINDINETLESMKK 730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
840-1378 |
2.06e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 840 IKPLLKSAEAE-----KEMATMKEDFERAKEDLARSEARRKELE---EKMVSLLQEKNDLQLQVQSETENLMDAEERCEG 911
Cdd:PRK03918 191 IEELIKEKEKEleevlREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 912 LIKSKIQLEAKVKElnerleeeeemnselVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEE 991
Cdd:PRK03918 271 LKKEIEELEEKVKE---------------LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 992 TISKLTKEKKSLQEAhQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEG-SLEQEKKLRADLERVKRKLEGDLKMSQESI 1070
Cdd:PRK03918 336 KEERLEELKKKLKEL-EKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1071 MDLENDTQQLEEKLKKKEFEMSQLQT---RIDDEQVLSL---------QLQKKIKELQARTEELEEEIEAEHTVRAKIEK 1138
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKCPVcgrELTEEHRKELleeytaelkRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1139 QRS--DLARELEEISERLEEASgatsaqIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHA--DTVAELGEQIDNL 1214
Cdd:PRK03918 495 LIKlkELAEQLKELEEKLKKYN------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1215 QRVKQKLEKEKSELKME-IDDMASNIE----------TVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKAR 1283
Cdd:PRK03918 569 EEELAELLKELEELGFEsVEELEERLKelepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1284 LQTQNGELSHQ-VEEKESLVSQLTKSKQALTQQLEELKRQLEEETKaknalahalqssrhDCDLLREQYEEEQEGKAELQ 1362
Cdd:PRK03918 649 LEELEKKYSEEeYEELREEYLELSRELAGLRAELEELEKRREEIKK--------------TLEKLKEELEEREKAKKELE 714
|
570
....*....|....*.
gi 124486959 1363 RaLSKANSEVAQWRTK 1378
Cdd:PRK03918 715 K-LEKALERVEELREK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1201-1417 |
2.37e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1201 ADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFN----EIKAKDDQQTQLIHD 1276
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1277 LNMQKARLQTQNGEL--SHQVEEKESLVSQ------------LTKSKQALTQQLEELKRQLEEETKAKNALAHALQSsrh 1342
Cdd:COG4942 99 LEAQKEELAELLRALyrLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAE--- 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486959 1343 dcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEENTEASNSKCAS 1417
Cdd:COG4942 176 ----LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
973-1185 |
2.63e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 973 HATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSL----EQEKKL 1048
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1049 RADLERVKRKLEGDL----KMSQESIMDL---ENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEE 1121
Cdd:COG4942 96 RAELEAQKEELAELLralyRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1122 LEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEA 1185
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1398-1613 |
2.72e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1398 AQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDkvlaewkQKLDESQAELEAAQKE 1477
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1478 SRSLSTEIFKMRNAYEEVVDQLETLRREN------------------KNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQ 1539
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1540 EKSDLQAALEEvegsLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRN 1613
Cdd:COG4942 172 ERAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
960-1758 |
3.69e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 960 DLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKS-------LQEA--HQQTLDDLQVEedkvngLIKINVK 1030
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlVQTAlrQQEKIERYQED------LEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1031 LEQQTDDLEGSLEQEKKLRADLERvkrklegdlkmSQESIMDLEndtqqleeklkkkefemSQL---QTRIDDEQVLSLQ 1107
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEA-----------AEEEVDSLK-----------------SQLadyQQALDVQQTRAIQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1108 LQKKIKELQarteeleeeieaehtvRAKIEKQRSDLAreLEEISERLEEASGATSAQIEmnKKRESEfQKLRrDLEEATL 1187
Cdd:COG3096 415 YQQAVQALE----------------KARALCGLPDLT--PENAEDYLAAFRAKEQQATE--EVLELE-QKLS-VADAARR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1188 QHEATAATLRKKHADTVAElgeqiDNLQRVKQKLEkEKSELKMeiddMASNIETVSKSKSNMERMCRS---VEDQFNEIK 1264
Cdd:COG3096 473 QFEKAYELVCKIAGEVERS-----QAWQTARELLR-RYRSQQA----LAQRLQQLRAQLAELEQRLRQqqnAERLLEEFC 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1265 AKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHAlqssrhdC 1344
Cdd:COG3096 543 QRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-------R 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1345 DLLREQYEEEQEGKAELQRALSKansevaqwrtkyETDAIQRTEELEEAKKKLaqrLQEAEENTEASNSKCASLEKTKQR 1424
Cdd:COG3096 616 EQSGEALADSQEVTAAMQQLLER------------EREATVERDELAARKQAL---ESQIERLSQPGGAEDPRLLALAER 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1425 LQGEV-----DDLML--------------------DLERANTACATLDKKQRnfDKVLAEWK-QKLDES---QAELEAA- 1474
Cdd:COG3096 681 LGGVLlseiyDDVTLedapyfsalygparhaivvpDLSAVKEQLAGLEDCPE--DLYLIEGDpDSFDDSvfdAEELEDAv 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1475 --QKESRSLSTEIFKM-----RNAYEEvvdQLETLRRENKnlqeeisDLTEQIAETGKNLQEVEKTKKQVEQ-------- 1539
Cdd:COG3096 759 vvKLSDRQWRYSRFPEvplfgRAAREK---RLEELRAERD-------ELAEQYAKASFDVQKLQRLHQAFSQfvgghlav 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1540 --------EKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELD------------------RKVTEKDEEIEQ---- 1589
Cdd:COG3096 829 afapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpqanlladetlaDRLEELREELDAaqea 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1590 ---IKRNSQRA--VEAMQSVLDAEIRSrNDAL------------RLKKKMEG------------------------DLNE 1628
Cdd:COG3096 909 qafIQQHGKALaqLEPLVAVLQSDPEQ-FEQLqadylqakeqqrRLKQQIFAlsevvqrrphfsyedavgllgensDLNE 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1629 -MEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAiverrngLLQEELEEMKVAL--EQTERTRrl 1705
Cdd:COG3096 988 kLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ-------ELEQELEELGVQAdaEAEERAR-- 1058
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 124486959 1706 seqelldssDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEK 1758
Cdd:COG3096 1059 ---------IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1157-1386 |
4.01e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1157 ASGATSAQIEMNKKRESEFQKLRRDLEEA------TLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKM 1230
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELekelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1231 EIDDMASNIETVSKSKSNMER-MCRSVEDQFNEIKAKDDQQTQLIHDLNMQKA---RLQTQNGELSHQVEEKESLVSQLT 1306
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlapARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1307 KSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQR 1386
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1619-1844 |
4.87e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1619 KKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQ 1698
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1699 TERTRRLSE--------QELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQEsrnaeekakkaitdaammA 1770
Cdd:COG3883 98 SGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE------------------L 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1771 EELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVRELESELDAEQKRGAEALKGA 1844
Cdd:COG3883 160 EALKAE------LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1634 |
6.70e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 856 MKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNERLEEEEE 935
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 936 MNSELVAKKRNLEDKCssLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISkLTKEKkslQEAHQQTLDDLQ 1015
Cdd:TIGR00606 483 AERELSKAEKNSLTET--LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDK---MDKDEQIRKIKS 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1016 VEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQ 1095
Cdd:TIGR00606 557 RHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1096 TRIDDEQvLSLQLQKKIKELQARTEELEEEIEAEHTVRAK------IEKQRSDLARELEEISERLEeaSGATSAQIEMnK 1169
Cdd:TIGR00606 637 EESDLER-LKEEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpVCQRVFQTEAELQEFISDLQ--SKLRLAPDKL-K 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1170 KRESEFQKLRRDLEEATLQHEATAATLRKKHADtVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNM 1249
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKE-IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRsVEDQFNEIKAKDDQQTQLIH--DLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEET 1327
Cdd:TIGR00606 792 TIMER-FQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1328 KAKNALAHALQSSRHdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDaIQRTEEL----EEAKKKLAQRLQE 1403
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQ----FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD-QQEKEELisskETSNKKAQDKVND 945
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1404 AEENTEASNSKCASLEKTKQrlQGEVDDLMLDLERANTACATLD---KKQRNFDKVLAEWKQKLDES------------- 1467
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQ--DGKDDYLKQKETELNTVNAQLEeceKHQEKINEDMRLMRQDIDTQkiqerwlqdnltl 1023
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 --------QAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLqeveKTKKQVEQ 1539
Cdd:TIGR00606 1024 rkrenelkEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL----REPQFRDA 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1540 EKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSEldrkvTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLK 1619
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH-----SMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSA 1174
|
810
....*....|....*
gi 124486959 1620 KKMEGDLNEMEIQLS 1634
Cdd:TIGR00606 1175 SDKRRNYNYRVVMLK 1189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1254-1494 |
7.21e-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: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1254 RSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNAL 1333
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1334 AHALQssrhdcDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKYETDAIQ----RTEELEEAKKKLAQRLQEAEENTE 1409
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1410 ASNSKCASLEKTKQRLQGEvddlmldlerantacatldKKQRNfdKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMR 1489
Cdd:COG4942 175 ELEALLAELEEERAALEAL-------------------KAERQ--KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*
gi 124486959 1490 NAYEE 1494
Cdd:COG4942 234 AEAAA 238
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1043-1834 |
8.88e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1043 EQEKKLRADLErvkrKLEgdlkmSQESIMDLENDTQQLEEKLKkkefemsqLQTRIDDEQVLSLQLQKKIKELQARTeel 1122
Cdd:PRK10246 191 EQHKSARTELE----KLQ-----AQASGVALLTPEQVQSLTAS--------LQVLTDEEKQLLTAQQQQQQSLNWLT--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1123 eeeieaehtvrakiekQRSDLARELEEISERLEEASGA-TSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHA 1201
Cdd:PRK10246 251 ----------------RLDELQQEASRRQQALQQALAAeEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1202 DTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETvsksksnmermcrsvEDQF----NEIKAKDDQQTQLIHDl 1277
Cdd:PRK10246 315 EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAE---------------HDRFrqwnNELAGWRAQFSQQTSD- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1278 nmqKARLQTQNGELSHQVEEKESL-VSQLTKSKQALTQQLEELKRQleeetkaknalahalQSSRHDCDLLREQYEEEQE 1356
Cdd:PRK10246 379 ---REQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHAEQ---------------RPLRQRLVALHGQIVPQQK 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1357 GKAELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEENTEaSNSKCASLEKTKQRLQgevddlmldl 1436
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQ--------RNAALNEMRQRYKEKTQQLADVKTICE-QEARIKDLEAQRAQLQ---------- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1437 erANTACATLDKKQRnfDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDL 1516
Cdd:PRK10246 502 --AGQPCPLCGSTSH--PAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQAL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1517 TEQiaetgknLQEVEKTKKQVEQEKSDLQAALEEVEgslEHEEskilrvQLELSQVKSELDRKVTEKDEEIEQIkrnsQR 1596
Cdd:PRK10246 578 TQQ-------WQAVCASLNITLQPQDDIQPWLDAQE---EHER------QLRLLSQRHELQGQIAAHNQQIIQY----QQ 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1597 AVEAMQSVLDAEIrsrnDALRLKKKMEGDlnemEIQLSHANRQVAETQKHLRTVQGqlkdsqlhlddaqrsneDLKEQLA 1676
Cdd:PRK10246 638 QIEQRQQQLLTAL----AGYALTLPQEDE----EASWLATRQQEAQSWQQRQNELT-----------------ALQNRIQ 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1677 IVERrnglLQEELEEMKVALEQTErtrRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAE 1756
Cdd:PRK10246 693 QLTP----LLETLPQSDDLPHSEE---TVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1757 EKAKKaitdAAMMAEElkkeqdTSAHLERMKKNLEQtvkdlqhRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQ 1834
Cdd:PRK10246 766 QQAFL----AALLDEE------TLTQLEQLKQNLEN-------QRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQ 826
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1325-1827 |
1.06e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 57.40 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1325 EETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE--LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQ 1402
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1403 EAEENTEASNSKCASLEKTKQRLQGEVD-DLMLDLERANTACATLDKKQRNFDKV---------------LAEWKQKLDE 1466
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEegpsieyvklpelnkLHEVESKLKE 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1467 SQAELEAAQKES----RSLSTEIFKMRN-------------AYEEVVDQLETLRRENKNLQEEISDLTEQIAETgKNLQE 1529
Cdd:COG5022 969 TSEEYEDLLKKStilvREGNKANSELKNfkkelaelskqygALQESTKQLKELPVEVAELQSASKIISSESTEL-SILKP 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1530 VEKTKKQVEQEKSDLQAALEEVegSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEqiKRNSQRAVEAMQSVLDAEI 1609
Cdd:COG5022 1048 LQKLKGLLLLENNQLQARYKAL--KLRRENSLLDDKQLYQLESTENLLKTINVKDLEVT--NRNLVKPANVLQFIVAQMI 1123
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1610 RSrndalRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSN-EDLKEQLAIVERRNGLLQEE 1688
Cdd:COG5022 1124 KL-----NLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALsEKRLYQSALYDEKSKLSSSE 1198
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1689 LEEMK---VALEQTERTRRLSEQELLDSSDRVQLLHSQNTSL-----INTKKKLEA-----DLAQCQAEVENSIQESRNA 1755
Cdd:COG5022 1199 VNDLKnelIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLkgfnnLNKKFDTPAsmsneKLLSLLNSIDNLLSSYKLE 1278
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1756 EEKAKKAITD-----AAMMAEELKkeqdTSAHLERMKKNLEqtVKDLQHRLDE-AEQLALKGGKKQIQKLEARVRELE 1827
Cdd:COG5022 1279 EEVLPATINSllqyiNVGLFNALR----TKASSLRWKSATE--VNYNSEELDDwCREFEISDVDEELEELIQAVKVLQ 1350
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1584-1879 |
1.34e-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: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1584 DEEIEQIK--RNSQRAVEAMQ--SVLDAEIRSRNDAL-RLKKKME----GDLNEMEIQLSHANRQVAetQKHLRTVQGQL 1654
Cdd:COG3206 84 ETQIEILKsrPVLERVVDKLNldEDPLGEEASREAAIeRLRKNLTvepvKGSNVIEISYTSPDPELA--AAVANALAEAY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1655 KDSQL--HLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKvaleqtertrrlSEQELLDSSDRVQLLHSQNTSLINTKK 1732
Cdd:COG3206 162 LEQNLelRREEARKALEFLEEQLPELRKELEEAEAALEEFR------------QKNGLVDLSEEAKLLLQQLSELESQLA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1733 KLEADLAQCQAEVeNSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNLEQTVKDLQHRLD 1802
Cdd:COG3206 230 EARAELAEAEARL-AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1803 EAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKY-----ERKVKEMTYQAEEDRKNILRLQDLVDKLQA 1877
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELrrlerEVEVARELYESLLQRLEEARLAEALTVGNV 388
|
..
gi 124486959 1878 KV 1879
Cdd:COG3206 389 RV 390
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1388-1923 |
1.62e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 56.19 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1388 EELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKqrlqGEVDDLMLDLERANTacatlDKKQRNFDKVLAewkqKLDES 1467
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLERAQT-----EEAQAKQDSELA----KLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 QAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAA 1547
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1548 LEEVEGSLE------HE-ESKILRVQLELSQVKSELDRKVTEKDEEIEQIkRNSQRAVEAMQSVLDAeirsrndALRLKK 1620
Cdd:pfam05701 189 LIATKESLEsahaahLEaEEHRIGAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1621 KMEGDLNE-MEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQT 1699
Cdd:pfam05701 261 DLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1700 ERTRRLSeqelldssdrvqllhsqntslintkkklEADLAQCQAEVENSIQESRNAEEKAKKAitdAAMMAEELKKEQDT 1779
Cdd:pfam05701 341 RQREGMA----------------------------SIAVSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1780 SAHLERMKKNLEQTVKDLQHRLDEAEQlalkgGKKQIQKLEARVRELESELDA---EQKRGAEALKGAHKYERKvKEMTY 1856
Cdd:pfam05701 390 AQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKLALAAIKALQESESS-AESTN 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 1857 QAEEDRKNILRLQDLvdklqakvKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNK 1923
Cdd:pfam05701 464 QEDSPRGVTLSLEEY--------YELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1445-1927 |
1.68e-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: 56.57 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1445 TLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETG 1524
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1525 K---NLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAM 1601
Cdd:TIGR04523 201 LllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1602 QSVLDAEirsrNDALRLKKKMEgDLNEMEIQ--LSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVE 1679
Cdd:TIGR04523 281 KKIKELE----KQLNQLKSEIS-DLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1680 RRNGLLQEELEEMKVALEQTERTRRLSEQELLDssdrvqlLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKA 1759
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKN-------LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1760 KKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD-------------EAEQLALKGGKKQIQKLEARVREL 1826
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1827 ESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQ-AKVKSYKRQAEEAEEQANTQLSRcrrvqh 1905
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlEKEIDEKNKEIEELKQTQKSLKK------ 582
|
490 500
....*....|....*....|..
gi 124486959 1906 ELEEAEERADIAESQVNKLRAK 1927
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKE 604
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1250 |
1.83e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 839 KIKPLLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQ 918
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 919 LEAKVKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHatENKVKnlSEEMTALEETISKLTK 998
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 999 EKKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESimdlendtq 1078
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--------- 1749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1079 qleeklkkkefemsqlqtRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEE-A 1157
Cdd:PTZ00121 1750 ------------------KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiI 1811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1158 SGATSAQIEMNKKRESEFQKLR---------RDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEL 1228
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIKevadsknmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
410 420
....*....|....*....|..
gi 124486959 1229 KMEIDDMASNIETVSKSKSNME 1250
Cdd:PTZ00121 1892 KIDKDDIEREIPNNNMAGKNND 1913
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
938-1606 |
2.23e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.39 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 938 SELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQVE 1017
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1018 ----EDKVNGLIKINVKLEQQTDDLEGSLEQEkkLRADLERVKRKLEGDLKMSQESIMDLENDTQQleeKLKKKEFEMSQ 1093
Cdd:pfam12128 356 lenlEERLKALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIKDKLAKIREARDRQLAVAEDDLQA---LESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1094 LQTRIDDEQvlsLQLQKKIKELQARTEELEEEIEAEHTVRAKIEkqRSDLARelEEISERLEEASGATSAQIEMNKKRES 1173
Cdd:pfam12128 431 GKLEFNEEE---YRLKSRLGELKLRLNQATATPELLLQLENFDE--RIERAR--EEQEAANAEVERLQSELRQARKRRDQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1174 EFQKLRRdlEEATLQHEATAatlrkkhadtvaelgeqidnLQRVKQKLEKEKSE----LKMEIDDMASNIETVSKSksnm 1249
Cdd:pfam12128 504 ASEALRQ--ASRRLEERQSA--------------------LDELELQLFPQAGTllhfLRKEAPDWEQSIGKVISP---- 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRSveDQFNEIKAKDDQQTQLIHDLNMQKARLQTQN-GELSHQVEEKESLVSQLTKSKQALTQQLEE----LKRQLE 1324
Cdd:pfam12128 558 ELLHRT--DLDPEVWDGSVGGELNLYGVKLDLKRIDVPEwAASEEELRERLDKAEEALQSAREKQAAAEEqlvqANGELE 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1325 EETKAKNALAHALQSSRHDcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAkkkLAQRLQEA 1404
Cdd:pfam12128 636 KASREETFARTALKNARLD---LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW---LEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1405 EENTEASNSKCASLEKTKQRLQGEVDDLMLDLERAntACATLDKKQRNFDKVLAewkqKLDESQAELEAAQKESRSLSTE 1484
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALLKAAIAARRSG--AKAELKALETWYKRDLA----SLGVDPDVIAKLKREIRTLERK 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1485 IFKMRNAYEEVVD----QLETLRRENKNLQEEISDLTEQIAETGKNL----QEVEKTKKQVEQEKSDLQAALEEVEGSLE 1556
Cdd:pfam12128 784 IERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLarliADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1557 HEESKILRV-QLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLD 1606
Cdd:pfam12128 864 GLRCEMSKLaTLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1589-1812 |
2.29e-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: 55.16 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1589 QIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSN 1668
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1669 EDLKEQLAIVER---RNG--------LLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEAD 1737
Cdd:COG4942 100 EAQKEELAELLRalyRLGrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486959 1738 LAQcQAEVENSIQESRNAEEKAKKAItdaammAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGG 1812
Cdd:COG4942 180 LAE-LEEERAALEALKAERQKLLARL------EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1468-1659 |
2.83e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 QAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENK--NLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQ 1545
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1546 AALEEVEGSLE--HEESKILRVQLELSQVKSELDR----------KVTEKDEEIEQIKRNSQRAVEAMQSVLDAEI---R 1610
Cdd:COG3206 247 AQLGSGPDALPelLQSPVIQQLRAQLAELEAELAElsarytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAELealQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1611 SRNDALR-----LKKKMEgDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQL 1659
Cdd:COG3206 327 AREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1653-1889 |
2.93e-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: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1653 QLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKK 1732
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1733 KLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKkeqdtsahleRMKKNLEQTVKDLQHRLDEAEQL--ALK 1810
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK----------YLAPARREQAEELRADLAELAALraELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1811 GGKKQIQKLEARVRELESELDAEQKRGAEALKgahKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEA 1889
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
652-679 |
3.27e-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: 52.35 E-value: 3.27e-07
10 20
....*....|....*....|....*...
gi 124486959 652 SAVFRENLNKLMTNLRSTHPHFVRCLIP 679
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1400-1563 |
3.59e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1400 RLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAA--QKE 1477
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1478 SRSLSTEIfkmrnayeevvdqlETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEH 1557
Cdd:COG1579 91 YEALQKEI--------------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 124486959 1558 EESKIL 1563
Cdd:COG1579 157 ELEELE 162
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1258-1656 |
4.11e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1258 DQFNEIKAKDDQQTQLIHDLNmqkarlQTQngELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEeTKAKNALAHAL 1337
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLE------QTL--ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-LKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1338 QSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKlaqrlqeaeeNTEAS 1411
Cdd:PRK11281 117 TLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKG----------GKVGG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1412 NSKCASLektKQRLQGEVD--DLMLDLER----ANTACATLDKKQRNFdkvLAEWKQKLDESQAELEAAQKESRslstei 1485
Cdd:PRK11281 187 KALRPSQ---RVLLQAEQAllNAQNDLQRksleGNTQLQDLLQKQRDY---LTARIQRLEHQLQLLQEAINSKR------ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1486 fkmRNAYEEVVDQLETLRRENKN-----LQEEIS---DLTEQIAETGKNL----QEVEKTKKQVEqekSDLQA--ALEE- 1550
Cdd:PRK11281 255 ---LTLSEKTVQEAQSQDEAARIqanplVAQELEinlQLSQRLLKATEKLntltQQNLRVKNWLD---RLTQSerNIKEq 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1551 ---VEGSLEHeeSKIL-RVQLELSQVKseLDRKVTEK--DEEIEQIKRNSQR-----------AVEAMQS--VLDAEIRS 1611
Cdd:PRK11281 329 isvLKGSLLL--SRILyQQQQALPSAD--LIEGLADRiaDLRLEQFEINQQRdalfqpdayidKLEAGHKseVTDEVRDA 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 124486959 1612 RNDALRLKKKMEGDLN-EMEIQLSHA-NRQVaeTQKHLRTVQGQLKD 1656
Cdd:PRK11281 405 LLQLLDERRELLDQLNkQLNNQLNLAiNLQL--NQQQLLSVSDSLQS 449
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
962-1256 |
4.95e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 54.76 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 962 ELTLTKVEKEKHATENKVKNLSEEMTA-LEETISKLTKEKKSLQEAHQQTLDDLQVEEDKVNGLIKINV----KLEQQTD 1036
Cdd:pfam09731 150 EAKDDAIQAVKAHTDSLKEASDTAEISrEKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPetppKLPEHLD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1037 DLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQqlEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQ 1116
Cdd:pfam09731 230 NVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDII--PVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1117 ARTEELeeeieaehtVRAKIEKQRSDLARELEEISERLEEASGATSAQIEmnKKRESEFQKLRRDLEE---ATLQHEATA 1193
Cdd:pfam09731 308 KREEKH---------IERALEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEA 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1194 ATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASN---IETVSKSKSNMERMCRSV 1256
Cdd:pfam09731 377 HEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKA 442
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1593-1927 |
7.30e-07 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 54.56 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1593 NSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVaETQKHLR---TVQGQLKDSQL----HLDDAQ 1665
Cdd:PLN03188 853 GSESAEKSKKQVPKAVEKVLAGAIRREMALEEFCTKQASEITQLNRLV-QQYKHERecnAIIGQTREDKIirleSLMDGV 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1666 RSNED-LKEQLAIVERRNGLLQEELE----------EMKVALEQTERTRR---LSEQELL--DSSD-RVQLLHSQNTSLI 1728
Cdd:PLN03188 932 LSKEDfLEEELASLMHEHKLLKEKYEnhpevlrtkiELKRVQDELEHYRNfydMGEREVLleEIQDlRSQLQYYIDSSLP 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1729 NTKK-----KLEADLAQCQAEVENSIQES--RNAEEKAKK-------AITDAAMMAEELKKEQDTSAHL-ERMKKNLEqT 1793
Cdd:PLN03188 1012 SARKrnsllKLTYSCEPSQAPPLNTIPEStdESPEKKLEQerlrwteAESKWISLAEELRTELDASRALaEKQKHELD-T 1090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1794 VKDLQHRLDEAEQLALKGGKKQIQK----------LEARVRELESELDAEQK-------RGAE--------ALKGAHKYE 1848
Cdd:PLN03188 1091 EKRCAEELKEAMQMAMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKKaaaragvRGAEskfinalaAEISALKVE 1170
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1849 RKvKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRqAEEAEEQANTqlsrcrrVQHELEEAEERADIAESQVNKLRAK 1927
Cdd:PLN03188 1171 RE-KERRYLRDENKSLQAQLRDTAEAVQAAGELLVR-LKEAEEALTV-------AQKRAMDAEQEAAEAYKQIDKLKRK 1240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
938-1117 |
8.58e-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: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 938 SELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQ-- 1015
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAel 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1016 ----------------VEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQ 1079
Cdd:COG4942 110 lralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 124486959 1080 LEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQA 1117
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
943-1537 |
1.11e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 943 KKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEEtiskltkekkslqeahqqTLDDLQVEEDKVN 1022
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS------------------ALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1023 gliKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQleeklkkkEFEMSQLQTRIDDEQ 1102
Cdd:PRK01156 253 ---RYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKND--------IENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1103 VLSLQLQKKIKELQArteeleeeieaEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEfqklrrdl 1182
Cdd:PRK01156 322 NKYHAIIKKLSVLQK-----------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEY-------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1183 eeatlqheataatlRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNE 1262
Cdd:PRK01156 383 --------------SKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1263 IKAK-----------DDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQqlEELKRQLEEETKAKN 1331
Cdd:PRK01156 449 LNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1332 AlAHALQSSRHDCDLLREQYEEEQEGKAELQRA-LSKANSEVAQW------RTKYETDAIQ-RTEELEEAKKKLAQRLQE 1403
Cdd:PRK01156 527 A-RADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWlnalavISLIDIETNRsRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1404 AEENTEASNSkcaSLEKTKQRLQGEVDDL---MLDLERANTACATLDKKQRNFDKVLAEWKQKLDeSQAELEAAQKESrs 1480
Cdd:PRK01156 606 IEIGFPDDKS---YIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIP-DLKEITSRINDI-- 679
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 1481 lSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQV 1537
Cdd:PRK01156 680 -EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1382-1708 |
1.16e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.76 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1382 DAIQRTEELEEAKKKLAQRLQEAEE---NTEASNSKCASLEKTKQRLQGEVDDLMLDLERAnTACATLDKKQRNFDKVLA 1458
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETLSTLSLR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1459 EWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETlrrenkNLQ--EEISDLTEQIAETGKNLQEVEKTKKQ 1536
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYA------NSQrlQQIRNLLKGGKVGGKALRPSQRVLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1537 VEQEKSDLQAALEEVE----------GSLEHEES--KILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSV 1604
Cdd:PRK11281 199 AEQALLNAQNDLQRKSlegntqlqdlLQKQRDYLtaRIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1605 LDAEIRSRNDAL--RLKKKMEgDLNEMeiqlshanrqvaeTQKHLRTVQgqlkdsqlHLDDAQRSNEDLKEQLAiVERRN 1682
Cdd:PRK11281 279 LVAQELEINLQLsqRLLKATE-KLNTL-------------TQQNLRVKN--------WLDRLTQSERNIKEQIS-VLKGS 335
|
330 340
....*....|....*....|....*.
gi 124486959 1683 GLLQEELEEMKVALEQTERTRRLSEQ 1708
Cdd:PRK11281 336 LLLSRILYQQQQALPSADLIEGLADR 361
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
980-1534 |
1.17e-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: 53.60 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 980 KNLSEEMTALEETISKLTKEK-KSLQEAHQQTLDDLQveeDKVNGlikinvkLEQQTDDLEGSLEQEKKLRADLERVKRK 1058
Cdd:pfam07111 132 KNLEEGSQRELEEIQRLHQEQlSSLTQAHEEALSSLT---SKAEG-------LEKSLNSLETKRAGEAKQLAEAQKEAEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1059 LEGDLKMSQEsimDLEndtQQLEEKLKKKEFEMSQLQTRIdDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEK 1138
Cdd:pfam07111 202 LRKQLSKTQE---ELE---AQVTLVESLRKYVGEQVPPEV-HSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1139 QRSDLARELEEISERLE-----EASGATSAQIEMNKKRESEFqKLRRDLEEATLQHEATAATLRkkhaDTVAELGEQIDN 1213
Cdd:pfam07111 275 LTHMLALQEEELTRKIQpsdslEPEFPKKCRSLLNRWREKVF-ALMVQLKAQDLEHRDSVKQLR----GQVAELQEQVTS 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1214 -------LQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQF----NEIKAKDDQQTQLIHDLNMQKA 1282
Cdd:pfam07111 350 qsqeqaiLQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLkfvvNAMSSTQIWLETTMTRVEQAVA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1283 RLQTQNGELSHQVeEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRhdcdllreqyEEEQEGKAELQ 1362
Cdd:pfam07111 430 RIPSLSNRLSYAV-RKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLR----------EERNRLDAELQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1363 RALSKANSEVAQWRTKYETDAIQrteeLEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTA 1442
Cdd:pfam07111 499 LSAHLIQQEVGRAREQGEAERQQ----LSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEI 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1443 CAtlDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRenknLQEEISdlTEQIAE 1522
Cdd:pfam07111 575 YG--QALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRR----LQDEAR--KEEGQR 646
|
570
....*....|..
gi 124486959 1523 TGKNLQEVEKTK 1534
Cdd:pfam07111 647 LARRVQELERDK 658
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1134-1334 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1134 AKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEAtlqheataatlRKKHADTVAELGEQIDN 1213
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----------EAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1214 LQRVKQKLekekSELKM-----EIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQN 1288
Cdd:COG3883 95 LYRSGGSV----SYLDVllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124486959 1289 GELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALA 1334
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
845-1616 |
1.50e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 845 KSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLmdaEERCEGLIKSKIQLEAKVK 924
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 925 elnerlEEEEEMNSELVAKKRNLEDKCSSLKRDIDDL----ELTLTKVEKE-KHATENKVKNLSEEMTALEETISKLtke 999
Cdd:pfam12128 379 ------RRRSKIKEQNNRDIAGIKDKLAKIREARDRQlavaEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL--- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1000 kKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRadlervKRKLEGDLKMSQESIMDLENDTQQ 1079
Cdd:pfam12128 450 -KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR------KRRDQASEALRQASRRLEERQSAL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1080 LEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKI-KELQART-------EELEEEIEAEHTVRAKIEK-QRSDLARELEEI 1150
Cdd:pfam12128 523 DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVIsPELLHRTdldpevwDGSVGGELNLYGVKLDLKRiDVPEWAASEEEL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1151 SERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLrKKHADTVAELGEQIDNLQRVKQKLEKEKSELKM 1230
Cdd:pfam12128 603 RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSAN 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1231 EiddmasnietvsksksnmermcrsvedqfnEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEK-----ESLVSQL 1305
Cdd:pfam12128 682 E------------------------------RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvveGALDAQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1306 TKSKQALTQQLEELKRQLEE-ETKAKNALAHALQSSRHDCDLLREqyeeeqegKAELQRALSKA---NSEVAQWRTKY-E 1380
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKAlETWYKRDLASLGVDPDVIAKLKRE--------IRTLERKIERIavrRQEVLRYFDWYqE 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1381 TDAIQR------TEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMldlerantacatldKKQRNFD 1454
Cdd:pfam12128 804 TWLQRRprlatqLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENL--------------RGLRCEM 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1455 KVLAEWKQKLDESQAELEAAQkesRSLSTEIFKMRNAYEEvvdqlETLRRENKNLQEEISDLT-EQIAETGKNLQEVEKT 1533
Cdd:pfam12128 870 SKLATLKEDANSEQAQGSIGE---RLAQLEDLKLKRDYLS-----ESVKKYVEHFKNVIADHSgSGLAETWESLREEDHY 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1534 ---KKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLE-LSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQ-----SV 1604
Cdd:pfam12128 942 qndKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSiLGVDLTEFYDVLADFDRRIASFSRELQREVGEEAffegvSE 1021
|
810
....*....|..
gi 124486959 1605 LDAEIRSRNDAL 1616
Cdd:pfam12128 1022 SAVRIRSKVSEL 1033
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1524-1930 |
1.69e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.37 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1524 GKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQvKSELDRKVTEKDeeieqikrNSQRaveamqs 1603
Cdd:PLN02939 41 GFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQ-KSTSSDDDHNRA--------SMQR------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1604 vlDAEIRSRNDalRLKKKMEGDLNEMEIQLSHANRQVAETQKH-LRTVQGQLKDSQlHLDDAQRSNEDLKEQLAIVERRn 1682
Cdd:PLN02939 105 --DEAIAAIDN--EQQTNSKDGEQLSDFQLEDLVGMIQNAEKNiLLLNQARLQALE-DLEKILTEKEALQGKINILEMR- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1683 glLQEELEEMKVALEQTERTRRLSEQelldssdrvqllhsqntsLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKA 1762
Cdd:PLN02939 179 --LSETDARIKLAAQEKIHVEILEEQ------------------LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1763 ITDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAE 1839
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1840 A---LKGAHKYERKVKEMTYQAEEdrKNILRLQ-DLVDKLQAKVKSYKRQAEEAEEQANTQlsrcrrVQHELEEAEERAD 1915
Cdd:PLN02939 319 AalvLDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSY------IQLYQESIKEFQD 390
|
410
....*....|....*
gi 124486959 1916 IAESQVNKLRAKSRD 1930
Cdd:PLN02939 391 TLSKLKEESKKRSLE 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1747-1930 |
1.98e-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: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1747 NSIQESRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVREL 1826
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA---LLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1827 ESELDAEQKRGAEALKGAHKYERK---------------VKEMTY----------QAEEDRKNILRLQDLVDKLQAKVKS 1881
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYlkylaparreQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 124486959 1882 YKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRD 1930
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1385-1914 |
2.08e-06 |
|
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: 53.05 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1385 QRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKL 1464
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1465 DESQAELEAAQKESRslsteifkmrnayeevvdqletLRRENKNLQEEISDLTEQIAEtgknlqeVEKTKKQVEQEKSDL 1544
Cdd:TIGR00618 243 AYLTQKREAQEEQLK----------------------KQQLLKQLRARIEELRAQEAV-------LEETQERINRARKAA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1545 QAALEEveGSLEHEESKILRVQLELsQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDAlrlkkkmeg 1624
Cdd:TIGR00618 294 PLAAHI--KAVTQIEQQAQRIHTEL-QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH--------- 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1625 dlNEMEIQLSHANRQVAETQkHLRTVQGQLKdsqlHLDDAQRSNEDLKEQLaiverRNGLLQEELEEMKVALEQTERTRR 1704
Cdd:TIGR00618 362 --EVATSIREISCQQHTLTQ-HIHTLQQQKT----TLTQKLQSLCKELDIL-----QREQATIDTRTSAFRDLQGQLAHA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1705 LSEQELLDSSDRVQLLHSQNTSLINTKKKLEA-DLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQdtsahL 1783
Cdd:TIGR00618 430 KKQQELQQRYAELCAAAITCTAQCEKLEKIHLqESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP-----C 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1784 ERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAE-------ALKGAHKYERKVKEMTY 1856
Cdd:TIGR00618 505 PLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASlkeqmqeIQQSFSILTQCDNRSKE 584
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1857 QAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERA 1914
Cdd:TIGR00618 585 DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1453-1623 |
2.57e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1453 FDKVLAEWKQKLDESQAE--LEAAQKESRSLSTEifKMRNAYEEVVDQLETLRRENKNLQEEisdlteqiaetgknLQEV 1530
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNE--------------LQKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1531 EKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRavEAMQSVLD-AEI 1609
Cdd:PRK12704 88 EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEILLEkVEE 165
|
170
....*....|....
gi 124486959 1610 RSRNDALRLKKKME 1623
Cdd:PRK12704 166 EARHEAAVLIKEIE 179
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1731-1894 |
2.71e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1731 KKKLEADLAQCQAEVENSIQESRN-AEEKAKKAITDAAMMAEELKKEQDTS-----AHLERMKKNLEQTVKDLQHRLDEA 1804
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFEKElrerrNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1805 EQLalkggKKQIQKLEARVRELESELDAEQKRgaeaLKGAHKYERKVKE--MTYQAEEDRKNIlrLQDLVDKLQAKVKSY 1882
Cdd:PRK12704 106 EKR-----EEELEKKEKELEQKQQELEKKEEE----LEELIEEQLQELEriSGLTAEEAKEIL--LEKVEEEARHEAAVL 174
|
170
....*....|...
gi 124486959 1883 KRQAE-EAEEQAN 1894
Cdd:PRK12704 175 IKEIEeEAKEEAD 187
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
939-1565 |
2.85e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.75 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 939 ELVAKKRNLEDKCSSLKRDIDDLELTLTK---------VEKEKHATENKV---KNLSEEMTALEETISKLTKEKKSLQE- 1005
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKaisnddpeeIEKKIENIVTKIdkkKNIYDEIKKLLNEIAEIEKDKTSLEEv 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1006 -----AHQQTLDDLQVEedkvnglikinvKLEQQTDDLEGSLEQEKKLRADLERVKRKL-EGDLKMSQESIMDLENDTQQ 1079
Cdd:TIGR01612 1213 kginlSYGKNLGKLFLE------------KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSpEIENEMGIEMDIKAEMETFN 1280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1080 LEEKLKKKEFEMSQLQTR-IDDEQVLSLqlqkKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISE-----R 1153
Cdd:TIGR01612 1281 ISHDDDKDHHIISKKHDEnISDIREKSL----KIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilK 1356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1154 LEEASGATSAQIEMNKKRESEFQKLRRDLEEA-----TLQHEATAATLRKKHADTVAelGEQIDN-LQRVKqklekeksE 1227
Cdd:TIGR01612 1357 LNKIKKIIDEVKEYTKEIEENNKNIKDELDKSeklikKIKDDINLEECKSKIESTLD--DKDIDEcIKKIK--------E 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1228 LKMEIDDMASNIETVSKsksNMERMCRSVEDQFNEIKAKDDQQTQLIhdlnmqkaRLQTQNGELSHQVeekeslvsqltk 1307
Cdd:TIGR01612 1427 LKNHILSEESNIDTYFK---NADENNENVLLLFKNIEMADNKSQHIL--------KIKKDNATNDHDF------------ 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1308 skqaltqQLEELKRQLEEETKAKN-ALAHALQSSRHdcDLLREQYeeeqegKAELQRALSKANS-EVAQWRTKYETDAIQ 1385
Cdd:TIGR01612 1484 -------NINELKEHIDKSKGCKDeADKNAKAIEKN--KELFEQY------KKDVTELLNKYSAlAIKNKFAKTKKDSEI 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1386 RTEELEEAKKKLAQRLQEAEEnteasnsKCASLEKTKQRLQGEVddlmLDLERANTACATLDKKQRNFDKVL---AEWKQ 1462
Cdd:TIGR01612 1549 IIKEIKDAHKKFILEAEKSEQ-------KIKEIKKEKFRIEDDA----AKNDKSNKAAIDIQLSLENFENKFlkiSDIKK 1617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1463 KLDESQAELEAAQKESRSLS-----TEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQ- 1536
Cdd:TIGR01612 1618 KINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNy 1697
|
650 660 670
....*....|....*....|....*....|...
gi 124486959 1537 ----VEQEKSDLQAALEEVEGSLEHEESKILRV 1565
Cdd:TIGR01612 1698 eigiIEKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1379-1621 |
3.05e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 52.53 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1379 YETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKcASLEKTKQRLQGEVDDLMldleranTACATLDKKQRNFDKvla 1458
Cdd:NF012221 1529 YILDNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQL-------AAISGSQSQLESTDQ--- 1597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1459 ewkQKLDES-QAELEAAQKESRSLSTEIFKMRNAYEEV----VDQLETLRRENKNLQEEI-SDLTEQIAETGKNLQE-VE 1531
Cdd:NF012221 1598 ---NALETNgQAQRDAILEESRAVTKELTTLAQGLDALdsqaTYAGESGDQWRNPFAGGLlDRVQEQLDDAKKISGKqLA 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1532 KTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKvteKDEEIEQIKRNSQRAVEAMQSVLDAEIRS 1611
Cdd:NF012221 1675 DAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR---KDDALAKQNEAQQAESDANAAANDAQSRG 1751
|
250
....*....|
gi 124486959 1612 RNDALRLKKK 1621
Cdd:NF012221 1752 EQDASAAENK 1761
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
858-1237 |
3.69e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 858 EDFERAKEDL-ARSEARRKELEEKMVSLLQEKNdlqlQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNERLEEEEEM 936
Cdd:PRK02224 310 EAVEARREELeDRDEELRDRLEECRVAAQAHNE----EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 937 NSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETIskltKEKKSLQEA---------- 1006
Cdd:PRK02224 386 IEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEAgkcpecgqpv 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1007 ----HQQTLDDlqvEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEgDLKMSQESIMDLENDTQQLEE 1082
Cdd:PRK02224 462 egspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE-RREDLEELIAERRETIEEKRE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1083 KLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLArELEEISERLEEASGATS 1162
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKRE 616
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1163 AQIEMNKKRESEFQKLR---RDLEEATLQHEATAATLRKKHADT-VAELGEQIDNLQRVKQKLEKEKSELKMEIDDMAS 1237
Cdd:PRK02224 617 ALAELNDERRERLAEKRerkRELEAEFDEARIEEAREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1108-1800 |
4.22e-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: 51.75 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1108 LQKKIKELQarteeleeeiEAEHTVRAKIEKQRSDLARELEEISE------------RLEEASgATSAQIEMNKKRESEF 1175
Cdd:pfam10174 1 LQAQLRDLQ----------RENELLRRELDIKESKLGSSMNSIKTfwspelkkeralRKEEAA-RISVLKEQYRVTQEEN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1176 QKL-------------RRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETv 1242
Cdd:pfam10174 70 QHLqltiqalqdelraQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIET- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1243 skSKSNMERMCRSVEDQFNEIKAK---------DDQQTQLIHDLNMQ----KARLQTQNGELSHQVEE------------ 1297
Cdd:pfam10174 149 --QKQTLGARDESIKKLLEMLQSKglpkksgeeDWERTRRIAEAEMQlghlEVLLDQKEKENIHLREElhrrnqlqpdpa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1298 KESLVSQLTKSKQALTQQLEELKRQLEEEtkaknalahaLQSSRHDCDLLREQYEEE--------------QEGKAELQR 1363
Cdd:pfam10174 227 KTKALQTVIEMKDTKISSLERNIRDLEDE----------VQMLKTNGLLHTEDREEEikqmevykshskfmKNKIDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1364 ALSKANSEVAQWRTKYET------DAIQRTEELEEakkklaqrlqeaeenteasnskcaSLEKTKQR---LQGEVDDLML 1434
Cdd:pfam10174 297 ELSKKESELLALQTKLETltnqnsDCKQHIEVLKE------------------------SLTAKEQRaaiLQTEVDALRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1435 DLErantacatldkkqrnfdkvlaEWKQKLDESQAELEAAQKESRSLSTEIFKMRnayeevvDQLETLRRENKNLQEEIS 1514
Cdd:pfam10174 353 RLE---------------------EKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1515 DLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRvqlelsqVKSELDRKVTEKDEEIEQIKRNS 1594
Cdd:pfam10174 405 NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIER-------LKEQREREDRERLEELESLKKEN 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1595 QRAVEAMqSVLDAEIRSRNDAL-RLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTV---QGQLKDSQlHLDDAQRSNED 1670
Cdd:pfam10174 478 KDLKEKV-SALQPELTEKESSLiDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECsklENQLKKAH-NAEEAVRTNPE 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1671 LKEQLAIVERR-------NGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLH-SQNTSLINTKKKLEADLAQCQ 1742
Cdd:pfam10174 556 INDRIRLLEQEvarykeeSGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMkEQNKKVANIKHGQQEMKKKGA 635
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1743 AEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNLEQTVKDLQHR 1800
Cdd:pfam10174 636 QLLEEARRREDNLADNSQQLQLEELMGALEKTRQE-----LDATKARLSSTQQSLAEK 688
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1307 |
4.47e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 844 LKSAEAE-KEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQsetenlmdaeerCEGLIKSKIQLEAK 922
Cdd:COG4717 73 LKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ------------LLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 VKELNERLEEEEEMN---SELVAKKRNLEDKCSSLKRDIDDL-ELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTK 998
Cdd:COG4717 141 LAELPERLEELEERLeelRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 999 EKKSLQEAHQQTLDDLQVEEDK--------VNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESI 1070
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEerlkearlLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1071 mdlendtqQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEI 1150
Cdd:COG4717 301 --------GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1151 SERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQ-HEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELK 1229
Cdd:COG4717 373 AALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1230 MEIDDMASNIETVSKSK--SNMERMCRSVEDQFNEIkAKDDQQTQLIHDLnMQKARLQTQNGELSHQVEEKESLVSQLTK 1307
Cdd:COG4717 453 EELAELEAELEQLEEDGelAELLQELEELKAELREL-AEEWAALKLALEL-LEEAREEYREERLPPVLERASEYFSRLTD 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-1930 |
5.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1757 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggkKQIQKLEARVRELESELDAEQKR 1836
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1837 GAEALKGAHKYERKVKEMtyqaEEDRKNILRLQDLVDKLQAKVKSYKRQA-EEAEEQANTQLSRCRRVQHELEEAEERAD 1915
Cdd:COG4717 148 LEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*
gi 124486959 1916 IAESQVNKLRAKSRD 1930
Cdd:COG4717 224 ELEEELEQLENELEA 238
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1328-1686 |
5.65e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.38 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1328 KAKNALAHALQssrhDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdaIQRT------------EELEEAKK 1395
Cdd:PRK04778 102 KAKHEINEIES----LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRE--LRKSllanrfsfgpalDELEKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1396 KLAQRLQEAEENTEASNSKCAS-----------------------LEKTKQRLQGEVDDLML---DLERANTACATLDkk 1449
Cdd:PRK04778 176 NLEEEFSQFVELTESGDYVEAReildqleeelaaleqimeeipelLKELQTELPDQLQELKAgyrELVEEGYHLDHLD-- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1450 qrnFDKVLAEWKQKLDESQA-----ELEAAQKESRSLSTEIFKMRNAYE--------------EVVDQLETLRRENKNLQ 1510
Cdd:PRK04778 254 ---IEKEIQDLKEQIDENLAlleelDLDEAEEKNEEIQERIDQLYDILErevkarkyveknsdTLPDFLEHAKEQNKELK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1511 EEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSleheeskilrvqlelSQVKSELDRKVTEKDEEIEQI 1590
Cdd:PRK04778 331 EEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQ---------------EIAYSELQEELEEILKQLEEI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1591 KRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEG-------------------DLNEMEIQLSHANRQVAETQKHLRTVQ 1651
Cdd:PRK04778 396 EKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEikryleksnlpglpedyleMFFEVSDEIEALAEELEEKPINMEAVN 475
|
410 420 430
....*....|....*....|....*....|....*
gi 124486959 1652 GQLKDSQLHLDDAQRSNEDLKEQLAIVERrngLLQ 1686
Cdd:PRK04778 476 RLLEEATEDVETLEEETEELVENATLTEQ---LIQ 507
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1488-1924 |
6.06e-06 |
|
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: 51.01 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1488 MRNAYEEVVDQLETLRRE--NKNLQEEISDLtEQIAETGKNLQEVEKTKKQ----VEQEKSDLQAALEEVEGSLEheESK 1561
Cdd:pfam06160 4 LRKKIYKEIDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND--KYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1562 ILRVQLELSQVKSELDR---KVTEKDEEIEQIKRNSQRAVEAMQSVLDA------EIRSRNDAL-RLKKKMEGDLNEMEI 1631
Cdd:pfam06160 81 FKKAKKALDEIEELLDDieeDIKQILEELDELLESEEKNREEVEELKDKyrelrkTLLANRFSYgPAIDELEKQLAEIEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1632 QLSH------------ANRQVAETQKHLRTVQGQLKDSQLHLDDAQRsneDLKEQLAivERRNGLlqEELEEMKVALEQT 1699
Cdd:pfam06160 161 EFSQfeeltesgdyleAREVLEKLEEETDALEELMEDIPPLYEELKT---ELPDQLE--ELKEGY--REMEEEGYALEHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1700 ErtrrlSEQELLDSSDRVQllhsQNTSLINtkkklEADLAQCQAEVE------NSIQESRNAEEKAKKaitdaammaeEL 1773
Cdd:pfam06160 234 N-----VDKEIQQLEEQLE----ENLALLE-----NLELDEAEEALEeieeriDQLYDLLEKEVDAKK----------YV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1774 KKEQDT-SAHLERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELE----------SELDAEQKRG 1837
Cdd:pfam06160 290 EKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVerleekevaySELQEELEEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1838 AEALKGAHKYERKVKEMTYQAEEDRKnilRLQDLVDKLQAKVKSYKR-------------------QAEEAEEQANTQLS 1898
Cdd:pfam06160 370 LEQLEEIEEEQEEFKESLQSLRKDEL---EAREKLDEFKLELREIKRlveksnlpglpesyldyffDVSDEIEDLADELN 446
|
490 500 510
....*....|....*....|....*....|
gi 124486959 1899 RCR----RVQHELEEAEERADIAESQVNKL 1924
Cdd:pfam06160 447 EVPlnmdEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1213 |
6.46e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 845 KSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSL--LQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAk 922
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 vkelnerleeeeemnselvakkrnLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKS 1002
Cdd:COG4913 690 ------------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1003 LQEAHqqtLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQ-EKKLRADLERVKRKLEGDLKMSQESIMDLEnDTQQle 1081
Cdd:COG4913 746 ELRAL---LEERFAAALGDAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-EYLA-- 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1082 eklkkkefemsqLQTRIDDEQVLslQLQKKIKELQARTEEleeeieaehtvrAKIEKQRSDLARELEEISERLEEASGA- 1160
Cdd:COG4913 820 ------------LLDRLEEDGLP--EYEERFKELLNENSI------------EFVADLLSKLRRAIREIKERIDPLNDSl 873
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1161 --------TSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDN 1213
Cdd:COG4913 874 kripfgpgRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1732-1926 |
7.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1732 KKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAH----LERMKKNLEQTVKDLQHRLDEAEQL 1807
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAelarLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1808 ALKGGKKQIQKLEARVRELESELDAEQKRgaealkgAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAE 1887
Cdd:COG4913 332 IRGNGGDRLEQLEREIERLERELEERERR-------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE 404
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124486959 1888 EAEEQANTQLSRCRR----VQHELEEAEERADIAESQVNKLRA 1926
Cdd:COG4913 405 EALAEAEAALRDLRRelreLEAEIASLERRKSNIPARLLALRD 447
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1440-1934 |
7.03e-06 |
|
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: 51.17 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1440 NTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRS-------LSTEIFKMRNAYEEVVDQLETLRRENKNLQEE 1512
Cdd:TIGR04523 74 NNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNdkeqknkLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1513 ISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEgsleheeSKILRVQLELS--QVKSELDRKVTEKDEEIEQI 1590
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK-------NKLLKLELLLSnlKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1591 KRNSQRAVEAMQSvldaeirsrndalrlkkkmegDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNED 1670
Cdd:TIGR04523 227 NNQLKDNIEKKQQ---------------------EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1671 LKEQL-----AIVERRNGLLQEELEEMKVALEQTERTRRLSEQELldssdrvqllhSQNTSLINtkkkleaDLAQCQAEV 1745
Cdd:TIGR04523 286 LEKQLnqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI-----------SQNNKIIS-------QLNEQISQL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1746 ENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQLAlkggkkqiQKLEARVRE 1825
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQS---YKQEIKNLESQINDLESKIQNQEKLN--------QQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1826 LESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEaeeqantqlsrcrrVQH 1905
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK--------------IKQ 482
|
490 500
....*....|....*....|....*....
gi 124486959 1906 ELEEAEERADIAESQVNKLRAKSRDVGGQ 1934
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
843-1325 |
7.43e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 843 LLKSAEAEKEmATMKEDFERAKEDLARSEARRKELEEKMvSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKiqlEAK 922
Cdd:pfam05557 59 LLEKREAEAE-EALREQAELNRLKKKYLEALNKKLNEKE-SQLADAREVISCLKNELSELRRQIQRAELELQST---NSE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 VKELNERLEEEEEMNSELVAKKRNLEDKCSSLK---RDIDDLELTLTKVEKEKHATENkvknlseeMTALEETISKLTKE 999
Cdd:pfam05557 134 LEELQERLDLLKAKASEAEQLRQNLEKQQSSLAeaeQRIKELEFEIQSQEQDSEIVKN--------SKSELARIPELEKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1000 KKSLQEahqqtlddlqvEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRA-------DLERVKRKLEGDLKMSQE---- 1068
Cdd:pfam05557 206 LERLRE-----------HNKHLNENIENKLLLKEEVEDLKRKLEREEKYREeaatlelEKEKLEQELQSWVKLAQDtgln 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1069 --SIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARE 1146
Cdd:pfam05557 275 lrSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1147 LEEISERLE---------EASGATSAQI--------EMNKKRESEFQKLRRDLEEATLQHEATAA-----TLRKKHADT- 1203
Cdd:pfam05557 355 RDGYRAILEsydkeltmsNYSPQLLERIeeaedmtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTlerelQALRQQESLa 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1204 -VAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKA 1282
Cdd:pfam05557 435 dPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIE 514
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 124486959 1283 RLQTQNGELSHQVEEKESLVSQltkSKQALTQQLEELKRQLEE 1325
Cdd:pfam05557 515 RLKRLLKKLEDDLEQVLRLPET---TSTMNFKEVLDLRKELES 554
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1030-1449 |
7.64e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1030 KLEQQTDDLEGSLEQEKKLRADLERvKRKLEGDLKMSQESIMDLENDTQQleeklkkkefeMSQLQTRIDDEQVLSlQLQ 1109
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEK-----------LEKLLQLLPLYQELE-ALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1110 KKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQH 1189
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1190 EATAATLRKKHADTVAELgeqidNLQRVKQKLEKEKSELK---------MEIDDMASNIETV------------------ 1242
Cdd:COG4717 219 QEELEELEEELEQLENEL-----EAAALEERLKEARLLLLiaaallallGLGGSLLSLILTIagvlflvlgllallflll 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1243 SKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTK-SKQALTQQLEELKR 1321
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1322 QLEEETKAKN--ALAHALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiqrTEELEEAKKKLAQ 1399
Cdd:COG4717 374 ALLAEAGVEDeeELRAALE--------QAEEYQELKEELEELEEQLEELLGELEELLEALD------EEELEEELEELEE 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1400 RLQEAEENTEASNSKCASLEKTKQRL--QGEVDDLMLDLERANTACATLDKK 1449
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
949-1174 |
1.06e-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: 50.15 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 949 DKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQveedkvnglikin 1028
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1029 vKLEQQTDDLEGSLEQEKKLRAD----LERVKRKLEGDLKMSQESIMDLEND-------TQQLEEKLKKKEFEMSQLQTR 1097
Cdd:COG4942 87 -ELEKEIAELRAELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRlqylkylAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 1098 IDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESE 1174
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1352-1537 |
1.22e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1352 EEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqeaEENTEasnSKCASLEKTKQRLQGEVDD 1431
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLD---RKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1432 lmldlerantacatLDKKQRNFDKVLAEWKQKLDESQAELEaaqkESRSLSTEifkmrNAYEEVVDQLEtlrrenKNLQE 1511
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELE----RISGLTAE-----EAKEILLEKVE------EEARH 169
|
170 180
....*....|....*....|....*.
gi 124486959 1512 EISDLTEQIAETGKnlQEVEKTKKQV 1537
Cdd:PRK12704 170 EAAVLIKEIEEEAK--EEADKKAKEI 193
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1256-1702 |
1.31e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1256 VEDQFNEIKAKDDQQTQLIHDLNMQKARlqtqngelsHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAH 1335
Cdd:pfam06160 58 VTKSLPDIEELLFEAEELNDKYRFKKAK---------KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1336 ALQSSRHDCDLLREQYEEEQEgkaELQRALSKANSEVAQWRTKYET-DAIQRTEELEEAKKklaqRLQEAEENTEasnsK 1414
Cdd:pfam06160 129 KYRELRKTLLANRFSYGPAID---ELEKQLAEIEEEFSQFEELTESgDYLEAREVLEKLEE----ETDALEELME----D 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1415 CASL-EKTKQRLQGEVDDL---MLDLERANTACATLdkkqrNFDKVLAEWKQKLDESQA-----ELEAAQKESRSLSTEI 1485
Cdd:pfam06160 198 IPPLyEELKTELPDQLEELkegYREMEEEGYALEHL-----NVDKEIQQLEEQLEENLAllenlELDEAEEALEEIEERI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1486 FKM-------RNAYEEVVDQLETL-------RRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQeksdLQAALEEV 1551
Cdd:pfam06160 273 DQLydllekeVDAKKYVEKNLPEIedylehaEEQNKELKEELERVQQSYTLNENELERVRGLEKQLEE----LEKRYDEI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1552 EGSLEHEEskilrvqlelsQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKmegdLNEMEI 1631
Cdd:pfam06160 349 VERLEEKE-----------VAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLE----LREIKR 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1632 QLSHAN---------RQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAiverrngLLQEELEEMKVALEQTERT 1702
Cdd:pfam06160 414 LVEKSNlpglpesylDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVD-------TLYEKTEELIDNATLAEQL 486
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
959-1337 |
1.42e-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: 50.17 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 959 DDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSL----QEAHQQTLDDLQVEEDKVNGLIKINVKleqQ 1034
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLevnmQALKAQFERDLQARDEQGEEKRRQLVK---Q 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1035 TDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQ-------VLSLQ 1107
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilAQSKE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1108 LQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELeeiserleeASGATSAQIEMNKKR--ESEFQKLRRDLEEA 1185
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEI---------ASGASGKSALQDEKRrlEARIAQLEEELEEE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1186 TLQHEATAATLRK--KHADTV-AELGEQIDNLQRV---KQKLEKEKSELKMEIDDMASNIETVSKSK-SNMERMCRSVED 1258
Cdd:pfam01576 902 QSNTELLNDRLRKstLQVEQLtTELAAERSTSQKSesaRQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEE 981
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1259 QFnEIKAKDDQQT--------QLIHDLNMQ-----------KARLQTQNG---ELSHQVEEKESLVSQLTKSKQALTQQL 1316
Cdd:pfam01576 982 QL-EQESRERQAAnklvrrteKKLKEVLLQvederrhadqyKDQAEKGNSrmkQLKRQLEEAEEEASRANAARRKLQREL 1060
|
410 420
....*....|....*....|.
gi 124486959 1317 EELKRQLEEETKAKNALAHAL 1337
Cdd:pfam01576 1061 DDATESNESMNREVSTLKSKL 1081
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1448-1938 |
1.43e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1448 KKQRNFDKVLAEWKQKLDESQAE---LEAAQKESRSLSTEIFKMRNAYE---EVVDQLETLRRENKNLQEEISDLTEQIA 1521
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMElkyLKQYKEKACEIRDQITSKEAQLEssrEIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1522 ETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHE---------------ESKILRVQLE----------LSQVKSEL 1576
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlndlyhnhqrtvrekERELVDCQREleklnkerrlLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1577 DRKVTEKDEEIEQI-----KRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQ 1651
Cdd:TIGR00606 346 LVEQGRLQLQADRHqehirARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1652 GQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEE----MKVALEQTERTRR-LSEQELLDSSD-------RVQL 1719
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKaERELSKAEKNSltetlkkEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1720 LHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKK-------------AITDAAMMAEELKKEQDTSAHLERM 1786
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKdeqirkiksrhsdELTSLLGYFPNKKQLEDWLHSKSKE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1787 KKNLEQTVKDLQHRLDEAEQLA------LKGGKKQIQKLEARVRE------LESELDAEQKRGAEALK-------GAHKY 1847
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKnhinneLESKEEQLSSYEDKLFDvcgsqdEESDLERLKEEIEKSSKqramlagATAVY 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1848 ERKVKEMTYQA-------EEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQ 1920
Cdd:TIGR00606 666 SQFITQLTDENqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
570
....*....|....*...
gi 124486959 1921 VNKLRAKSRDVGGQKMEE 1938
Cdd:TIGR00606 746 IPELRNKLQKVNRDIQRL 763
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1381-1609 |
1.47e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1381 TDAIQRTEELEEAKKKLAQRLQEAEENteasnskcasLEKTKQR-----LQGEVDDLMLDLERANTACATLDKKqrnfdk 1455
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAA----------LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAE------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1456 vLAEWKQKLDESQAELEAAQKESRSL--STEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNL-QEVEK 1532
Cdd:COG3206 235 -LAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1533 TKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQlELSQVKSELDRKVTEKDEEIEQIKRNSQRA-VEAMQSVLDAEI 1609
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEVARELYESLLQRLEEArLAEALTVGNVRV 390
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1417-1927 |
1.47e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1417 SLEKTKQRLQGEVDDLMLDLERANTACATLDKKQ---RNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYE 1493
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNlelENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1494 EVVDQLETLRRENKNLQEEISDLTEQIAETGKnLQEVEKTKKQVEQEKS------------------DLQAALEEVEGSL 1555
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVyknrnyindyfkykndieNKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1556 EHEESKILRVQlELSQVKSELDRKVTEKDE------EIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEM 1629
Cdd:PRK01156 322 NKYHAIIKKLS-VLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1630 EIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGL------------------LQEELEE 1691
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgeeksnhiinhYNEKKSR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1692 MKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTS-LINTKKKLEADLAQCQaEVENSIQESRNAEEKAKKAITDAAMMA 1770
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADLE-DIKIKINELKDKHDKYEEIKNRYKSLK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1771 EELKKEQDTSaHLERMKKNLEQTVKDLQHRLDEAeqlalkggKKQIQKLEARVRELESELDAEQKRgaealkgAHKYERK 1850
Cdd:PRK01156 560 LEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFPDDKSY-------IDKSIRE 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1851 VKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQA---EEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAK 1927
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1685-1923 |
1.63e-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: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1685 LQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAIT 1764
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1765 DAAMMAE----ELKKEQDTSAHLERMKKNLEQTVkdlQHRLDEAEQLalkggKKQIQKLEARVRELESELdAEQKRGAEA 1840
Cdd:COG4942 112 ALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLA---PARREQAEEL-----RADLAELAALRAELEAER-AELEALLAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1841 LKGAHKyerkvkemTYQAEEDRKnilrlQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQ 1920
Cdd:COG4942 183 LEEERA--------ALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 124486959 1921 VNK 1923
Cdd:COG4942 250 ALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1359-1567 |
1.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1359 AELQRALSKANSEVAQWRTKYE-TDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMldle 1437
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGlVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL---- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1438 rANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFK-MRNAYEEVVDQLETLRRENKNLQEEISDL 1516
Cdd:COG3206 261 -QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1517 TEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQL 1567
Cdd:COG3206 340 EARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1783-1908 |
2.14e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1783 LERMKK-NLEQTVKDLQHRLDEAEQL------ALKGGKKQIQKLEARVRELESELDAEQKRGAEALkgahkyeRKVKEMT 1855
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEAErsrlqaLLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124486959 1856 YQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSrcRRVQhELE 1908
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ-ELN 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1576-1810 |
2.16e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1576 LDRKVTEKD-----EEIEQIKRNSQRAVEAMQSV-LDAEIRSRNDALRlkkKMEGDLNEMEIQLSHANRQVAET-----Q 1644
Cdd:COG4913 218 LEEPDTFEAadalvEHFDDLERAHEALEDAREQIeLLEPIRELAERYA---AARERLAELEYLRAALRLWFAQRrlellE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1645 KHLRTVQGQLKDSQLHLDDAQRSNEDLKEQL-AIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSq 1723
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1724 ntSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLde 1803
Cdd:COG4913 374 --PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL-- 449
|
....*..
gi 124486959 1804 AEQLALK 1810
Cdd:COG4913 450 AEALGLD 456
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1500-1740 |
2.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1500 ETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKS--DLQAALEEVEGSLEHEESKILRVQLELSQVKSELD 1577
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1578 RKVtekdeeiEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKkkmegdLNEMEIQLSHANRQVAETQKHLRTVQGQLKDS 1657
Cdd:COG3206 244 ALR-------AQLGSGPDALPELLQSPVIQQLRAQLAELEAE------LAELSARYTPNHPDVIALRAQIAALRAQLQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1658 qlhlddAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTrrlsEQELLDSSDRVQLLHSQNTSLINTKKKLEAD 1737
Cdd:COG3206 311 ------AQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARLA 380
|
...
gi 124486959 1738 LAQ 1740
Cdd:COG3206 381 EAL 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1093-1240 |
2.38e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1093 QLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASG------------A 1160
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkeyeA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1161 TSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIE 1240
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
856-1423 |
2.70e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 856 MKEDFERAKEdLARSEARRKELEEKMVSLLQekndlqLQVQSETENLMDAEERCEGLIKSKIQLEAKVKEL----NERLE 931
Cdd:pfam05483 217 LKEDHEKIQH-LEEEYKKEINDKEKQVSLLL------IQITEKENKMKDLTFLLEESRDKANQLEEKTKLQdenlKELIE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 932 EEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTL 1011
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1012 DDLQVEEDKvngLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIM------DLENDTQQLEEKLK 1085
Cdd:pfam05483 370 QRLEKNEDQ---LKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiaeELKGKEQELIFLLQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1086 KKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEasgaTSAQI 1165
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK----HQEDI 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1166 EMNKKRESEFQKLRRDLEEATLQheataatLRkkhadtvaelgeqiDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKS 1245
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMN-------LR--------------DELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1246 KSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEEL----KR 1321
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyQK 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1322 QLEEETKAKNALAHALQSSRHDCDllrEQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAK-KKLAQR 1400
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKnKEQEQS 738
|
570 580
....*....|....*....|...
gi 124486959 1401 LQEAEENTEASNSKCASLEKTKQ 1423
Cdd:pfam05483 739 SAKAALEIELSNIKAELLSLKKQ 761
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1316-1891 |
2.80e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1316 LEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE--TDAIQRTEELEEA 1393
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1394 KKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWK---QKLDESQAE 1470
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDaeiNKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1471 LEAAQKESrslsTEIFKMRNAYEEVVDQLETLRRENKNLQ---EEISDLTEQIAETGKNLQ----EVEKTKKQVEQEKSD 1543
Cdd:PRK01156 331 LSVLQKDY----NDYIKKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIErmsaFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1544 LQAALEEVEGSLEHEESKILRVQLELSQVKSELDrkvtEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKME 1623
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLD----ELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1624 GDLNEMEIQLSHANrqvaETQKHLRTVQGQLKDSQLhlddaqrsNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTR 1703
Cdd:PRK01156 483 EKIREIEIEVKDID----EKIVDLKKRKEYLESEEI--------NKSINEYNKIESARADLEDIKIKINELKDKHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1704 RLSEQELLDSSDrvqlLHSQNTSLINTkkkleadlaqcQAEVEN-SIQESRNAEEKAKKAITDAAMMAEELKKE-QDTSA 1781
Cdd:PRK01156 551 IKNRYKSLKLED----LDSKRTSWLNA-----------LAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGfPDDKS 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1782 HLERMKKNLEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELE---SELDAEQKRGAEALKGAHKYERKVKEMTYQA 1858
Cdd:PRK01156 616 YIDKSIREIENEANNLNNKYNEIQEN-----KILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKAL 690
|
570 580 590
....*....|....*....|....*....|...
gi 124486959 1859 EEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEE 1891
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1467-1926 |
3.40e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1467 SQAELEAAQKEsRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQE----------VEKTKKQ 1536
Cdd:pfam05557 12 SQLQNEKKQME-LEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqaelnrlkkkYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1537 VEQEKSDLQAALEEVEGSLEHEES----KILRVQLELSQVKSEL----------DRKVTEKDEEIEQIKRNSQRAVEAMQ 1602
Cdd:pfam05557 91 KLNEKESQLADAREVISCLKNELSelrrQIQRAELELQSTNSELeelqerldllKAKASEAEQLRQNLEKQQSSLAEAEQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1603 SV--LDAEIRSRNDALRLKKKMEGDL---NEMEIQLshanRQVAETQKHLRTVQGQ---LKDSQLHLDDAQRSNEDLKEQ 1674
Cdd:pfam05557 171 RIkeLEFEIQSQEQDSEIVKNSKSELariPELEKEL----ERLREHNKHLNENIENkllLKEEVEDLKRKLEREEKYREE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1675 LAIVERRNGLLQEELEEMKVALEQTERTRRLSEqellDSSDRVQLLHSQNTSLINTKKKLEADLAQcqaeVENSIQESRN 1754
Cdd:pfam05557 247 AATLELEKEKLEQELQSWVKLAQDTGLNLRSPE----DLSRRIEQLQQREIVLKEENSSLTSSARQ----LEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1755 AEEKAKKAITDAAMMAEELK------KEQDTSAHLER--MKKNLEQTVKDL-QHRLDEAEQLALKGGKKQIQKLEARVRE 1825
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKalvrrlQRRVLLLTKERdgYRAILESYDKELtMSNYSPQLLERIEEAEDMTQKMQAHNEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1826 LESELDAEQKRGAEALKGAHKYERKVKEMTYQAE-----EDRKNILRLQDLVDKLQAKVKSYKRQAEEAEE-------QA 1893
Cdd:pfam05557 399 MEAQLSVAEEELGGYKQQAQTLERELQALRQQESladpsYSKEEVDSLRRKLETLELERQRLREQKNELEMelerrclQG 478
|
490 500 510
....*....|....*....|....*....|...
gi 124486959 1894 NTQLSRCRRVQHELEEAEERADIAESQVNKLRA 1926
Cdd:pfam05557 479 DYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1459-1712 |
3.64e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.97 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1459 EWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVD--QLETLRRENKNL-QEEISDLTEQIAETGKNLQEVEKTKK 1535
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKNE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1536 QVEQEksdLQAAleevegslehEESKILrvqlelsqvKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEiRSRnda 1615
Cdd:pfam17380 393 RVRQE---LEAA----------RKVKIL---------EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE-RAR--- 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1616 lrlkkkmegdlnEME-IQLSHANRQvaETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQlaiverRNGLLQEELEEMKV 1694
Cdd:pfam17380 447 ------------EMErVRLEEQERQ--QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQ 506
|
250
....*....|....*...
gi 124486959 1695 ALEQTERTRRLSEQELLD 1712
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEE 524
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1028-1935 |
4.11e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1028 NVKLEQQTD---DLEGSLEQEKKLRADLERVKRKLEgdlkMSQESIMDLENDTQQleeklkkkefemsqlqtrIDDEQVL 1104
Cdd:PRK04863 282 RVHLEEALElrrELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQA------------------ASDHLNL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1105 ---SLQLQKKIKELQArteeleeeieaehtvrakiekqrsdlarELEEISERLEEASGATSAQIEMNKKRESEFqklrrd 1181
Cdd:PRK04863 340 vqtALRQQEKIERYQA----------------------------DLEELEERLEEQNEVVEEADEQQEENEARA------ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1182 lEEATLQHEATAATLrkkhADTVAELGEQ---IDNLQRVKQKLEKEKSELK---MEIDDMASNIET-VSKSKSNMERMcR 1254
Cdd:PRK04863 386 -EAAEEEVDELKSQL----ADYQQALDVQqtrAIQYQQAVQALERAKQLCGlpdLTADNAEDWLEEfQAKEQEATEEL-L 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1255 SVEDQFN---EIKAKDDQQTQLIHDLNMQKARLQTQNG--ELSHQVEEKESLVSQLtkskQALTQQLEELKRQLEEETKA 1329
Cdd:PRK04863 460 SLEQKLSvaqAAHSQFEQAYQLVRKIAGEVSRSEAWDVarELLRRLREQRHLAEQL----QQLRMRLSELEQRLRQQQRA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1330 KNALAHALQSSRHDCDlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQE---AEE 1406
Cdd:PRK04863 536 ERLLAEFCKRLGKNLD-DEDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQRLAARAPAwlaAQD 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1407 NTEASNSKCASLEKTKQRlqgeVDDLMLDL---ERAntacATLDKKQrnfdkvLAEWKQKLDE-----SQAE-------L 1471
Cdd:PRK04863 611 ALARLREQSGEEFEDSQD----VTEYMQQLlerERE----LTVERDE------LAARKQALDEeierlSQPGgsedprlN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1472 EAAQKESRSLSTEIFK----------------MRNAYeeVVDQLETLRRENKNLQEEISD--LTEQ-IAETGKNLQEVEK 1532
Cdd:PRK04863 677 ALAERFGGVLLSEIYDdvsledapyfsalygpARHAI--VVPDLSDAAEQLAGLEDCPEDlyLIEGdPDSFDDSVFSVEE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1533 TKKQVEQEKSDLQ--------------AALEEvegSLEheeskILRVQLElsqvksELDRKVTEKDEEIEQIkrnsQRAV 1598
Cdd:PRK04863 755 LEKAVVVKIADRQwrysrfpevplfgrAAREK---RIE-----QLRAERE------ELAERYATLSFDVQKL----QRLH 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1599 EAMQSVLdaeirSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRsnedLKEQLAIV 1678
Cdd:PRK04863 817 QAFSRFI-----GSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNR----LLPRLNLL 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1679 ERRNglLQEELEEMKVALEQTERTRRlseqelldSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEK 1758
Cdd:PRK04863 888 ADET--LADRVEEIREQLDEAEEAKR--------FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQ 957
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1759 AkKAITDAAMMAEELKKEqDTSAHLERMKKNLEQtvkdLQHRLDEAEQL------ALKGGKKQIQKLEARVRELESELDA 1832
Cdd:PRK04863 958 A-FALTEVVQRRAHFSYE-DAAEMLAKNSDLNEK----LRQRLEQAEQErtrareQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1833 EQKRGAEAlkgahkyERKVKEMTYQAEEDRKNILRLQDlvDKLQAKVksykRQAEEAEEQANTQLSRCrrvqheleEAEe 1912
Cdd:PRK04863 1032 KRQMLQEL-------KQELQDLGVPADSGAEERARARR--DELHARL----SANRSRRNQLEKQLTFC--------EAE- 1089
|
970 980
....*....|....*....|...
gi 124486959 1913 radiAESQVNKLRAKSRDVGGQK 1935
Cdd:PRK04863 1090 ----MDNLTKKLRKLERDYHEMR 1108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
945-1365 |
4.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 945 RNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLS--EEMTALEETISKLTKEKKSLQEAHQQTLDdlqveedkvn 1022
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE---------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1023 glikinvkLEQQTDDLEGSLEQ-EKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDD- 1100
Cdd:COG4717 161 --------LEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQl 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1101 -EQVLSLQLQKKIKELQArteeleeeIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKK----RESEF 1175
Cdd:COG4717 233 eNELEAAALEERLKEARL--------LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARekasLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1176 QKLRRDLEEATLQHEATAATLRKKHADT------VAELGEQIDNLQRVKQKLEKEKSELKMEiddmasniETVSKSKSNM 1249
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPdlspeeLLELLDRIEELQELLREAEELEEELQLE--------ELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESlvSQLTKSKQALTQQLEELKRQLEEETKA 1329
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREE 454
|
410 420 430
....*....|....*....|....*....|....*.
gi 124486959 1330 KNALAHALQSSRHDcDLLREQYEEEQEGKAELQRAL 1365
Cdd:COG4717 455 LAELEAELEQLEED-GELAELLQELEELKAELRELA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1218-1449 |
4.97e-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: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1218 KQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEE 1297
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1298 KESLVSQLTKSKQALTQQ--LEELKRQleeetKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQW 1375
Cdd:COG4942 102 QKEELAELLRALYRLGRQppLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1376 RTKYEtdaiqrteELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKK 1449
Cdd:COG4942 177 EALLA--------ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1110-1250 |
5.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1110 KKIKELQARteeleeeiEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQH 1189
Cdd:PRK12704 55 KKEALLEAK--------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQEL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1190 EATAATLRKKHADTVAELgEQIDNLQR---VKQKLEKEKSELKMEIDDMASNIETVSKSKSNME 1250
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL-ERISGLTAeeaKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKK 189
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1180-1439 |
5.87e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.22 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1180 RDLEEATLQHEATAATLRKKHADTVAELGE----QIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRS 1255
Cdd:pfam00038 21 RFLEQQNKLLETKISELRQKKGAEPSRLYSlyekEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1256 VEDQFNEIKakddqqtQLIHDLNMQKARLQTQ----NGELSHQVEEKESLVSQLTKskqaltqQLEELKRQLEEETKAKN 1331
Cdd:pfam00038 101 AENDLVGLR-------KDLDEATLARVDLEAKieslKEELAFLKKNHEEEVRELQA-------QVSDTQVNVEMDAARKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1332 ALAHALQSsrhdcdlLREQYEEeqegkaelQRALSKANSEvAQWRTKYE---TDAIQRTEELEEAKKKLAQ---RLQEAE 1405
Cdd:pfam00038 167 DLTSALAE-------IRAQYEE--------IAAKNREEAE-EWYQSKLEelqQAAARNGDALRSAKEEITElrrTIQSLE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124486959 1406 ENTEASNSKCASLEK----TKQRLQGEVDD---LMLDLERA 1439
Cdd:pfam00038 231 IELQSLKKQKASLERqlaeTEERYELQLADyqeLISELEAE 271
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1147-1405 |
6.30e-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: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1147 LEEISERLEEASGATSAQIEmnkkreSEFQKLRRDLEEAtlqhEATAATLRKKHAdtVAELGEQIDNLQRVKQKLEKEKS 1226
Cdd:COG3206 162 LEQNLELRREEARKALEFLE------EQLPELRKELEEA----EAALEEFRQKNG--LVDLSEEAKLLLQQLSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1227 ELKMEIDDMASNIETVSKSKSNMERMCRSVEDqfNEIKAKDDQQtqlIHDLNMQKARLQTQNGELSHQVeekeslvsqlt 1306
Cdd:COG3206 230 EARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQ---LAELEAELAELSARYTPNHPDV----------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1307 kskQALTQQLEELKRQLEEETKAknalahALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdAIQR 1386
Cdd:COG3206 294 ---IALRAQIAALRAQLQQEAQR------ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR------RLER 358
|
250 260
....*....|....*....|..
gi 124486959 1387 teELEEAKKK---LAQRLQEAE 1405
Cdd:COG3206 359 --EVEVARELyesLLQRLEEAR 378
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1215-1523 |
6.68e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1215 QRVKQKLEKEKSE-LKMEIDDMASNIETVSKSKSNMErmcrSVEDQFNEIKAKDDQQTqlihdlnmqKARLQTQNGELSH 1293
Cdd:pfam05667 242 KRKRTKLLKRIAEqLRSAALAGTEATSGASRSAQDLA----ELLSSFSGSSTTDTGLT---------KGSRFTHTEKLQF 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1294 QVEEKESLVSQLTKskqalTQQLEELKRQLEEETKAknalahalqssrhdcdlLREQYEEEQEGKAELQRALSKANSEVA 1373
Cdd:pfam05667 309 TNEAPAATSSPPTK-----VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1374 QwrTKYETDAIQRT-EELEEA---KKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDD----LMLDLERANTACAT 1445
Cdd:pfam05667 367 Q--VEEELEELKEQnEELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSN 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1446 -LDKKQRNFDKvLAEWKQKLDESQAELEAAQKESRSLSTEIFKM-----RNAYE----EVVDQLETLRRE-------NKN 1508
Cdd:pfam05667 445 kEDESQRKLEE-IKELREKIKEVAEEAKQKEELYKQLVAEYERLpkdvsRSAYTrrilEIVKNIKKQKEEitkilsdTKS 523
|
330
....*....|....*
gi 124486959 1509 LQEEISDLTEQIAET 1523
Cdd:pfam05667 524 LQKEINSLTGKLDRT 538
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1136-1426 |
6.82e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1136 IEKQRSDLARELEEISERLEEAsgatsaQIEMNKKRESEFQKLRRDLEEATLQHEAT---AATLRKKHADTVAELGEQID 1212
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1213 NLQRVKQKLEKEK---SELKMEIDDMASNIETVSKSKSNMERMCRSVED-QFNEIKAKDDQQTQLIHDLNMQKARLQTQN 1288
Cdd:pfam17380 352 RIRQEERKRELERirqEEIAMEISRMRELERLQMERQQKNERVRQELEAaRKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1289 G---ELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE----- 1360
Cdd:pfam17380 432 ArqrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamiee 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1361 ------LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEnteaSNSKCASLEKTKQRLQ 1426
Cdd:pfam17380 512 erkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMR 579
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1507-1899 |
7.30e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1507 KNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALE-EVEGSLEHEESKILRVQLELSQVK-SELDRKVTEKD 1584
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1585 EEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEgdlnEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLdda 1664
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKID----QLKQELSKKESELLALQTKLETLTNQNSDCKQHI--- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1665 qrsnEDLKEQLAIVERRNGLLQEELEEMKVALEQTErtrrlseqelldssdrvqllhsqntSLINTKKKleadlaqcqae 1744
Cdd:pfam10174 327 ----EVLKESLTAKEQRAAILQTEVDALRLRLEEKE-------------------------SFLNKKTK----------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1745 vensiQESRNAEEKAkkaiTDAAmmaeELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVR 1824
Cdd:pfam10174 367 -----QLQDLTEEKS----TLAG----EIRDLKDMLDVKERKINVLQKKIENLQEQLRDKD--------KQLAGLKERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1825 ELES-------------ELDAEQKRGAEALKgaHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEE 1891
Cdd:pfam10174 426 SLQTdssntdtalttleEALSEKERIIERLK--EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKE 503
|
....*...
gi 124486959 1892 QANTQLSR 1899
Cdd:pfam10174 504 HASSLASS 511
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1314-1426 |
8.62e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 47.44 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1314 QQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEE-----QEGKAELQRALSKANSEVAQWRTKYETDAIQRtE 1388
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilEKAREEAEEILREARKEAEELIRELREAQAEE-E 599
|
90 100 110
....*....|....*....|....*....|....*...
gi 124486959 1389 ELEEAKKKLAQRLQEAEENTEASNSKcASLEKTKQRLQ 1426
Cdd:COG1193 600 ELKEARKKLEELKQELEEKLEKPKKK-AKPAKPPEELK 636
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1695-1927 |
9.73e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1695 ALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENsiqesrnAEEKAKKAitdaammaeeLK 1774
Cdd:COG1842 17 LLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK-------WEEKARLA----------LE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1775 KEQDTSAH--LERmKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLEARVRELESELDA--EQKRGAEALKgahkyerK 1850
Cdd:COG1842 80 KGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELKAKKDTlkARAKAAKAQE-------K 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 1851 VKEMTYQAEEDRknilrLQDLVDKLQAKVksykrQAEEAEEQANTQLSRCRRVQHELEEAEERADIaESQVNKLRAK 1927
Cdd:COG1842 151 VNEALSGIDSDD-----ATSALERMEEKI-----EEMEARAEAAAELAAGDSLDDELAELEADSEV-EDELAALKAK 216
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1176-1551 |
1.03e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1176 QKLRRDLEEATlqheataATLRKKHADTVAELGEQIDNLQRVKQKLEKEKsELKMEIDDMASNIETVSKSKSNMERMCRS 1255
Cdd:PRK10929 26 KQITQELEQAK-------AAKTPAQAEIVEALQSALNWLEERKGSLERAK-QYQQVIDNFPKLSAELRQQLNNERDEPRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1256 VEDqfneikakddqqTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEE---------- 1325
Cdd:PRK10929 98 VPP------------NMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEierrlqtlgt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1326 ----ETKAKNALAHALQSSRHdcdLLREQYEEEQEgKAELQRALSKANSEVAQWRTKyETDAiqrteELEEAKKKL-AQR 1400
Cdd:PRK10929 166 pntpLAQAQLTALQAESAALK---ALVDELELAQL-SANNRQELARLRSELAKKRSQ-QLDA-----YLQALRNQLnSQR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1401 LQEAE---ENTEASNSKCASLEK--TKQ-RLQGEVDDLM------LDLERANTACATLDKKQ-RNFDKVLAEWKQKLDES 1467
Cdd:PRK10929 236 QREAEralESTELLAEQSGDLPKsiVAQfKINRELSQALnqqaqrMDLIASQQRQAASQTLQvRQALNTLREQSQWLGVS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1468 QAELEA--AQ-------KESRSLSTEIFKMRNA---YEevvDQLETLRRENKNLQEEISDLT---EQIAE----TGKNL- 1527
Cdd:PRK10929 316 NALGEAlrAQvarlpemPKPQQLDTEMAQLRVQrlrYE---DLLNKQPQLRQIRQADGQPLTaeqNRILDaqlrTQRELl 392
|
410 420 430
....*....|....*....|....*....|...
gi 124486959 1528 ---------QEVEKTKKQVEQekSDLQAALEEV 1551
Cdd:PRK10929 393 nsllsggdtLILELTKLKVAN--SQLEDALKEV 423
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1456-1720 |
1.40e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1456 VLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKK 1535
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1536 QVEQEKSDLQAALEEvegsLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDA 1615
Cdd:COG4372 105 SLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1616 LRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVA 1695
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260
....*....|....*....|....*
gi 124486959 1696 LEQTERTRRLSEQELLDSSDRVQLL 1720
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALEL 285
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1387-1708 |
1.43e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.60 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1387 TEELEEAKKKLA---QRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACatldkkqRNFDKVLAEWKQK 1463
Cdd:pfam19220 40 LRELPQAKSRLLeleALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAAL-------REAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1464 LDESQAELEAAQKEsrsLSTEifkmrnayeevVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSD 1543
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAE-----------TEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1544 LQAALEEV--------------EGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIK--RNSQRA-VEAMQSVLD 1606
Cdd:pfam19220 179 LQALSEEQaaelaeltrrlaelETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRaeRASLRMkLEALTARAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1607 AeirsrndALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQ 1686
Cdd:pfam19220 259 A-------TEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLT 331
|
330 340
....*....|....*....|...
gi 124486959 1687 EELEEMKVALEQ-TERTRRLSEQ 1708
Cdd:pfam19220 332 KALAAKDAALERaEERIASLSDR 354
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1488-1913 |
1.47e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1488 MRNAYE--EVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQeksDLQAA---LEEVEGSLEHEEsKI 1562
Cdd:COG3096 274 MRHANErrELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQ---DYQAAsdhLNLVQTALRQQE-KI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1563 LRVQLELSqvksELdrkvTEKDEEIEQIkrnsqrAVEAMQSVLDAEIRSRNdalrlkkkMEGDLNEMEIQLshANRQVAE 1642
Cdd:COG3096 350 ERYQEDLE----EL----TERLEEQEEV------VEEAAEQLAEAEARLEA--------AEEEVDSLKSQL--ADYQQAL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1643 TQKHLRTVQGQlkdsqlhldDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRvqllHS 1722
Cdd:COG3096 406 DVQQTRAIQYQ---------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAA----RR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1723 QNtslintKKKLEAdLAQCQAEVENSiqesrNAEEKAKKAITDAammaeelkkeqdtsahleRMKKNLEQTVKDLQHRLD 1802
Cdd:COG3096 473 QF------EKAYEL-VCKIAGEVERS-----QAWQTARELLRRY------------------RSQQALAQRLQQLRAQLA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1803 EAEQLALKggkkqiqklEARVRELESELDAEQKRgaealkgahkyerkvkemTYQAEEDrknilrLQDLVDKLQAkvksy 1882
Cdd:COG3096 523 ELEQRLRQ---------QQNAERLLEEFCQRIGQ------------------QLDAAEE------LEELLAELEA----- 564
|
410 420 430
....*....|....*....|....*....|.
gi 124486959 1883 krQAEEAEEQANTQLSRCRRVQHELEEAEER 1913
Cdd:COG3096 565 --QLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1262-1484 |
1.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1262 EIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAhalqssr 1341
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1342 hdcDLLREQYEEEQE-----------------GKAELQRALSKANSEVAQwrtkyetDAIQRTEELEEAKKKLAQRLQEA 1404
Cdd:COG3883 90 ---ERARALYRSGGSvsyldvllgsesfsdflDRLSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1405 EENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTE 1484
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
864-1077 |
1.59e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.21 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 864 KEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMdaEERCEGLIKSKIQLEAKVKELNERLEEEEEM----NSE 939
Cdd:pfam15742 113 QEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCILE--KKQLEERIKEASENEAKLKQQYQEEQQKRKLldqnVNE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 940 LVAKKRNLEDKCSSLKR-------DIDDLELTLTKVEKEKHATENKVKNLSEemtaLEETISKLTKEKKSLQEAHQQTLD 1012
Cdd:pfam15742 191 LQQQVRSLQDKEAQLEMtnsqqqlRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKLSSLQQEKEALQEELQQVLK 266
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124486959 1013 DLQVEEDKVNglikinvkleqqtddlegslEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDT 1077
Cdd:pfam15742 267 QLDVHVRKYN--------------------EKHHHHKAKLRRAKDRLVHEVEQRDERIKQLENEI 311
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1743-1938 |
1.61e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1743 AEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQtVKDLQHRLDEAEQLALKGGK----KQIQK 1818
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER---LRREREKAER-YQALLKEKREYEGYELLKEKealeRQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1819 LEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKN-ILRLQDLVDKLQAKVKSYKRQAEEAEEqantql 1897
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEAEIASLERSIAEKER------ 315
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 124486959 1898 srcrrvqhELEEAEERADIAESQVNKLRAKSRDVGGQKMEE 1938
Cdd:TIGR02169 316 --------ELEDAEERLAKLEAEIDKLLAEIEELEREIEEE 348
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1284-1550 |
1.77e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1284 LQTQNGELSHQVEEKESLVS-QLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQ 1362
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1363 ---RALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDL 1432
Cdd:pfam00038 103 ndlVGLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1433 MldlerantacatldkkQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEE 1512
Cdd:pfam00038 183 A----------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260 270
....*....|....*....|....*....|....*....
gi 124486959 1513 ISDLTEQIAETGKNLQE-VEKTKKQVEQEKSDLQAALEE 1550
Cdd:pfam00038 247 LAETEERYELQLADYQElISELEAELQETRQEMARQLRE 285
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1362-1541 |
1.80e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1362 QRALSKANseVAQWRTKYET---DAIQRTEELEEAKKKLAQRLQEAEENTEAS---NSKCASLEKTKQRLQGEVDdlmld 1435
Cdd:PHA02562 207 QRKKNGEN--IARKQNKYDElveEAKTIKAEIEELTDELLNLVMDIEDPSAALnklNTAAAKIKSKIEQFQKVIK----- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1436 LERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQK----------ESRSLSTEIFKMRNAYEEVVDQLETLRRE 1505
Cdd:PHA02562 280 MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTaideleeimdEFNEQSKKLLELKNKISTNKQSLITLVDK 359
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124486959 1506 NKNLQEEISDL-------TEQIAETGKNLQEVEKTKKQVEQEK 1541
Cdd:PHA02562 360 AKKVKAAIEELqaefvdnAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
839-1412 |
1.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 839 KIKPLLKSAEAE-KEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQS---ETENLMDAEERCEGLIK 914
Cdd:PRK01156 170 KLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 915 SKIQLEAKVKELNERLEEEEEMNSEL--------------VAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVK 980
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNNYYkeleerhmkiindpVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 981 NLSEemtaLEETISKLTKEKKSLQEAHQQtLDDLQVEEDKVNGLIKinvKLEQQTDDLEGSLEQEKKLRADLERVKRKLE 1060
Cdd:PRK01156 330 KLSV----LQKDYNDYIKKKSRYDDLNNQ-ILELEGYEMDYNSYLK---SIESLKKKIEEYSKNIERMSAFISEILKIQE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1061 GDLKMSQESIMDLENDTQQleeklkkKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQR 1140
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQD-------ISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1141 SDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDnlqrvkqK 1220
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHD-------K 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1221 LEKEKSELK-MEIDDMASNIETVSKSKSNMERM-CRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEK 1298
Cdd:PRK01156 548 YEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1299 ESLVSQLTKSKQALTQQLEELKRQLeEETKAKNALAHALQSSRHDcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTK 1378
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKI-DNYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
570 580 590
....*....|....*....|....*....|....
gi 124486959 1379 YETDaIQRTEELEEAKKKLAQRLQEAEENTEASN 1412
Cdd:PRK01156 704 IEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1261-1496 |
2.18e-04 |
|
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: 46.38 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1261 NEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEekeSLVSQLTKSKQALtQQLEelkRQLEEETKAKNALAHALQSS 1340
Cdd:pfam09726 419 QELRSQISSLTSLERSLKSELGQLRQENDLLQTKLH---NAVSAKQKDKQTV-QQLE---KRLKAEQEARASAEKQLAEE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1341 RhdcdllreQYEEEQEGKAELQRALSKANSevaqwrtKYETDAI-QRTEELEEAKKKLAQRLQEAEENTEASNSKCASLE 1419
Cdd:pfam09726 492 K--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1420 KTKQRlQGEVDDLMLDLErantacATLDKKQRNFDKVLAEWKQKLD------ESQAELEAAQKESRSLSTEIFKMRNAYE 1493
Cdd:pfam09726 557 KYKES-EKDTEVLMSALS------AMQDKNQHLENSLSAETRIKLDlfsalgDAKRQLEIAQGQIYQKDQEIKDLKQKIA 629
|
...
gi 124486959 1494 EVV 1496
Cdd:pfam09726 630 EVM 632
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1493-1592 |
2.28e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1493 EEVVDQLeTLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQ---EKSDLQAALEEVEGSLEHEESKILRVQLEL 1569
Cdd:COG2433 379 EEALEEL-IEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERleaEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100
....*....|....*....|...
gi 124486959 1570 SQvKSELDRKVTEKDEEIEQIKR 1592
Cdd:COG2433 458 RR-EIRKDREISRLDREIERLER 479
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1573-1766 |
2.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1573 KSELDRKVTEKDEEIEQIKRNSQRAVEAMQSvlDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQvaetqkhlrtvqg 1652
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKLEKR------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1653 qLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALE--QTERTRRLSEQELLDSSDRVQLLhsqntsLINT 1730
Cdd:PRK12704 91 -LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEelIEEQLQELERISGLTAEEAKEIL------LEKV 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 124486959 1731 KKKLEADLAQCQAEVENSIQEsrNAEEKAKKAITDA 1766
Cdd:PRK12704 164 EEEARHEAAVLIKEIEEEAKE--EADKKAKEILAQA 197
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1131-1394 |
2.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1131 TVRAKIEKQRSDLARELEEISERLEEAsgatsaqiemnkkrESEFQKLRRDLEEATLQHEATAATLRKKHADtVAELGEQ 1210
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAA--------------QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1211 IDNLQrvkQKLEKEKSELKMEIDDM------ASNIETVSKSKSnmermcrsVEDQFNEIKAKD---DQQTQLIHDLNMQK 1281
Cdd:COG3883 74 IAEAE---AEIEERREELGERARALyrsggsVSYLDVLLGSES--------FSDFLDRLSALSkiaDADADLLEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1282 ARLQTQNGELSHQVEEKEslvsqltkskqALTQQLEELKRQLEEETKAKNALAHALQSSRhdcDLLREQYEEEQEGKAEL 1361
Cdd:COG3883 143 AELEAKKAELEAKLAELE-----------ALKAELEAAKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAELAAA 208
|
250 260 270
....*....|....*....|....*....|...
gi 124486959 1362 QRALSKANSEVAQWRTKYETDAIQRTEELEEAK 1394
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1176-1351 |
2.72e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 45.62 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1176 QKLRRDLEEatlQHEATAATLRKKhadtvaelgeqIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSksnmermcrs 1255
Cdd:pfam03148 232 EQTANDLRA---QADAVNFALRKR-----------IEETEDAKNKLEWQLKKTLQEIAELEKNIEALEKA---------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1256 vedqfneIKAKDDQ----QTQL---IHDLNMQKARLQTQNG---ELSHQVEEKESLVSQLTKSKQALtQQLEELKRQLEE 1325
Cdd:pfam03148 288 -------IRDKEAPlklaQTRLenrTYRPNVELCRDEAQYGlvdEVKELEETIEALKQKLAEAEASL-QALERTRLRLEE 359
|
170 180
....*....|....*....|....*.
gi 124486959 1326 ETKAKNalaHALQSSRHDCDLLREQY 1351
Cdd:pfam03148 360 DIAVKA---NSLFIDREKCMGLRKRL 382
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1060 |
2.77e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 844 LKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERcegliksKIQLEAKV 923
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-------IKSIEKEI 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 924 KELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSL 1003
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1004 QEAHQQ---------TLDDLQVEEDKVNGLIK----INVKLEQQTDDLEGSLEQEKKLRADLERVKRKLE 1060
Cdd:TIGR02169 937 EDPKGEdeeipeeelSLEDVQAELQRVEEEIRalepVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1241 |
2.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 845 KSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVK 924
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 925 ELNERleeeeemnselVAKKRNL--EDKCSSLKRDIDDLELTLTKVEKEKhatenKVKNLSEEMTALEETISKLtkekks 1002
Cdd:PRK02224 437 TARER-----------VEEAEALleAGKCPECGQPVEGSPHVETIEEDRE-----RVEELEAELEDLEEEVEEV------ 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1003 lqEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEE 1082
Cdd:PRK02224 495 --EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1083 KLKKKEFEMSQLQTRIDdeqvlSLQlqkKIKELQARteeleeeieaehtvRAKIEKQRSDLARELEEISERLEEASGATS 1162
Cdd:PRK02224 573 EVAELNSKLAELKERIE-----SLE---RIRTLLAA--------------IADAEDEIERLREKREALAELNDERRERLA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1163 AQIEMNKKRESEFQKLRrdLEEATLQHEaTAATLRKKHADTVAELGEQIDNLQR----VKQKLEkEKSELKMEIDDMASN 1238
Cdd:PRK02224 631 EKRERKRELEAEFDEAR--IEEAREDKE-RAEEYLEQVEEKLDELREERDDLQAeigaVENELE-ELEELRERREALENR 706
|
...
gi 124486959 1239 IET 1241
Cdd:PRK02224 707 VEA 709
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1494-1710 |
3.38e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1494 EVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDlQAALEEVEGSLEHEESKILRVQLELSQVK 1573
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1574 SEL-------DRKVTEKDE------EIEQIKRNSQRAVEAM----QSVLDAEIRSRNDALRLKKK-MEG-----DLneME 1630
Cdd:PRK11281 149 SQLvslqtqpERAQAALYAnsqrlqQIRNLLKGGKVGGKALrpsqRVLLQAEQALLNAQNDLQRKsLEGntqlqDL--LQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1631 IQLSHANRQVAETQKHLRTVQG-----QLKDSQLHLDDAQRSNEDLKEQlaiverRNGLLQEELEE----MKVALEQTER 1701
Cdd:PRK11281 227 KQRDYLTARIQRLEHQLQLLQEainskRLTLSEKTVQEAQSQDEAARIQ------ANPLVAQELEInlqlSQRLLKATEK 300
|
....*....
gi 124486959 1702 TRRLSEQEL 1710
Cdd:PRK11281 301 LNTLTQQNL 309
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1398-1767 |
3.50e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1398 AQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQrnfdkvLAEWKQKLDESQAELEAAQKE 1477
Cdd:PLN02939 63 SKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ------QTNSKDGEQLSDFQLEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1478 SRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEH 1557
Cdd:PLN02939 137 IQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGAT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1558 EESKILRVQLELSQVKSEldrKVTEKDEeieqikrnsqraVEAMQSVLDAEIRSRNDALRLKKK---MEGDLNEMEIQLS 1634
Cdd:PLN02939 217 EGLCVHSLSKELDVLKEE---NMLLKDD------------IQFLKAELIEVAETEERVFKLEKErslLDASLRELESKFI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1635 HANRQVAEtqkhLRTVQ-----GQLKDSQLHLDDAQrsneDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRrlseqe 1709
Cdd:PLN02939 282 VAQEDVSK----LSPLQydcwwEKVENLQDLLDRAT----NQVEKAALVLDQNQDLRDKVDKLEASLKEANVSK------ 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1710 llDSSDRVQLLHSQntslintKKKLEADLAQCQAEV-------ENSIQE-----SRNAEEKAKKAITDAA 1767
Cdd:PLN02939 348 --FSSYKVELLQQK-------LKLLEERLQASDHEIhsyiqlyQESIKEfqdtlSKLKEESKKRSLEHPA 408
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1101-1607 |
3.84e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1101 EQVLSL-QLQKKIKELQARTEELEEEIEAehtVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKReSEFQKLR 1179
Cdd:PRK10246 301 EQSAALaHTRQQIEEVNTRLQSTMALRAR---IRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWR-AQFSQQT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1180 RDLEEATLQHEATAATLRKKHA----------DTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNM 1249
Cdd:PRK10246 377 SDREQLRQWQQQLTHAEQKLNAlpaitltltaDEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1250 ERMCRSVEDQFNEIKAKDD---------QQTQLIHDLNMQKARLQT---------------------------------- 1286
Cdd:PRK10246 457 TQRNAALNEMRQRYKEKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpaveayqalepgvnqsrldale 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1287 ---------------QNGELSHQVEEKESLVSQLTKSKQALTQQLEELkrqleeetkaKNALAHALQSSRHDCDLLREQY 1351
Cdd:PRK10246 537 kevkklgeegaalrgQLDALTKQLQRDESEAQSLRQEEQALTQQWQAV----------CASLNITLQPQDDIQPWLDAQE 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1352 EEEQE-----GKAELQRALSKANSEVAQWRTKYET------DAIQR-----TEELEEA-----KKKLAQRLQEAEENTEA 1410
Cdd:PRK10246 607 EHERQlrllsQRHELQGQIAAHNQQIIQYQQQIEQrqqqllTALAGyaltlPQEDEEAswlatRQQEAQSWQQRQNELTA 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1411 SNSKCASLEKTKQRL------QGEVDDLMLD-LERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLST 1483
Cdd:PRK10246 687 LQNRIQQLTPLLETLpqsddlPHSEETVALDnWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQ 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1484 EIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQevektkkQVEQEKSDLQAALEEvegsleheeskil 1563
Cdd:PRK10246 767 QAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ-------QHRPDGLDLTVTVEQ------------- 826
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 124486959 1564 rVQLELSQVKSELDRKVTEKDEEIEQIKR---NSQRAVEAMQSVLDA 1607
Cdd:PRK10246 827 -IQQELAQLAQQLRENTTRQGEIRQQLKQdadNRQQQQALMQQIAQA 872
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1776-1932 |
3.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1776 EQDTSAHLERMKKNLEQtvkdlqhrLDEAEQLALKGgKKQIQKLEaRVRELESELDA--EQKRGAEALKGAHKY---ERK 1850
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYAAarERLAELEYLRAALRLwfaQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1851 VKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQ-ANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSR 1929
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
...
gi 124486959 1930 DVG 1932
Cdd:COG4913 370 ALG 372
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1344-1561 |
3.95e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1344 CDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQ 1423
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1424 RLQGEVDDLM------LDLERANT------ACATLDKKQrnfdkvLAEWKQKLDESQAELEAAQKESRSLSteIFKMRNA 1491
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLLLGfkyvsvFVGTVPEDK------LEELKLESDVENVEYISTDKGYVYVV--VVVLKEL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124486959 1492 YEEVVDQLETLRRENKNL------QEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVegsLEHEESK 1561
Cdd:PRK05771 190 SDEVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY---LEIELER 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1294-1551 |
4.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1294 QVEEKESLVSQLTKSKQALTQQLEELKRQLEEetkaknalahalqssrhdcdlLREQYEEEQEGKAELQRALSKANSEVA 1373
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEE---------------------LNEEYNELQAELEALQAEIDKLQAEIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1374 QwrtkyetdaiqRTEELEEAKKKLAQRLQEAEENTEASN---------------SKCASLEKTKQRLQGEVDDLMLDLER 1438
Cdd:COG3883 76 E-----------AEAEIEERREELGERARALYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1439 ANTACATLDKKQRNFDKVLAEwkqkLDESQAELEAAQKESRSLsteifkmrnayeevvdqLETLRRENKNLQEEISDLTE 1518
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAE----LEAAKAELEAQQAEQEAL-----------------LAQLSAEEAAAEAQLAELEA 203
|
250 260 270
....*....|....*....|....*....|...
gi 124486959 1519 QIAETGKNLQEVEKTKKQVEQEKSDLQAALEEV 1551
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1441-1590 |
4.90e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1441 TACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEifkmrnayeevvdQLETLRRENKNLQEEISDLTEQi 1520
Cdd:COG0542 397 EAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFE-------------RLAELRDELAELEEELEALKAR- 462
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1521 aetgknlqevEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEkdEEIEQI 1590
Cdd:COG0542 463 ----------WEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--EDIAEV 520
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
841-1176 |
5.18e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 841 KPLLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSlLQEKNDLQLQVQSETENLmdAEERCEGLikSKIQLE 920
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKA-RQAEMDRQAAIYAEQERM--AMEREREL--ERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 921 AKVKELNERLEEEEEMNselVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALE----ETISKL 996
Cdd:pfam17380 357 ERKRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEqiraEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 997 TKEKKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRK-LEGDLKMSQESIMDLEN 1075
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEER 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1076 DTQqleeklkKKEFEMSQLQTRIDDEQvlslqlQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLareleEISERLE 1155
Cdd:pfam17380 514 KRK-------LLEKEMEERQKAIYEEE------RRREAEEERRKQQEMEERRRIQEQMRKATEERSRL-----EAMERER 575
|
330 340
....*....|....*....|.
gi 124486959 1156 EasgaTSAQIEMNKKRESEFQ 1176
Cdd:pfam17380 576 E----MMRQIVESEKARAEYE 592
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1133-1365 |
5.73e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1133 RAKIEKQRSDLARELEEISERLEEasgatsaqiEMNKKR--ESEFQKLRRDLEEATLQHeataATLRKKhadtVAELGEQ 1210
Cdd:pfam00038 70 RARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLAR----VDLEAK----IESLKEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1211 IDNLqrvKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQ---------TQLIHDLNMQK 1281
Cdd:pfam00038 133 LAFL---KKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEaeewyqsklEELQQAAARNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1282 ARLQTQNGELS---HQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQssrhdcdllreqyEEEQEGK 1358
Cdd:pfam00038 210 DALRSAKEEITelrRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELE-------------AELQETR 276
|
....*..
gi 124486959 1359 AELQRAL 1365
Cdd:pfam00038 277 QEMARQL 283
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
989-1286 |
5.83e-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: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 989 LEETISKL------TKEKKSLQEAHQQTLDDLQVEEDKVNGLIKINVK----------------------LEQQTDDLEG 1040
Cdd:COG3206 96 LERVVDKLnldedpLGEEASREAAIERLRKNLTVEPVKGSNVIEISYTspdpelaaavanalaeayleqnLELRREEARK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1041 SL----EQEKKLRADLERVKRKLEgDLKmSQESIMDLENDTQQLEEKlkkkefeMSQLQTRIddeqvlsLQLQKKIKELQ 1116
Cdd:COG3206 176 ALefleEQLPELRKELEEAEAALE-EFR-QKNGLVDLSEEAKLLLQQ-------LSELESQL-------AEARAELAEAE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1117 ARteeleeeieaehtvrakiekqrsdlareLEEISERLEEASGATSAQIEmnkkrESEFQKLRRDLEEATLQHEATAATL 1196
Cdd:COG3206 240 AR----------------------------LAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1197 RKKHADtVAELGEQIDNL-QRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERmcrsvedQFNEIKAKDDQQTQLIH 1275
Cdd:COG3206 287 TPNHPD-VIALRAQIAALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA-------RLAELPELEAELRRLER 358
|
330
....*....|.
gi 124486959 1276 DLNMQKARLQT 1286
Cdd:COG3206 359 EVEVARELYES 369
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1135-1398 |
6.63e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1135 KIEKQRSdLARELEEISERLEEASG-ATSAQIEMNKKRESEFQKLRRDLEEATLQHEataatlrkkhaDTVAELGEQIDN 1213
Cdd:PRK05771 44 RLRKLRS-LLTKLSEALDKLRSYLPkLNPLREEKKKVSVKSLEELIKDVEEELEKIE-----------KEIKELEEEISE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1214 LQRVKQKLEKEKSELK------MEIDDMASN----IETVSKSKSNMERMcRSVEDQFNEIKAKDDQQTQLIHDLNMQKAr 1283
Cdd:PRK05771 112 LENEIKELEQEIERLEpwgnfdLDLSLLLGFkyvsVFVGTVPEDKLEEL-KLESDVENVEYISTDKGYVYVVVVVLKEL- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1284 LQTQNGEL-SHQVEEKEslvsqlTKSKQALTQQLEELKRQLEEETKAKNALAHALqssrhdCDLLREQYEEEQEGKAELQ 1362
Cdd:PRK05771 190 SDEVEEELkKLGFERLE------LEEEGTPSELIREIKEELEEIEKERESLLEEL------KELAKKYLEELLALYEYLE 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124486959 1363 RALSKANSEVAQWRTKYeTDAIQ------RTEELEEAKKKLA 1398
Cdd:PRK05771 258 IELERAEALSKFLKTDK-TFAIEgwvpedRVKKLKELIDKAT 298
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1575-1926 |
7.08e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1575 ELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQL 1654
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1655 KDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKL 1734
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1735 EADLAQCQAEVENSIQEsrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKK 1814
Cdd:COG4372 163 QEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1815 QIQKLEARVRELESELDAEQKRGAEALKGAHKYER-KVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQA 1893
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEeELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 124486959 1894 NTQLSRCRRVQHELEEAEERADIAESQVNKLRA 1926
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1389-1708 |
7.99e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1389 ELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQ 1468
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1469 AELEAAQKESRSLSTEifkmrnaYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAAL 1548
Cdd:COG4372 94 AELAQAQEELESLQEE-------AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1549 EEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKmegDLNE 1628
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL---DALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1629 MEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQ 1708
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
918-1347 |
8.47e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 918 QLEAKVKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLT 997
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 998 KEKKSL---QEAHQQTLDDLqveEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLE 1074
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1075 NDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQarteeleeeieaehtvrAKIEKQRSdlARELEEISERL 1154
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE-----------------ALLEELRS--LQERLNASERK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1155 EEASGATSAQIEMNKKR-ESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEL-KMEi 1232
Cdd:pfam07888 253 VEGLGEELSSMAAQRDRtQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRLE- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1233 ddmasniETVSKSKsnMERMCRSVEDQfneiKAKDDQQTQlihdLNMQKARLQTQNGELSHQVEEKEslvsQLTKSKQAL 1312
Cdd:pfam07888 332 -------ERLQEER--MEREKLEVELG----REKDCNRVQ----LSESRRELQELKASLRVAQKEKE----QLQAEKQEL 390
|
410 420 430
....*....|....*....|....*....|....*
gi 124486959 1313 TQQLEELKRQLEEETKAKNALAHALQSSRHDCDLL 1347
Cdd:pfam07888 391 LEYIRQLEQRLETVADAKWSEAALTSTERPDSPLS 425
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1600-1767 |
8.97e-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: 42.99 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1600 AMQSVLDA-----EIRSRNDALR-LKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKE 1673
Cdd:COG1579 1 AMPEDLRAlldlqELDSELDRLEhRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1674 QLAIVerRNgllQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESR 1753
Cdd:COG1579 81 QLGNV--RN---NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....
gi 124486959 1754 NAEEKAKKAITDAA 1767
Cdd:COG1579 156 AELEELEAEREELA 169
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1382-1615 |
9.68e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.06 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1382 DAIQRTEELEEAKKKLAQRLQEAEEN---TEASNSKCASLEKTKQRLQGEVDDLMLDLERANTAcATLDKKQRNFDKVLA 1458
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLldkIDASKQRAAAYQKALDDAPAELRELRQELAALQAK-AEAAPKEILASLSLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1459 EWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLEtlrrENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVE 1538
Cdd:pfam12795 82 ELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLS----EARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1539 QEKSDLQAALEEVEGSLEHEESKILRVQLELsqvkseLDRKVTEKDEEIEQIKR--NSQRAVEAMQSVLDAEIRSRNDA 1615
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLLKARRDL------LTLRIQRLEQQLQALQEllNEKRLQEAEQAVAQTEQLAEEAA 230
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1299-1599 |
9.71e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.23 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1299 ESLVSQLTKSKQALTQQLEELKRQLEEETKAKN-ALAHALQSSR----HDCDLLREQYEEE--QEGKAELQRALSKANSE 1371
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNvALNKKLSDIKteylYELNVLKEKSEAEltSKTKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1372 VAQWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLML---------DLERANTA 1442
Cdd:NF033838 134 TLEPGKKVA----EATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELvkeeakeprDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1443 CATLDKKQRNFDKVLaewKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEE----------VVDQLETLRRENKNLQEE 1512
Cdd:NF033838 210 KAKVESKKAEATRLE---KIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQdkpkrrakrgVLGEPATPDKKENDAKSS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1513 ISDLTEQ------------IAETGKNLQEVEK----------------TKKQVEQEKSDLQAALEEVEGSLEHEESKILR 1564
Cdd:NF033838 287 DSSVGEEtlpspslkpekkVAEAEKKVEEAKKkakdqkeedrrnyptnTYKTLELEIAESDVKVKEAELELVKEEAKEPR 366
|
330 340 350
....*....|....*....|....*....|....*
gi 124486959 1565 VQLELSQVKSELDRKVTEKdEEIEQIKRNSQRAVE 1599
Cdd:NF033838 367 NEEKIKQAKAKVESKKAEA-TRLEKIKTDRKKAEE 400
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1311 |
9.81e-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: 43.60 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1066 SQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARteeleeeieaehtvRAKIEKQRSDLAR 1145
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR--------------IRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1146 ELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLqheataatlrkKHADTVAELGEQIDNLQRVKQKLEKEK 1225
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL-----------LSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1226 SELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQL 1305
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*.
gi 124486959 1306 TKSKQA 1311
Cdd:COG4942 233 EAEAAA 238
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1139-1441 |
1.01e-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: 44.18 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1139 QRSDLARELEEISERLEEASGATSAQIEMNKKResefQKLRRDLEEatLQHEATAATLRKKHADTVAELGEQIDNLQRVK 1218
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKS----IDIKKATES--LEEQLAAAEAEQELEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1219 QKLEKEKSELKMEIDDMASNIETVSKSKSNMERMcRSVEDQFNEIKAKDDQQTQ--------LIHDLNMQKARLQTQNGE 1290
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSKSSEEL-DSFKDTIESTKESLDEIPQnqrgyaqeILATLEDTLKAADRQIEE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1291 LSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAK-----NALAHALQSSRHDCDLLREQYE--------EEQEG 1357
Cdd:COG5185 425 LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRleeayDEINRSVRSKKEDLNEELTQIEsrvstlkaTLEKL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1358 KAELQRALSKANSEVaQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLE 1437
Cdd:COG5185 505 RAKLERQLEGVRSKL-DQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQ 583
|
....
gi 124486959 1438 RANT 1441
Cdd:COG5185 584 QARE 587
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1095-1364 |
1.02e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.86 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1095 QTRIDDEQVLSLqLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSD-LARELEEISERLEEASGATSAQIEMNKKRES 1173
Cdd:pfam05667 197 QPSSRASVVPSL-LERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRkRTKLLKRIAEQLRSAALAGTEATSGASRSAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1174 EFQKL----------RRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVs 1243
Cdd:pfam05667 276 DLAELlssfsgssttDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQEL- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1244 ksKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARL----QTQNgelshQVEEKESLVSQLTKSKQALTQQLEEL 1319
Cdd:pfam05667 355 --EKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLdllpDAEE-----NIAKLQALVDASAQRLVELAGQWEKH 427
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 124486959 1320 KRQLEEETKA-KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRA 1364
Cdd:pfam05667 428 RVPLIEEYRAlKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQK 473
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1310-1717 |
1.05e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1310 QALTQQLEELKRQLEEetkaknalaHALQSSRHdcdllREQYEEEQEGKAELQRALSKANsevaqwrTKYETDAIQRTEE 1389
Cdd:COG3096 839 AALRQRRSELERELAQ---------HRAQEQQL-----RQQLDQLKEQLQLLNKLLPQAN-------LLADETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1390 LEEAkkklAQRLQEAEENTEASNSKCASLEKTKQRLQG---EVDDLMLDLERANTACATLDKKQRNFDKVLA-------- 1458
Cdd:COG3096 898 LREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfsye 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1459 EWKQKLDES-------QAELEAAQKEsRSLSTEifKMRNAYEEVVDQLETL-----RRENKnlQEEISDLTEQIAETGkn 1526
Cdd:COG3096 974 DAVGLLGENsdlneklRARLEQAEEA-RREARE--QLRQAQAQYSQYNQVLaslksSRDAK--QQTLQELEQELEELG-- 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1527 LQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQvkseLDRKVTEKDEEIEQIKRNSQRAVEAMQSVld 1606
Cdd:COG3096 1047 VQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS----LQKRLRKAERDYKQEREQVVQAKAGWCAV-- 1120
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1607 aeirsrndaLRLKKK--MEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQlHLDDAQRSNEDLKEQLAIV------ 1678
Cdd:COG3096 1121 ---------LRLARDndVERRLHRRELAYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPERKVqfyiav 1190
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 124486959 1679 -----ER-RNGLLQ-----EELEEMKVALEQ-TER-TRRlsEQELLDSSDRV 1717
Cdd:COG3096 1191 yqhlrERiRQDIIRtddpvEAIEQMEIELARlTEElTSR--EQKLAISSESV 1240
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1454-1589 |
1.05e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 42.99 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1454 DKVLAEWKQKLDESQAeleaAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKT 1533
Cdd:pfam11932 16 DQALDLAEKAVAAAAQ----SQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERT 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1534 KKQVE----------------------QEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQ 1589
Cdd:pfam11932 92 ERELVplmlkmldrleqfvaldlpfllEERQARLARLRELMDDADVSLAEKYRRILEAYQVEAEYGRTIEVYQGELEL 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1109-1609 |
1.10e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1109 QKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQ-----IEMNKKRESEFQKLRRDLE 1183
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKalqtvIEMKDTKISSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1184 EATLQHEATAATLRKKHADTVAELgEQIDN--------LQRVKQKLEKEKSEL-----KMEI-----DDMASNIETVSKS 1245
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQM-EVYKShskfmknkIDQLKQELSKKESELlalqtKLETltnqnSDCKQHIEVLKES 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1246 KSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQ----TQNGELSH---QVEEKESLVSQLTKSKQALTQQLEE 1318
Cdd:pfam10174 333 LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTeeksTLAGEIRDlkdMLDVKERKINVLQKKIENLQEQLRD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1319 LKRQLEE--------ETKAKNA------LAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAI 1384
Cdd:pfam10174 413 KDKQLAGlkervkslQTDSSNTdtalttLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1385 QRTEELEEAKK----------KLAQRLQEAEENTEASNSKCASLEKTKQRLQgevddlmlDLERANTACATLDKKQRNFD 1454
Cdd:pfam10174 493 EKESSLIDLKEhasslassglKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1455 KVLAEWKQKLDESQAELEAAQKESRSLSTEifkmRNAYEEVVDQLETLR-RENKNLQEEISDL-TEQIAETGKNLQEVEK 1532
Cdd:pfam10174 565 QEVARYKEESGKAQAEVERLLGILREVENE----KNDKDKKIAELESLTlRQMKEQNKKVANIkHGQQEMKKKGAQLLEE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1533 TKKQVEQEKSD--------LQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSV 1604
Cdd:pfam10174 641 ARRREDNLADNsqqlqleeLMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAISE 720
|
....*
gi 124486959 1605 LDAEI 1609
Cdd:pfam10174 721 KDANI 725
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1778-1932 |
1.18e-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: 42.71 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1778 DTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYER--KVKEMT 1855
Cdd:pfam00261 12 EAEERLKEAMKKLEEAEKRAEKAEAEVAAL-----NRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrKVLENR 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124486959 1856 YQAEEDRknilrlqdlVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVG 1932
Cdd:pfam00261 87 ALKDEEK---------MEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1037-1880 |
1.20e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1037 DLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQleeklkkkefeMSQLQTRIDDEQV----LSLQLQKKI 1112
Cdd:TIGR01612 541 EIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKD-----------LFDKYLEIDDEIIyinkLKLELKEKI 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1113 KELQARTEELeeeieaehtvrakieKQRSDLARELEEISERLEEASGATSAQI-EMNKKRESEFQKLRRDLEEAtlqHEA 1191
Cdd:TIGR01612 610 KNISDKNEYI---------------KKAIDLKKIIENNNAYIDELAKISPYQVpEHLKNKDKIYSTIKSELSKI---YED 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1192 TAATLRKKHADTVAElgEQIDNLQRvKQKLEKEKSELKMEIDDMAS-NIETVSKSKSNMERMCRSVEDQFNEIKAKddQQ 1270
Cdd:TIGR01612 672 DIDALYNELSSIVKE--NAIDNTED-KAKLDDLKSKIDKEYDKIQNmETATVELHLSNIENKKNELLDIIVEIKKH--IH 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1271 TQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLE-EETKAKNALAHALQSSRHDCDLLRE 1349
Cdd:TIGR01612 747 GEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINiDNIKDEDAKQNYDKSKEYIKTISIK 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1350 QYEEEQ---EGKAELQRALSKANSEVA---QWRTKYETDAIQRTEELEEAKKKLA-QRLQEAEENTEAS----NSKCASL 1418
Cdd:TIGR01612 827 EDEIFKiinEMKFMKDDFLNKVDKFINfenNCKEKIDSEHEQFAELTNKIKAEISdDKLNDYEKKFNDSksliNEINKSI 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1419 EKTKQRLQ--GEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQA-ELEAAQKESRSLSTEIFKMRNAYEEV 1495
Cdd:TIGR01612 907 EEEYQNINtlKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLiEKSYKDKFDNTLIDKINELDKAFKDA 986
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1496 vdQLETLRRENKNLQEEISDLTEQIAETGKNL-----QEVEKTKKQVEQEKSDLQAALEEVE-------GSLEHEESKIL 1563
Cdd:TIGR01612 987 --SLNDYEAKNNELIKYFNDLKANLGKNKENMlyhqfDEKEKATNDIEQKIEDANKNIPNIEiaihtsiYNIIDEIEKEI 1064
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1564 RVQLEL--SQVKSELDRKVTEKDEEIEQIKRN--SQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQ 1639
Cdd:TIGR01612 1065 GKNIELlnKEILEEAEINITNFNEIKEKLKHYnfDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENY 1144
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1640 VAETQKHLRTVQgQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLqeelEEMKVALEQTERTRRlsEQELLDSSDRVQL 1719
Cdd:TIGR01612 1145 IDEIKAQINDLE-DVADKAISNDDPEEIEKKIENIVTKIDKKKNIY----DEIKKLLNEIAEIEK--DKTSLEEVKGINL 1217
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1720 LHSQNTSLI------NTKKKLEADLAQCQAEVEN--SIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLE 1791
Cdd:TIGR01612 1218 SYGKNLGKLflekidEEKKKSEHMIKAMEAYIEDldEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD 1297
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1792 QTVKDLQHRL-----DEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAE-----ALKGAHKYERKVKEMTYQAEED 1861
Cdd:TIGR01612 1298 ENISDIREKSlkiieDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEEN 1377
|
890
....*....|....*....
gi 124486959 1862 RKNILRLQDLVDKLQAKVK 1880
Cdd:TIGR01612 1378 NKNIKDELDKSEKLIKKIK 1396
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1416-1757 |
1.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1416 ASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEV 1495
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1496 VDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSE 1575
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1576 LDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLK 1655
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1656 DSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLE 1735
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|..
gi 124486959 1736 ADLAQCQAEVENSIQESRNAEE 1757
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVA 368
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1256-1479 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1256 VEDQFNEIKAK-DDQQTQLihdlnmqkARLQTQNGELSHQvEEKESLVSQLTkskqALTQQLEELKRQLEEETKAKNALA 1334
Cdd:COG3206 180 LEEQLPELRKElEEAEAAL--------EEFRQKNGLVDLS-EEAKLLLQQLS----ELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1335 HALQSSRHDCDL---------LREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdaiqrtEELEEAKKKLAQR----L 1401
Cdd:COG3206 247 AQLGSGPDALPEllqspviqqLRAQLAELEAELAELSARYTPNHPDVIALR-----------AQIAALRAQLQQEaqriL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1402 QEAEENTEASNSKCASLEKTKQRLQGEVDDL------MLDLERantacaTLDKKQRNFDKVLaewkQKLDEsqAELEAAQ 1475
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELpeleaeLRRLER------EVEVARELYESLL----QRLEE--ARLAEAL 383
|
....
gi 124486959 1476 KESR 1479
Cdd:COG3206 384 TVGN 387
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1194-1341 |
1.30e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1194 ATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVsksKSNMERmcrsVEDQFNEIKaKDDQQTQL 1273
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV---EARIKK----YEEQLGNVR-NNKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1274 IHDLNMQKARLQTQN---GELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSR 1341
Cdd:COG1579 95 QKEIESLKRRISDLEdeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1370-1582 |
1.47e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.77 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1370 SEVAQWRTKYETDaiqrTEELEeaKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQ-----GEVDDLMLDLERANTACA 1444
Cdd:pfam15294 70 SQAEKWHLKLQAD----ISELE--NRELLEQIAEFEEREFTSSNKKPNFELNKPKLEplnegGGSALLHMEIERLKEENE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1445 TLDKKQRNFdkvlaewkqkldESQAELEAAQKEsrslsteifKMRNAYEEVVDQLETLRRENKNLQEeISDLTEQIAETG 1524
Cdd:pfam15294 144 KLKERLKTL------------ESQATQALDEKS---------KLEKALKDLQKEQGAKKDVKSNLKE-ISDLEEKMAALK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1525 KNLQevektkkQVEQEKSDLQAALEEVEGSLEHEeskILRVQLELSQVKSELDRKVTE 1582
Cdd:pfam15294 202 SDLE-------KTLNASTALQKSLEEDLASTKHE---LLKVQEQLEMAEKELEKKFQQ 249
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
844-1070 |
1.50e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.61 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 844 LKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMvsllqEKndlQLQVQSETENLMDAEERCEgliKSKIQLEAKV 923
Cdd:pfam18971 596 FNKAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEV-----EK---KLESKSGNKNKMEAKAQAN---SQKDEIFALI 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 924 KELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKH----ATENKVKNLSEEMTAL---EETISKL 996
Cdd:pfam18971 665 NKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNkdfsKAEETLKALKGSVKDLginPEWISKV 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 997 TKEKKSLQEAHQQTLDDL----QVEEDKVNGL--IKINVKLEQQTDDLEGSLEQEKKLrADLERVKRKLeGDLK-MSQES 1069
Cdd:pfam18971 745 ENLNAALNEFKNGKNKDFskvtQAKSDLENSVkdVIINQKVTDKVDNLNQAVSVAKAM-GDFSRVEQVL-ADLKnFSKEQ 822
|
.
gi 124486959 1070 I 1070
Cdd:pfam18971 823 L 823
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
1458-1833 |
1.53e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 43.69 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1458 AEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQV 1537
Cdd:pfam09730 30 AYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYSELEEENISL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1538 EQEKSDLQAALEEVEGsLEHE------ESKILRVQLELS-QVKSELDRKVTEKDEEIE---QIKRNSQRAVEAMQSVLDA 1607
Cdd:pfam09730 110 QKQVSVLKQNQVEFEG-LKHEitrkeeETELLNSQLEEAiRLREIAERQLDEALETLKterEQKNSLRKELSHYMTLNDF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1608 EIRS----RNDALRLKKKMEGDL---NEMEIQLSHANRQVAETQKHLRTVQGQLKD---------------SQLHLDDAQ 1665
Cdd:pfam09730 189 DYVShlsiSLDGLKFSEDEGAGTepnNDGEAMDGGENGGGGLKNSGLDNRTSTPRKsevfppapslvsdllSELNISEIQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1666 RsnedLKEQLAIVERRNGLL-------QEELEEMKVAL-EQTERTRRLSEQelLDSSDRVQLLHSQNTSLINTKKKLEAD 1737
Cdd:pfam09730 269 K----LKQQLIQVEREKVSLlstlqesQKQLEQAKGALsEQQEKVNRLTEN--LEAMRGLQASKERQDALDSEKDRDSHE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1738 LAQcqaEVENSIQESRNAEEKAKKAITDAAMMAEELKKeqdtsahLERMKKNLEQTVKDLQHRLdEAEQLALKGGKKQIQ 1817
Cdd:pfam09730 343 DGD---YYEVDINGPEILECKYRVAVEEAGELREELKA-------LKARYNTLEERYKEEKTRW-EAEAQDLAEKIRQLE 411
|
410
....*....|....*.
gi 124486959 1818 KLEARVRELESELDAE 1833
Cdd:pfam09730 412 KASHQDQERIAHLEKE 427
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1444-1830 |
1.57e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1444 ATLDKKQRNFDKVLAEW---KQKLDESQAELEAAQKESRSLSTEIFKMRNA-YEEVVDQLETLRRENKNLQEEISDLtEQ 1519
Cdd:pfam03528 4 EDLQQRVAELEKENAEFyrlKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAvLQEAQVELDALQNQLALARAEMENI-KA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1520 IAETGKNLQE--VEKTKKQVEQEKSDLQAALEEVEGSLEHEeskilrVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRA 1597
Cdd:pfam03528 83 VATVSENTKQeaIDEVKSQWQEEVASLQAIMKETVREYEVQ------FHRRLEQERAQWNQYRESAEREIADLRRRLSEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1598 VEAmQSVLDAEIRSRNDALRLKK---KMEGDLNEMEIQLSHANRQVAETQKhlrtvqGQLKDSQLHLDDAQRSNEDLKEQ 1674
Cdd:pfam03528 157 QEE-ENLEDEMKKAQEDAEKLRSvvmPMEKEIAALKAKLTEAEDKIKELEA------SKMKELNHYLEAEKSCRTDLEMY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1675 LAIVERRNGLLQEELEEMKVALEQterTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVenSIQESRN 1754
Cdd:pfam03528 230 VAVLNTQKSVLQEDAEKLRKELHE---VCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVL--TSEQLRQ 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1755 AEEKAKKaitdaammAEELKKEQDTSAHLERMKKNLEQTVK--DLQHRLDEAEQLALKGGKKQIQKLEARVRELESEL 1830
Cdd:pfam03528 305 VEEIKKK--------DQEEHKRARTHKEKETLKSDREHTVSihAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDV 374
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
844-1407 |
1.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 844 LKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQV-QSETENLMDAEERCEGLIKSKIQLEAK 922
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 VKELNERLEE----EEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTK 998
Cdd:COG4913 361 RARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 999 EkksLQEAHQQTLDDLQVEEDKVN---GLIKINVKLEQQTDDLEGSL---------------------EQEK-KLRADLE 1053
Cdd:COG4913 441 R---LLALRDALAEALGLDEAELPfvgELIEVRPEEERWRGAIERVLggfaltllvppehyaaalrwvNRLHlRGRLVYE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1054 RVKRKLEGDLKMSQES-----IMDLENDTQQleeklkkkEFEMSQLQTRIDDEQVLSLQ----LQKKI-KELQARTEELE 1123
Cdd:COG4913 518 RVRTGLPDPERPRLDPdslagKLDFKPHPFR--------AWLEAELGRRFDYVCVDSPEelrrHPRAItRAGQVKGNGTR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1124 EEIEAEHTVRAKI------EKQRSDLARELEEISERLEEAsgatSAQIEMNKKRESEFQKLRRDLEEATLQHEAtaatlr 1197
Cdd:COG4913 590 HEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAEYSWD------ 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1198 kkhADTVAELGEQIDNLQRVKQKLEKEKSELkmeiddmasnietvsksksnmermcRSVEDQFNEIKAKDDQQTQLIHDL 1277
Cdd:COG4913 660 ---EIDVASAEREIAELEAELERLDASSDDL-------------------------AALEEQLEELEAELEELEEELDEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1278 NMQKARLQTQNGELSHQVEEKESLVSQLTK-SKQALTQQLEELKRQLEEETKAKnALAHALQSSRHDCDLLREQYEEEQE 1356
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAEDlARLELRALLEERFAAALGDAVER-ELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 1357 GKaeLQRALSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQEAEEN 1407
Cdd:COG4913 791 RA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1294-1568 |
1.67e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1294 QVEEKESLVSQLTKSKQALTQQLEELKRQLEEetkaKNALAHALQSSRhdcDLLREQYEEEQEGKAELQRALSKANSEVA 1373
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDE----LNEELKELAEKR---DELNAQVKELREEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1374 QWRTKyetdAIQRTEELEEAKKKLAQRLQEAEENTEASNSKcASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNF 1453
Cdd:COG1340 75 ELKEE----RDELNEKLNELREELDELRKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1454 D--KVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVE 1531
Cdd:COG1340 150 EkaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 124486959 1532 KTKKQVEQEKSDLQ----AALEEVEGSLEHEESKILRVQLE 1568
Cdd:COG1340 230 EEIIELQKELRELRkelkKLRKKQRALKREKEKEELEEKAE 270
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
1202-1496 |
1.94e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 43.19 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1202 DTVAELGEQIDNLQR--VKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDlnm 1279
Cdd:COG5192 393 DTVDRESSEIDNVGRktRRQPTGKAIAEETSREDELSFDDSDVSTSDENEDVDFTGKKGAINNEDESDNEEVAFDSD--- 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1280 qkARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAK------NALAHALQSSRHDCDLLREQYEE 1353
Cdd:COG5192 470 --SQFDESEGNLRWKEGLASKLAYSQSGKRGRNIQKIFYDESLSPEECIEEykgesaKSSESDLVVQDEPEDFFDVSKVA 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1354 EQEGKAELQRA-------LSKANSEVAQWRTKYETDAI----QRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTK 1422
Cdd:COG5192 548 NESISSNHEKLmesefeeLKKKWSSLAQLKSRFQKDATldsiEGEEELIQDDEKGNFEDLEDEENSSDNEMEESRGSSVT 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1423 QRLQGEVDDLMLDLERANTAcATLDKKQRNFdkvlaEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVV 1496
Cdd:COG5192 628 AENEESADEVDYETEREENA-RKKEELRGNF-----ELEERGDPEKKDVDWYTEEKRKIEEQLKINRSEFETMV 695
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
847-1440 |
2.05e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 847 AEAEKEMATMKEDFERAKEDLARSEARRKELEEKMvSLLQEKNDLQLQvqsETENLMDAEERCEGLIKSKIQLEAKVKEL 926
Cdd:pfam05557 30 IELEKKASALKRQLDRESDRNQELQKRIRLLEKRE-AEAEEALREQAE---LNRLKKKYLEALNKKLNEKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 927 nerleeeeemnselvakKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEA 1006
Cdd:pfam05557 106 -----------------ISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1007 HQQtLDDLQVEedkvnglikinvkLEQQTDDlegsLEQEKKLRADLERVKrKLEGDLKMSQESImdlendtqqleeklkk 1086
Cdd:pfam05557 169 EQR-IKELEFE-------------IQSQEQD----SEIVKNSKSELARIP-ELEKELERLREHN---------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1087 kefemSQLQTRIDDeqvlSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKqrsdLARELEEIsERLEEASGATSAQIE 1166
Cdd:pfam05557 214 -----KHLNENIEN----KLLLKEEVEDLKRKLEREEKYREEAATLELEKEK----LEQELQSW-VKLAQDTGLNLRSPE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1167 MNKKRESEFQKlrrdlEEATLQHEATAATLRKKHAD-TVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKS 1245
Cdd:pfam05557 280 DLSRRIEQLQQ-----REIVLKEENSSLTSSARQLEkARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1246 KSNMERMCRSVEDQFNEIKAkDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQ--L 1323
Cdd:pfam05557 355 RDGYRAILESYDKELTMSNY-SPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQesL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1324 EEETKAK---NALAHALQSSRHDCDLLREQYE--EEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLA 1398
Cdd:pfam05557 434 ADPSYSKeevDSLRRKLETLELERQRLREQKNelEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEI 513
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 124486959 1399 QRLQEAEENTEASNSKCASLEKTKQRLQG-EVDDLMLDLERAN 1440
Cdd:pfam05557 514 ERLKRLLKKLEDDLEQVLRLPETTSTMNFkEVLDLRKELESAE 556
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
942-1118 |
2.07e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 942 AKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQVEEDKV 1021
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1022 NGL------------IKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEF 1089
Cdd:COG3883 103 SYLdvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180
....*....|....*....|....*....
gi 124486959 1090 EMSQLQTRIDDEQVLSLQLQKKIKELQAR 1118
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
985-1909 |
2.10e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 985 EMTALEETISKLTKEKKSLQEaHQQTLDDlQVEEDKVNGLIKINVKleqqtdDLEGSLEQEKKLRADLERVKRKL--EGD 1062
Cdd:TIGR01612 460 KLKALEKRFFEIFEEEWGSYD-IKKDIDE-NSKQDNTVKLILMRMK------DFKDIIDFMELYKPDEVPSKNIIgfDID 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1063 LKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIE----- 1137
Cdd:TIGR01612 532 QNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKekikn 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1138 --------KQRSDLARELEEISERLEEASGATSAQI-EMNKKRESEFQKLRRDLEEAtlqHEATAATLRKKHADTVAElg 1208
Cdd:TIGR01612 612 isdkneyiKKAIDLKKIIENNNAYIDELAKISPYQVpEHLKNKDKIYSTIKSELSKI---YEDDIDALYNELSSIVKE-- 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1209 EQIDNLQRvKQKLEKEKSELKMEIDDMAS-NIETVSKSKSNMERMCRSVEDQFNEIKAKddQQTQLIHDLNMQKARLQTQ 1287
Cdd:TIGR01612 687 NAIDNTED-KAKLDDLKSKIDKEYDKIQNmETATVELHLSNIENKKNELLDIIVEIKKH--IHGEINKDLNKILEDFKNK 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1288 NGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLE-EETKAKNALAHALQSSRHDCDLLREQYEEEQ---EGKAELQR 1363
Cdd:TIGR01612 764 EKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINiDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKiinEMKFMKDD 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1364 ALSKANSEV---AQWRTKYETDAIQRTEELEEAKKKLA-QRLQEAEENTEAS----NSKCASLEKTKQRLQ--GEVDDLM 1433
Cdd:TIGR01612 844 FLNKVDKFInfeNNCKEKIDSEHEQFAELTNKIKAEISdDKLNDYEKKFNDSksliNEINKSIEEEYQNINtlKKVDEYI 923
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1434 LDLERANTACATLDKKQRNFDKVLAEWKQKLDESQA-ELEAAQKESRSLSTEIFKMRNAYEEVvdQLETLRRENKNLQEE 1512
Cdd:TIGR01612 924 KICENTKESIEKFHNKQNILKEILNKNIDTIKESNLiEKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAKNNELIKY 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1513 ISDLTEQIAETGKNL-----QEVEKTKKQVEQEKSDLQAALEEVE-------GSLEHEESKILRVQLEL--SQVKSELDR 1578
Cdd:TIGR01612 1002 FNDLKANLGKNKENMlyhqfDEKEKATNDIEQKIEDANKNIPNIEiaihtsiYNIIDEIEKEIGKNIELlnKEILEEAEI 1081
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1579 KVTEKDEEIEQIKRN--SQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQgQLKD 1656
Cdd:TIGR01612 1082 NITNFNEIKEKLKHYnfDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLE-DVAD 1160
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1657 SQLHLDDAQRSNEDLKEQLAIVERRNGLlqeeLEEMKVALEQTERTRRlsEQELLDSSDRVQLLHSQNTSLI------NT 1730
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKKKNI----YDEIKKLLNEIAEIEK--DKTSLEEVKGINLSYGKNLGKLflekidEE 1234
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1731 KKKLEADLAQCQAEVE--NSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRldeaeQLA 1808
Cdd:TIGR01612 1235 KKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLK 1309
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1809 LKGGKKQIQKLEARVRELESELDAEQKRGAEalkgAHKYERKVKEMTyqaeedrkNILRLQDlVDKLQAKVKSYKRQAEE 1888
Cdd:TIGR01612 1310 IIEDFSEESDINDIKKELQKNLLDAQKHNSD----INLYLNEIANIY--------NILKLNK-IKKIIDEVKEYTKEIEE 1376
|
970 980
....*....|....*....|.
gi 124486959 1889 AEEQANTQLSRCRRVQHELEE 1909
Cdd:TIGR01612 1377 NNKNIKDELDKSEKLIKKIKD 1397
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
947-1230 |
2.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 947 LEDKCSSLKRDIDDLELTLTKVEkEKHATENKVKNLSEEMTA--LEETISKLTKEKKSLQEAHQQtLDDLQVEedkvngL 1024
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNKNIEEQRKKNGenIARKQNKYDELVEEAKTIKAE-IEELTDE------L 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1025 IKINVKLEQQTDDLegsleqeKKLRADLERVKRKLEgdlKMSQESIMDLEND-----TQQLEEKLKKkefeMSQLQTRID 1099
Cdd:PHA02562 244 LNLVMDIEDPSAAL-------NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEGPDR----ITKIKDKLK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1100 DEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEiserleeasgatsaqiemNKKRESEFQKLR 1179
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDK------------------AKKVKAAIEELQ 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 124486959 1180 RDleeatlqheataatlRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKM 1230
Cdd:PHA02562 372 AE---------------FVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1273-1596 |
2.15e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.11 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1273 LIHDLNMQKARLQTQ--------NGELSHQVEEKESLVSQL-----------TKSKQALTQQLEELKRQLEEETKAKNAL 1333
Cdd:PTZ00108 1000 LLGKLERELARLSNKvrfikhviNGELVITNAKKKDLVKELkklgyvrfkdiIKKKSEKITAEEEEGAEEDDEADDEDDE 1079
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1334 AHALQSSRHD-------CDLLREQYEEEQEGKAELQRALSK-ANSEVAQ-WRT---KYEtDAIQRTEELEEAKKKLAQRL 1401
Cdd:PTZ00108 1080 EELGAAVSYDyllsmpiWSLTKEKVEKLNAELEKKEKELEKlKNTTPKDmWLEdldKFE-EALEEQEEVEEKEIAKEQRL 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1402 QEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKqRNFDKVLAEWKQKLDESQAELEAAQKESRSL 1481
Cdd:PTZ00108 1159 KSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEK-RKLDDKPDNKKSNSSGSDQEDDEEQKTKPKK 1237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1482 STEifkmrNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESK 1561
Cdd:PTZ00108 1238 SSV-----KRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKK 1312
|
330 340 350
....*....|....*....|....*....|....*
gi 124486959 1562 ILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQR 1596
Cdd:PTZ00108 1313 RLEGSLAALKKKKKSEKKTARKKKSKTRVKQASAS 1347
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1781-1927 |
2.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1781 AHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELESELDAEQKR--GAEALKGAHKYERKVKEMTYQA 1858
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARikKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1859 EEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAK 1927
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1210-1403 |
2.22e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 42.90 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1210 QIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMcrsVEDQFNEIKAKDDQQTQLihdLNMQKARLQTQNg 1289
Cdd:pfam15066 333 QIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEEL---IEDKYNVILEKNDINKTL---QNLQEILANTQK- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1290 ELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKaknALAHALQSSRhdcdLLREQYEEE---QEGKAELQRALS 1366
Cdd:pfam15066 406 HLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNK---SVSQCLEMDK----TLSKKEEEVerlQQLKGELEKATT 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 124486959 1367 KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE 1403
Cdd:pfam15066 479 SALDLLKREKETREQEFLSLQEEFQKHEKENLEERQK 515
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1488-1924 |
2.39e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1488 MRNAYEEVVDQLETLRRE--NKNLQEEISDLtEQIAETGKNLQEVEKTKKQ----VEQEKSDLQAALEEVEGSLEheESK 1561
Cdd:PRK04778 23 LRKRNYKRIDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKwdeiVTNSLPDIEEQLFEAEELND--KFR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1562 ILRVQLELSQVKSELDRkvTEKD-----EEIEQIKRNSQRAVEAMQSVLD--AEIRSRNDALRLK-----KKMEGDLNEM 1629
Cdd:PRK04778 100 FRKAKHEINEIESLLDL--IEEDieqilEELQELLESEEKNREEVEQLKDlyRELRKSLLANRFSfgpalDELEKQLENL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1630 EIQLSHANRqvaetqkhlRTVQGQLKDSQLHLDDAQRSNEDLKEQL----AIVERRNGLLQEELEEMKVALEQ-TERTRR 1704
Cdd:PRK04778 178 EEEFSQFVE---------LTESGDYVEAREILDQLEEELAALEQIMeeipELLKELQTELPDQLQELKAGYRElVEEGYH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1705 LSEQELLDssdRVQLLHSQNTSLINTKKKLEADLAQCQ-AEVENSIQ---ESRNAEEKAKKaitdaammaeELKKEQDT- 1779
Cdd:PRK04778 249 LDHLDIEK---EIQDLKEQIDENLALLEELDLDEAEEKnEEIQERIDqlyDILEREVKARK----------YVEKNSDTl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1780 SAHLERMKKNLEQTVKDLQH-----RLDEAEQLALKGGKKQIQKLEARVRELE----------SELDAEQKRGAEALKGA 1844
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRvkqsyTLNESELESVRQLEKQLESLEKQYDEITeriaeqeiaySELQEELEEILKQLEEI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1845 HKYERKVKEMTYQAEED----RKNILRLQD-------LVDKLQ-----AKVKSYKRQAEEAEEQANTQLSRCR----RVQ 1904
Cdd:PRK04778 396 EKEQEKLSEMLQGLRKDeleaREKLERYRNklheikrYLEKSNlpglpEDYLEMFFEVSDEIEALAEELEEKPinmeAVN 475
|
490 500
....*....|....*....|
gi 124486959 1905 HELEEAEERADIAESQVNKL 1924
Cdd:PRK04778 476 RLLEEATEDVETLEEETEEL 495
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1502-1693 |
2.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1502 LRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEevegSLEHEESKILRVQLELSQVKSELDRKVT 1581
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLS----AAEAERSRLQALLAELAGAGAAAEGRAG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1582 EKDEEIEQIKRNSQRAveamqsvldaeiRSRNDALrlkkkmegdlnemeiqlshaNRQVAETQKHLRTVQGQLKDSQLHL 1661
Cdd:PRK09039 120 ELAQELDSEKQVSARA------------LAQVELL--------------------NQQIAALRRQLAALEAALDASEKRD 167
|
170 180 190
....*....|....*....|....*....|..
gi 124486959 1662 DDAQRSNEDLKEQLaiverrNGLLQEELEEMK 1693
Cdd:PRK09039 168 RESQAKIADLGRRL------NVALAQRVQELN 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1060 |
2.61e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 843 LLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAK 922
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 923 VKELNERLEEEEEMNSELVAK--KRNLEDKCSSL--KRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTK 998
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124486959 999 EKKSL------QEAHQQTLDDLQVEEDKVngLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLE 1060
Cdd:COG4942 172 ERAELeallaeLEEERAALEALKAERQKL--LARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1136-1766 |
2.91e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1136 IEKQRSDLARELE----EISERL---EEASGATSAQIE-MNKKRESEFQKLRRDLEEA--TLQHEATAATLR---KKHAD 1202
Cdd:NF041483 566 IAARQAEAAEELTrlhtEAEERLtaaEEALADARAEAErIRREAAEETERLRTEAAERirTLQAQAEQEAERlrtEAAAD 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1203 TVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNI----------------ETVSKSKSNMERMCRSVEDQFNEIKAK 1266
Cdd:NF041483 646 ASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVraeaaaaaervgteaaEALAAAQEEAARRRREAEETLGSARAE 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1267 DDQQTQLIHD-----LNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEE----LKRQLEEE-TKAKNALAHA 1336
Cdd:NF041483 726 ADQERERAREqseelLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEEEiAGLRSAAEHA 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1337 LQSSR----HDCDLLREQYEEEQEGKAE-LQRALSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQeaeenT 1408
Cdd:NF041483 806 AERTRteaqEEADRVRSDAYAERERASEdANRLRREAQEETEAAKALAErtvSEAIAEAERLRSDASEYAQRVR-----T 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1409 EASNSkCASLEKTKQRLQGEVDDlmlDLERANTACATldkkqrNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKM 1488
Cdd:NF041483 881 EASDT-LASAEQDAARTRADARE---DANRIRSDAAA------QADRLIGEATSEAERLTAEARAEAERLRDEARAEAER 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1489 RNAyeEVVDQLETLRRENKNLQEEisdLTEQIAET-GKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKIL-RVQ 1566
Cdd:NF041483 951 VRA--DAAAQAEQLIAEATGEAER---LRAEAAETvGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLdEAR 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1567 LELSQVKSE----LDRKVTEKDEEIEQIKRNSQRavEAMQSVLDAEirSRNDALRLKKKMEgdlnemeiqlshANRQVAE 1642
Cdd:NF041483 1026 KDANKRRSEaaeqADTLITEAAAEADQLTAKAQE--EALRTTTEAE--AQADTMVGAARKE------------AERIVAE 1089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1643 TqkhlrTVQGQLKdsqlhlddAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQT-----ERTRRLSEQELLDSSDRv 1717
Cdd:NF041483 1090 A-----TVEGNSL--------VEKARTDADELLVGARRDATAIRERAEELRDRITGEieelhERARRESAEQMKSAGER- 1155
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 124486959 1718 qllhsqntslintkkkleadlaqCQAEVENSIQESRNAEEKAKKAITDA 1766
Cdd:NF041483 1156 -----------------------CDALVKAAEEQLAEAEAKAKELVSDA 1181
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1459-1532 |
2.95e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.64 E-value: 2.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1459 EWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEK 1532
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1683-1869 |
3.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1683 GLLQEELEEMKVALE-QTERTRRLSEQELLDSSDRVQLLHSQNTS---LINTKKKLEADLAQCQAEVENsIQESRNAEEK 1758
Cdd:COG4717 45 AMLLERLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEE-LREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1759 AKKAITDAAMMA-------------EELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRE 1825
Cdd:COG4717 124 LLQLLPLYQELEaleaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 124486959 1826 LESELDA--EQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQ 1869
Cdd:COG4717 204 LQQRLAEleEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
856-1318 |
3.76e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 856 MKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEglikskiQLEAKVKELNERLEEEEE 935
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAA-------ILQTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 936 MNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQ 1015
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1016 VEEDKVNGLIKINVKLEQQTDDLE----GSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEM 1091
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREREDrerlEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1092 SQLQtriddeqvlsLQLQKKIKELQARTEELEEEIEAEHTVRAKIEkqRSDLARELEEISERLEEASGATSAQIE--MNK 1169
Cdd:pfam10174 520 KSLE----------IAVEQKKEECSKLENQLKKAHNAEEAVRTNPE--INDRIRLLEQEVARYKEESGKAQAEVErlLGI 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1170 KRESEFQKLRRD-----LEEATLQHEATAAT-----------LRKKHADTVAELGEQIDNLQRVKQKLEKEksELKMEID 1233
Cdd:pfam10174 588 LREVENEKNDKDkkiaeLESLTLRQMKEQNKkvanikhgqqeMKKKGAQLLEEARRREDNLADNSQQLQLE--ELMGALE 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1234 DMASNIETVSKSKSNMERMCRSVEDQFNEIKAkdDQQTQLIHDLNM-QKARLQTQNG--------ELSHQVEEK-ESLVS 1303
Cdd:pfam10174 666 KTRQELDATKARLSSTQQSLAEKDGHLTNLRA--ERRKQLEEILEMkQEALLAAISEkdaniallELSSSKKKKtQEEVM 743
|
490
....*....|....*
gi 124486959 1304 QLTKSKQALTQQLEE 1318
Cdd:pfam10174 744 ALKREKDRLVHQLKQ 758
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1382-1690 |
4.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1382 DAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWK 1461
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1462 QKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQ-----IAETGKNLQEVEKTKKQ 1536
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQElqalsEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1537 VEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDAL 1616
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1617 RLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELE 1690
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1196-1435 |
4.49e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1196 LRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKS--KSNMERMcrsvedqfnEIKAKDDQQTQL 1273
Cdd:PHA02562 207 QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAlnKLNTAAA---------KIKSKIEQFQKV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1274 IHdlnmqkarLQTQNGE---LSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNalahalqssrhdcdllreQ 1350
Cdd:PHA02562 278 IK--------MYEKGGVcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMD------------------E 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1351 YEEEQEGKAELQRALSKANSEVAqwRTKYETDAIQRT-EELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLqGEV 1429
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLI--TLVDKAKKVKAAiEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR-GIV 408
|
....*.
gi 124486959 1430 DDLMLD 1435
Cdd:PHA02562 409 TDLLKD 414
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1290-1561 |
5.16e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1290 ELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKAN 1369
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1370 SEVAQWRTKYetDAIQRTEELEEAKKKLAQRLQEAEENTEasnskcASLEKTKQrLQGEVDDLMLDLERANTAcATLDKK 1449
Cdd:COG1340 92 EELDELRKEL--AELNKAGGSIDKLRKEIERLEWRQQTEV------LSPEEEKE-LVEKIKELEKELEKAKKA-LEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1450 QRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQE 1529
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
250 260 270
....*....|....*....|....*....|..
gi 124486959 1530 VEKTKKQVEQEKSDLQAALEEVEGSLEHEESK 1561
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1206-1354 |
5.62e-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: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1206 ELGEQIDNLQRVKQKLEKEKSELKMEIDDM--------ASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDL 1277
Cdd:pfam09787 51 ELRQERDLLREEIQKLRGQIQQLRTELQELeaqqqeeaESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEEL 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124486959 1278 NMQKARLQTQngeLSHQVEEKESLVSQLTKSKQALTQQ--LEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEE 1354
Cdd:pfam09787 131 RRSKATLQSR---IKDREAEIEKLRNQLTSKSQSSSSQseLENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQ 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1512-1781 |
6.48e-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: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1512 EISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIK 1591
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1592 RNSqRAVEAMQSVLDAEirsrndalrlkkkmegDLNEMeIQLSHANRQVAETQKHLrtvQGQLKDSQLHLDDAQRSNEDL 1671
Cdd:COG3883 97 RSG-GSVSYLDVLLGSE----------------SFSDF-LDRLSALSKIADADADL---LEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1672 KEQLAiverrngLLQEELEEMKVALEQTERTRrlsEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQE 1751
Cdd:COG3883 156 LAELE-------ALKAELEAAKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250 260 270
....*....|....*....|....*....|
gi 124486959 1752 SRNAEEKAKKAITDAAMMAEELKKEQDTSA 1781
Cdd:COG3883 226 AAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1668-1938 |
6.66e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1668 NEDLKEQLAIVERRNGLLQEELEEMKVALEQtERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVEN 1747
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1748 SIQESRNAEEKAKKAITDaaMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ------------ 1815
Cdd:pfam17380 347 ERELERIRQEERKRELER--IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQrkiqqqkvemeq 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1816 --IQKLEARVRELEsELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQA 1893
Cdd:pfam17380 425 irAEQEEARQREVR-RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124486959 1894 NTQ--LSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKMEE 1938
Cdd:pfam17380 504 RKQamIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1387-1589 |
7.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1387 TEELEEAKKKLAQRLQEAEEntEASNSKcaslektkqrlqgevddlmldlerantacatldkkqrnfDKVLAEWKQKLDE 1466
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK--EAEAIK---------------------------------------KEALLEAKEEIHK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1467 SQAELEaaqKESRSLSTEIFKMRNayeEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQA 1546
Cdd:PRK12704 69 LRNEFE---KELRERRNELQKLEK---RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 124486959 1547 ALEEVEGsLEHEESKilrvQLELSQVKSELDRKVTEKDEEIEQ 1589
Cdd:PRK12704 143 ELERISG-LTAEEAK----EILLEKVEEEARHEAAVLIKEIEE 180
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1448-1575 |
7.40e-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: 40.77 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1448 KKQRNFDKVLAEwkqKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRR-----------ENKNLQEEISDL 1516
Cdd:smart00787 140 KLLEGLKEGLDE---NLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQledeledcdptELDRAKEKLKKL 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1517 TEQIAETGKNLQEVEKTKKQVEQE-------KSDLQAALEEVEGSLE----HEESKILRVQLELSQVKSE 1575
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKiedltnkKSELNTEIAEAEKKLEqcrgFTFKEIEKLKEQLKLLQSL 286
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1679-1917 |
8.37e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.67 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1679 ERRNGLLQEELEEMKvalEQTERTRR----LSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRN 1754
Cdd:pfam00038 24 EQQNKLLETKISELR---QKKGAEPSrlysLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1755 AEE--KAKKAITDAAMMA--------EELKKEqdtsahLERMKKNLEQTVKDLQHRL-DEAEQLALKGGKKQ-IQKLEAR 1822
Cdd:pfam00038 101 AENdlVGLRKDLDEATLArvdleakiESLKEE------LAFLKKNHEEEVRELQAQVsDTQVNVEMDAARKLdLTSALAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1823 VRELESELDAEQKRGAEALkgahkYERKVKEMTYQAE--------------EDRKNILRLQDLVDKLQAKVKSYKRQAEE 1888
Cdd:pfam00038 175 IRAQYEEIAAKNREEAEEW-----YQSKLEELQQAAArngdalrsakeeitELRRTIQSLEIELQSLKKQKASLERQLAE 249
|
250 260 270
....*....|....*....|....*....|.
gi 124486959 1889 AEEQANTQLSRCRRVQHELEEA--EERADIA 1917
Cdd:pfam00038 250 TEERYELQLADYQELISELEAElqETRQEMA 280
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1599-1926 |
8.47e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1599 EAMQSVLDAEIRSRNDALRL-----------KKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRS 1667
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAqeaanrqrekeKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1668 NEDLKEQLAIVERRNGLLQE---ELEEMKVALEQTERTRrlsEQELLDSSDRVQLLHSQntslintKKKLEADLAQCQAE 1744
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEArirELEEDIKTLTQRVLER---ETELERMKERAKKAGAQ-------RKEEEAERKQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1745 VENSIQESRNaeekakkaitdaamMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLEARVR 1824
Cdd:pfam07888 180 LQQTEEELRS--------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR--------KEAENEALLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1825 ELES--ELDAEQKRGAEALKG-----AHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQL 1897
Cdd:pfam07888 238 ELRSlqERLNASERKVEGLGEelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADK 317
|
330 340
....*....|....*....|....*....
gi 124486959 1898 SRCRRVQHELEEAEERADIAESQVNKLRA 1926
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKLEV 346
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1261-1658 |
8.77e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1261 NEIKAKDDQQTQLIHDLNMQKARLQTQNGELShqvEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSs 1340
Cdd:COG5185 162 KDIFGKLTQELNQNLKKLEIFGLTLGLLKGIS---ELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKG- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1341 rhdcdllREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEE---NTEASNSKCAS 1417
Cdd:COG5185 238 -------FQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEkiaEYTKSIDIKKA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1418 LEKTKQRLQ-----GEVDDLMLDLERANTAC-ATLDKKQRNFDKVLAEWK---------QKLDESQAELEAAQKESRSLS 1482
Cdd:COG5185 311 TESLEEQLAaaeaeQELEESKRETETGIQNLtAEIEQGQESLTENLEAIKeeienivgeVELSKSSEELDSFKDTIESTK 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1483 TEIF-KMRNAY---------------------EEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQE 1540
Cdd:COG5185 391 ESLDeIPQNQRgyaqeilatledtlkaadrqiEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1541 K--SDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRL 1618
Cdd:COG5185 471 EinRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASEL 550
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 124486959 1619 KKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQ 1658
Cdd:COG5185 551 IQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPI 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1762-1937 |
8.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1762 AITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELESELDAEQKRGAEAL 1841
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1842 KGAHKYERKVK--EMTYQAEE-----DRKNIL-RLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEER 1913
Cdd:COG3883 93 RALYRSGGSVSylDVLLGSESfsdflDRLSALsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180
....*....|....*....|....*...
gi 124486959 1914 ADI----AESQVNKLRAKSRDVGGQKME 1937
Cdd:COG3883 173 LEAqqaeQEALLAQLSAEEAAAEAQLAE 200
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1778-1931 |
9.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124486959 1778 DTSAHLERMKKNLEQTvkdLQHRLDeaeqlaLKGGKKQIQKLEARVRELESELDAeqkrgaealkgaHKYERKVKEMTYQ 1857
Cdd:PRK04863 273 DYMRHANERRVHLEEA---LELRRE------LYTSRRQLAAEQYRLVEMARELAE------------LNEAESDLEQDYQ 331
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124486959 1858 AEEDRKNilRLQDLVdKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDV 1931
Cdd:PRK04863 332 AASDHLN--LVQTAL-RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADY 402
|
|
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