|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1443.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHFS 579
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 6981234 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14913 641 KKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-767 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1322.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK-KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEWTFIDFGMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvvKGKAEAHF 578
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATTDADGGKKKVAKKKGSSFQTVSALFRENLNK 658
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASL---FKDYEESGGGGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 659 LMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFiD 738
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 6981234 739 SKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01377 634 GKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1214.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHFS 579
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 6981234 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1192.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKD-SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQpGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAID 338
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 499 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHF 578
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGG--KKKVAKKKGSSFQTVSALFRENL 656
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 6981234 737 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1185.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAI 337
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAH 577
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 578 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGG---KKKVAKKKGSSFQTVSALFRE 654
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAgggAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 655 NLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEG 734
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 6981234 735 QFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1181.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKK--DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAI 337
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAH 577
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 578 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADG-GKKKVAKKKGSSFQTVSALFRENL 656
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 6981234 737 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1177.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDS--KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAAsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAI 337
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAH 577
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 578 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDAD-GGKKKVAKKKGSSFQTVSALFRENL 656
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 6981234 737 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1161.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDLAKKKD----SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 256
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGPGKKAqflaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 257 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSA 336
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 497 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKV-VKGKAE 575
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPdKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 576 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDA---DGGKKKVAKKKGSSFQTVSALF 652
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 653 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 732
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 6981234 733 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1153.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHFS 579
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 6981234 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14917 641 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1132.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNAnKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAID 338
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 499 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHF 578
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDA-DGGKKKVAKKKGSSFQTVSALFRENLN 657
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 658 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 737
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 6981234 738 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1039.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL-----GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHFS 579
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 739
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 6981234 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14929 635 RKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-767 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1025.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 88 IEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 168 TDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 248 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQ-GEILVASIDD 326
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 327 REELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVK 406
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 407 VGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEK 485
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 486 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNF 564
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 565 QKPKVvkgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKK---- 640
Cdd:pfam00063 472 QKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrt 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 641 KGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 720
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 6981234 721 QRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:pfam00063 629 QRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-779 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 990.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 81 NPPKFDKIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 161 NAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRND 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGS--------NTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 241 NSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQG-EI 319
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 320 LVASIDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA-EPDGTEVADKTAYLMGLNSSDLLK 398
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 399 ALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLC 478
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 479 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQH 557
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 558 LGKSNNFQKPKVvkgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAtfattdadggKKKV 637
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP----------SGVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 638 AKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYG 717
Cdd:smart00242 537 NAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 718 DFKQRYRVLNASAIPEGQFiDSKKACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRD 779
Cdd:smart00242 617 EFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 989.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDIL 340
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 420
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 421 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 500
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 501 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGK-AEAHFS 579
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 580 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDAdggkkKVAKKKGSSFQTVSALFRENLNKL 659
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAG-----SKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDS 739
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDN 631
|
650 660
....*....|....*....|....*...
gi 6981234 740 KKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14934 632 KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-767 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 965.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASK--KTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVK-GKAEAHF 578
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKG-SSFQTVSALFRENLN 657
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKgGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 658 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQfi 737
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 6981234 738 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14909 637 DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-767 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 835.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQ-EAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATIAATGdlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSG---SSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIE---LLLITTNPYDYPFISQGEIL-VASIDDREELLATD 334
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREelkLELLLSYYYLNDYLNSSGCDrIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 335 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREE--QAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 412
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 413 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 490
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 491 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKv 569
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 570 vkgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSnrllahlyatfattdadggkkkvakkkgssfqtvs 649
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 650 aLFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 729
Cdd:cd00124 518 -QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 6981234 730 AiPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd00124 597 A-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
31-1112 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 831.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 31 PFDAKTYCFVVDSKEEYAKGKIKSsqdgkvTVETEDNRTLVVKPEDV--YAMNPPKFDKIEDMAMLTHLNEPAVLYNLKD 108
Cdd:COG5022 15 PDEEKGWIWAEIIKEAFNKGKVTE------EGKKEDGESVSVKKKVLgnDRIKLPKFDGVDDLTELSYLNEPAVLHNLEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 109 RYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVN 188
Cdd:COG5022 89 RYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 189 TKRVIQYFATIAATgdlakkkDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYL 268
Cdd:COG5022 169 AKRIMQYLASVTSS-------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 269 LEKSRVTFQLKAERSYHIFYQILSNKkPELIELLLITTNPYDYPFISQGE-ILVASIDDREELLATDSAIDILGFTPEEK 347
Cdd:COG5022 242 LEKSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 348 SGLYKLTGAVMHYGNMKFKqKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNA 427
Cdd:COG5022 321 DQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 428 LSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI 507
Cdd:COG5022 400 LAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 508 EWTFIDFgMDLAACIELIEK--PMGIFSILEEECMFPKATDTSFKNKLYDQ-HLGKSNNFQKPKVVKGKaeahFSLIHYA 584
Cdd:COG5022 480 EWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 585 GTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfattdadggKKKVAKKKGSSFQTVSALFRENLNKLMSNLR 664
Cdd:COG5022 555 GDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLF-----------DDEENIESKGRFPTLGSRFKESLNSLMSTLN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 665 TTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI---DSKK 741
Cdd:COG5022 624 STQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKN 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 742 ACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDERLAKLITRTQAVCRGFLMRVEFQKMMQRRESIFCIQYNIRA 821
Cdd:COG5022 704 AVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 822 FMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELaKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLD 901
Cdd:COG5022 784 RRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFS 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 902 AEERCDQLIKAKFQLEAKIKEVTERAEDEEEINaELTAKKRKLEDECSELKKDIDDLELtlakvekekhateNKVKNLTE 981
Cdd:COG5022 863 LLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSSDLI-------------ENLEFKTE 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 982 ELAGLDETIAKLTREKKALQEAHQQtlddlqaeeDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLK 1061
Cdd:COG5022 929 LIARLKKLLNNIDLEEGPSIEYVKL---------PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1062 LAQEsILDLENDKQQLDERLKKKDFEYSQLQS--KVEDEQTLSLQLQKKIKEL 1112
Cdd:COG5022 1000 ELAE-LSKQYGALQESTKQLKELPVEVAELQSasKIISSESTELSILKPLQKL 1051
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 810.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAAT---GDLAKKKDSK----MKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 253
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVnpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 254 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILVASIDDREELLAT 333
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 334 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 412
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 413 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 491
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 492 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksnnfQKPKVVK 571
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 572 G--KAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATTDAdggkKKVAKKK 641
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaeivgmAQQALTDT----QFGARTR 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 642 GSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 721
Cdd:cd14911 550 KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 6981234 722 RYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14911 630 RYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 783.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHK--GRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGKA 574
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKDKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 575 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF-ATTDADGGKKKVAKKKGSS-------FQ 646
Cdd:cd14920 476 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdRIVGLDQVTGMTETAFGSAyktkkgmFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 647 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 6981234 727 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14920 634 TPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 722.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM--KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDREELLATDSAI 337
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYSKYR--FLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 496 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKvvKG 572
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 573 KAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF-------ATTDADGGKKKVAKKKGSSF 645
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldKVAGMGESLHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 646 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 725
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 6981234 726 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 704.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHK--GKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPyDYPFISQGEILVASIDDREELLATDSAIDIL 340
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLE 498
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 499 QEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGKAE 575
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 576 ahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF--------ATTDADGGKKKVAKKKGSSFQT 647
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 648 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 727
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 6981234 728 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14921 635 ANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-767 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 691.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYT-SWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATIAATgdlakkkDSKMKGTlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGS-------SSGETQV-EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNK-KPELIELLLitTNPYDYPFISQGE-ILVASIDDREELLATDSA 336
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHL--GSAEDFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLP--RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 495 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNN-FQKPKVVKGK 573
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 574 aeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLlahlyatfattdadggkkkvakkkgssfQTVSALFR 653
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------KTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAipE 733
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 6981234 734 GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01380 596 WLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
101-767 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 681.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM--KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSLAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEILVASIDDREELLATDSAID 338
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKvvKGKA 574
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 575 EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfatTDADGGKKKVAKKKGSS---------- 644
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELW-----KDVDRIVGLDKVSGMSEmpgafktrkg 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 645 -FQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRY 723
Cdd:cd15896 553 mFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 6981234 724 RVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 678.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPK--GRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEIlVASIDDREELLATDSAIDIL 340
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPS-SSPGQERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 419
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 420 QVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14930 317 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGKA 574
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRDQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 575 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY------ATFATTDADGGKKKVAKKKGSSFQTV 648
Cdd:cd14930 475 D--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegiVGLEQVSSLGDGPPGGRPRRGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 649 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 728
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 6981234 729 SAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14930 633 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
101-767 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 677.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGKA 574
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKDKA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 575 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF--------ATTDADGGKKKVAKKKGSSFQ 646
Cdd:cd14919 473 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 647 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 6981234 727 NASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14919 631 TPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-767 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 640.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRgkKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDlakkkdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGSS-----------GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEIL-VASIDDREELLATDSAID 338
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNCLtIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 418
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 419 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDT-KLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 497
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 498 EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFqkpkvvKGKAEA 576
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 577 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQkSSNRLLAHLYAT-FATTDADGGKKKVAKKKGSSFQTVSALFREN 655
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLS-SCSCQLPQLFASkMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 656 LNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQ 735
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ 617
|
650 660 670
....*....|....*....|....*....|..
gi 6981234 736 FIDSkkACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01383 618 DPLS--TSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
101-767 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 629.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIaatgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI-----------SGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEILVAS-IDDREELLATDSAIDI 339
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQRE--EQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF---IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 494
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 495 FVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPkvvKGK 573
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP---KSD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 574 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKvakkkgssfQTVSALFR 653
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS---------PTLSSQFR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLnASAIPE 733
Cdd:cd01381 536 KSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGIPP 614
|
650 660 670
....*....|....*....|....*....|....
gi 6981234 734 GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01381 615 AHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
101-767 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 623.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDlakKKDSKMKgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSE---SEVERVK----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAIDIL 340
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 341 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDgTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY---VTKGQT 417
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQ-HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHhmFV 496
Cdd:cd01378 314 VEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 497 L--EQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKLyDQHLGKSNNFQKPKVVKG 572
Cdd:cd01378 392 LkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 573 KAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatFATTDADGGKKKVakkkgssfqTVSALF 652
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF--PEGVDLDSKKRPP---------TAGTKF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 653 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 732
Cdd:cd01378 539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWP 618
|
650 660 670
....*....|....*....|....*....|....*
gi 6981234 733 EGQFIDsKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01378 619 AWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
101-767 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 604.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFAtiAATGdlakkKDSKmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14883 82 SGAGKTETTKLILQYLC--AVTN-----NHSW----VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKK--PELIELLLItTNPYDYPFISQ-GEILVASIDDREELLATDSAI 337
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14883 310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 497 LEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKvvKGKAE 575
Cdd:cd14883 390 LEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 576 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL--YATFATTDADGGKKKVAKKKGSSFQ---TVSA 650
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKgkpTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 651 LFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASA 730
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRA 625
|
650 660 670
....*....|....*....|....*....|....*..
gi 6981234 731 IPEGQFIDsKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14883 626 RSADHKET-CGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-767 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 592.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFAtiaatgDLAKKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA------YMGGRAVTEGR-SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGE-ILVASIDDREELLATDSAI 337
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKqkqreEQAEPDGTEVADK--------TAYLMGLNSSDLLKALCFPRVKVGN 409
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVTPD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 410 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 489
Cdd:cd01384 308 GIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 490 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQKPK 568
Cdd:cd01384 388 FNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 569 vvkgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDAdggkkkvakKKGSSFQTV 648
Cdd:cd01384 466 ----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT---------SSSSKFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 649 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLnA 728
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL-A 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 6981234 729 SAIPEGQFiDSKKACEKLLASIDIDhtQYKFGHTKVFFK 767
Cdd:cd01384 612 PEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-767 |
6.37e-172 |
|
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: 538.98 E-value: 6.37e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATIAatGDLakkKDSKMKgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--GGL---NDSTIK-----KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFiSQGEILVASIDDREELLATDSAID 338
Cdd:cd14903 151 LVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEE-RLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE--PDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14903 229 LIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14903 309 KKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 497 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKgkaeA 576
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR----T 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 577 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGS-----SFQTVSAL 651
Cdd:cd14903 464 QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrggalTTTTVGTQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 652 FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAi 731
Cdd:cd14903 544 FKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG- 622
|
650 660 670
....*....|....*....|....*....|....*..
gi 6981234 732 pEGQFIDSKKACEKLLASIDIDH-TQYKFGHTKVFFK 767
Cdd:cd14903 623 -RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-767 |
9.64e-170 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 532.59 E-value: 9.64e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 103 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 182 GAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGA----------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLittnpydypfisqgeiLVASIDDREELLATDSAIDILG 341
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 342 FTPEEKSGLYKLTGAVMHYGNMKFkqkqrEEQAEPD--GTEVADK-------TAYLMGLNSSDLLKALCfPRVKVGNEYV 412
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLT-TRVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 413 TKGQ------TVDQVHHAVNALSKSVYEKLFLWMVTRINQQldtkLPRQ---HFIGVLDIAGFEIFEYNSLEQLCINFTN 483
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQC----IPFEtssYFIGVLDIAGFEYFEVNSFEQFCINYCN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 484 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLgksN 562
Cdd:cd01382 368 EKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---N 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 563 NFQKPKVVKGKAEAH--------FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGK 634
Cdd:cd01382 444 HFRLSIPRKSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 635 KKVAKkkgsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRI 714
Cdd:cd01382 524 KAGKL----SFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 6981234 715 LYGDFKQRYRVLNASAIPEgqfIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01382 600 SFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-767 |
1.04e-169 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 532.43 E-value: 1.04e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATgdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS-----------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSnkKPELIELLLITTNPyDYPFISQGEIL-VASIDDREELLATDSAID 338
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLA--SPDPASRGGWGSSA-AYGYLSLSGCIeVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT---EVADKTAYLMGLNSSDLLKALCFPRVKVgneyvtKG 415
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEI------KG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 416 Q-------TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQ 487
Cdd:cd14872 301 CdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 488 QFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnnFQK 566
Cdd:cd14872 381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 567 PKVVKGkAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATTDADggkkkvakkKGSSFQ 646
Cdd:cd14872 458 YAEVRT-SRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL---FPPSEGD---------QKTSKV 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 647 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14872 525 TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 6981234 727 NaSAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14872 605 V-KTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
101-767 |
4.80e-168 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 528.58 E-value: 4.80e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEAPPHIFSISDNAY-QFM---LTDRENQSI 175
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 176 LITGESGAGKTVNTKRVIQYFATIAA--------TGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGK 247
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSgfaqgasgEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 248 FIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEILVASIDDR 327
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 328 EELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT-EVADKTAYLMGLNSSDLLKALCFPRVK 406
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 407 VGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKL 486
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-----KPmGIFSILEEECMFPKA-TDTSFKNKLYDQHLGK 560
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITLDDCWRFKGEeANKKFVSQLHASFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 561 SN------------NFQKPKVvkgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAhlyatfatt 628
Cdd:cd14890 479 SGsggtrrgssqhpHFVHPKF---DADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIRE--------- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 629 dadggkkkvakkkgssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRK 708
Cdd:cd14890 547 -----------------VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQ 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 709 GFPNRILYGDFKQRYRVLNASAipegqfiDSKKACEKLLASI-DIDHTQYKFGHTKVFFK 767
Cdd:cd14890 610 GFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
101-767 |
4.36e-166 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 523.16 E-value: 4.36e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKLA 260
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRN----------NLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQIL---SNKKPELIELLlittNPYDYPFISQG-EILVASIDDREELLATDSA 336
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLaglPAQLRQKYGLQ----EAEKYFYLNQGgNCEIAGKSDADDFRRLLAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEpdGTEVADK-----TAYLMGLNSSDLLKALCFPRVKVGNEY 411
Cdd:cd01387 227 MQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDaeiqwVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 412 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 491
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 492 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVv 570
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRM- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 571 kGKAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTdadgGKKKVAKKKGSSF----- 645
Cdd:cd01387 462 -PLPE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQ----TDKAPPRLGKGRFvtmkp 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 646 --QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRY 723
Cdd:cd01387 535 rtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRY 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 6981234 724 RVLNASAIPEGQFIDSKKACEKLLASIDIDhTQYKFGHTKVFFK 767
Cdd:cd01387 615 RCLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-767 |
4.40e-164 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 516.44 E-value: 4.40e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFAtiaatgDLAKKKDskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01379 81 ESGAGKTESANLLVQQLT------VLGKANN----RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQIL----SNKKpeLIELLLITTNPYDYPFISQGEILVASIDD--REELLAT 333
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSgnREKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 334 DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ----AEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGN 409
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 410 EYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--DTKLP-RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKL 486
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 487 QQFFNHHMFVLEQEEYKKEGIEWTFIDFG-----MDLaacieLIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKS 561
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 562 NNFQKPKvvkgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAhlyatfattdadggkkkvakkk 641
Cdd:cd01379 462 KYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 642 gssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 721
Cdd:cd01379 516 ----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLK 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 6981234 722 RYRVL--NASAIPEGqfidSKKACEKLLASIDIDHtqYKFGHTKVFFK 767
Cdd:cd01379 592 RYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-767 |
4.61e-162 |
|
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: 512.32 E-value: 4.61e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRgKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATiaatgdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF----- 253
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-------AGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 254 ----GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTN-----------PYDYPFISQGE 318
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENdeklakgadakPISIDMSSFEP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 319 ILV------------ASIDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVAD 383
Cdd:cd14888 233 HLKfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 384 KTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLD 462
Cdd:cd14888 313 KVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 463 IAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMF 541
Cdd:cd14888 393 IFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 542 PKATDTSFKNKLYDQHLGkSNNFqkpKVVKGKAEAhFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL 621
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKG-HKRF---DVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 622 YATFATTDADGGKKKVAkkkgssFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLE 701
Cdd:cd14888 547 FSAYLRRGTDGNTKKKK------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQ 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 702 GIRICRKGFPNRILYGDFKQRYRVLnasAIPEGQfidskkacekllasidIDHTQYKFGHTKVFFK 767
Cdd:cd14888 621 AVQVSRAGYPVRLSHAEFYNDYRIL---LNGEGK----------------KQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-767 |
1.60e-161 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 511.92 E-value: 1.60e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 103 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 183 AGKTVNTKRVIQYFATIAatgdlakkkdskMKGT---LEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd01385 84 SGKTESTNFLLHHLTALS------------QKGYgsgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITtnPYDYPFISQGEILVA-SIDDREELLATDSAI 337
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGaSEEERKELHLKQ--PEDYHYLNQSDCYTLeGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQK--QREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 415
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 416 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL----DTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 491
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 492 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKlYDQHLGKSNNFQKPKvv 570
Cdd:cd01385 390 QHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 571 kgKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLL--------------AHLYATFATTDADGGKKK 636
Cdd:cd01385 466 --VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVreligidpvavfrwAVLRAFFRAMAAFREAGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 637 VAKKKGSSFQ---------------------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLR 695
Cdd:cd01385 544 RRAQRTAGHSltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLR 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 696 CNGVLEGIRICRKGFPNRILYGDFKQRYRVLnasaIPEGQfIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-765 |
1.83e-161 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 510.49 E-value: 1.83e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGY------RGKKRQEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 172 --NQSILITGESGAGKTVNTKRVIQYFAtiAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLA--SVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 250 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKP-ELIELLLITTNPYDYPFISQGEILVASIDDRE 328
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 329 ELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEV-ADKTAYLMGLNSSDLLKALCFPRVKV 407
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 408 GNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLP--RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEK 485
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 486 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNF 564
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 565 QKPKVVKGKAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAhlyatfattdadggkkkvakkkgss 644
Cdd:cd14901 477 SVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 645 fQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd14901 530 -STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 6981234 725 VLNAS------AIPEGQFIDSKKACEKLLASIDIDHTQykFGHTKVF 765
Cdd:cd14901 609 CLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPPFQ--VGKTKVF 653
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1924 |
1.02e-157 |
|
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: 514.72 E-value: 1.02e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER 926
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 927 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQ 1006
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1007 TLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDF 1086
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1087 EYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNK 1166
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1167 KREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANL 1246
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1247 EKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKA 1326
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1327 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDSEEQVE 1406
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1407 AVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLK 1486
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1487 NAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLEL 1566
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1567 TQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRS 1646
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1647 VQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIH 1726
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1727 TKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLAL 1806
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1807 KGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEA 1886
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 6981234 1887 DEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-767 |
1.25e-156 |
|
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: 496.97 E-value: 1.25e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 106 LKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRG--KKRQEAPPHIFSISDNAYQFMLTDR----ENQSILIT 178
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATI--AATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 256
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATAskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 257 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPyDYPFISQGEIL-VASIDDREELLATDS 335
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAE-SFLFLNQGNCVeVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 336 AIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAD--KTAYLMGLNSSDLLKALCFpRVKVGneyvT 413
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 414 KGQ------TVDQVHHAVNALSKSVYEKLFLWMVTRIN----QQL------DTKLPRQHFIGVLDIAGFEIFEYNSLEQL 477
Cdd:cd14892 321 RGSvleiklTAREAKNALDALCKYLYGELFDWLISRINachkQQTsgvtggAASPTFSPFIGILDIFGFEIMPTNSFEQL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 478 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEK-PMGIFSILEEECMFP-KATDTSFKNKLYD 555
Cdd:cd14892 401 CINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYHQ 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 556 QHLGKSNNFQKPKVvkgkAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNrllahlyatfattdadggkk 635
Cdd:cd14892 480 THLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 636 kvakkkgssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRIL 715
Cdd:cd14892 536 ----------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQ 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981234 716 YGDFKQRYRVL-------NASAIPEGQFIDSKKACEKLLASIDIDHTQykFGHTKVFFK 767
Cdd:cd14892 600 FEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
101-767 |
4.51e-156 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 495.47 E-value: 4.51e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQS--LELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQ-GEILVASIDDREELLATDSAID 338
Cdd:cd14873 160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITAME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFkqkqreeqAEPDGTEVADKTAY-----LMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd14873 239 VMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 414 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 493
Cdd:cd14873 311 TPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 494 MFVLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgkSNN--FQKPKVvk 571
Cdd:cd14873 390 IFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPRV-- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 572 gkAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSnrlLAHLYATFATTDADGGKKKVAKKKGSSFQTVSAL 651
Cdd:cd14873 464 --AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESR---FDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 652 FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL-NASA 730
Cdd:cd14873 539 FKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNLA 618
|
650 660 670
....*....|....*....|....*....|....*..
gi 6981234 731 IPEgqfiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14873 619 LPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-753 |
1.74e-145 |
|
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: 465.55 E-value: 1.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGY-----------RGKKRQEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 167 -LTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 246 GKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIElllittnpydypfisqgeilvasid 325
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 326 dREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA-------DKTAYLMGLNSSDLLK 398
Cdd:cd14900 218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 399 ALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-----DTKLPRQHFIGVLDIAGFEIFEYNS 473
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 474 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNK 552
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 553 LYdQHLGKSNNFQKPKVVKGKaeAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNrllahlyatfattdadg 632
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ----------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 633 gkkkvakkkgssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPN 712
Cdd:cd14900 516 -------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 6981234 713 RILYGDFKQRYRVLNASAIPegqfidsKKACEKLLASIDID 753
Cdd:cd14900 577 RLLHDEFVARYFSLARAKNR-------LLAKKQGTSLPDTD 610
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-767 |
3.09e-145 |
|
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: 464.93 E-value: 3.09e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKK-RQEAPPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLSPSDD----------SDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 261 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEILVASIDDREEL----LATDSA 336
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDIL---GFTPEEKSGLYKLTGAVMHYGNMKFkqkqrEEQAEPDGTEVADKT-----AYLMGLNSSDLLKALCFPRVKVG 408
Cdd:cd14897 232 TNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEYplhavAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 409 NEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF-----IGVLDIAGFEIFEYNSLEQLCINFTN 483
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 484 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDqHLGKSN 562
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 563 NFQKPKvvKGKAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFattdadggkkkvakkkg 642
Cdd:cd14897 465 RYVASP--GNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 643 ssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQR 722
Cdd:cd14897 524 ---------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 6981234 723 YRVLNASaiPEGQFIDSKKACEKLLASIDIDhtQYKFGHTKVFFK 767
Cdd:cd14897 595 YKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-767 |
2.23e-141 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 455.64 E-value: 2.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRG--KKRQEA------PPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEqiIQNGEYfdikkePPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 173 QSILITGESGAGKTVNTKRVIQYFATIAA---------TGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSS 243
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevlTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 244 RFGKFIRIHFG-TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYP--FISQGEIL 320
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRydYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 321 -VASIDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLL 397
Cdd:cd14907 243 eVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 398 KALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--------DTKLPRQHFIGVLDIAGFEIF 469
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 470 EYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF--IDFgMDLAACIELIEK-PMGIFSILEEECMFPKATD 546
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 547 TSFKNKLYDQHlgksNNFQKPKVVKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA 626
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 627 TTDADGGKKKVAKKKGSSFqtVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIC 706
Cdd:cd14907 558 GSQQQNQSKQKKSQKKDKF--LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 707 RKGFPNRILYGDFKQRYRVLNasaipegqfidskkacekllasididhTQYKFGHTKVFFK 767
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-767 |
2.71e-140 |
|
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: 452.09 E-value: 2.71e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATIAAtgdlaKKKDSKMkgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----GRKDKTI-----AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSAI 337
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 338 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVAdKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 417
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 418 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR-QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRiKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 497 LEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQH--LGKSNNFQKPKVVKgka 574
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 575 eAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDAdgGKKKVAKKKGSSFQTVSALFRE 654
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSE--TKEGKSGKGTKAPKSLGSQFKT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 655 NLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEG 734
Cdd:cd14904 543 SLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK 622
|
650 660 670
....*....|....*....|....*....|....
gi 6981234 735 qfiDSKKACEKLLASIDIDHT-QYKFGHTKVFFK 767
Cdd:cd14904 623 ---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-826 |
3.00e-139 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 454.87 E-value: 3.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 62 VETEDNRTLVVKPEDVYAMNPP-KFDKIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVV 140
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 141 DGYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATiAATGDlakkkdskMKGTLED 219
Cdd:PTZ00014 151 RRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGN--------MDLKIQN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 220 QIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELI 299
Cdd:PTZ00014 222 AIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 300 ELLLItTNPYDYPFISQGEILVASIDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE---- 375
Cdd:PTZ00014 302 EKYKL-KSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaai 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 376 -PDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR 454
Cdd:PTZ00014 381 sDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGF 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 455 QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI-----EWTfidfgmDLAACIELI-EKP 528
Cdd:PTZ00014 461 KVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESVIDLLcGKG 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 529 MGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQKPKVVKGKaeaHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVG 608
Cdd:PTZ00014 535 KSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVE 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 609 LYQKSSNRLLAHLYATFATTDADGGKKkvakkkgssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHS 688
Cdd:PTZ00014 611 VVKASPNPLVRDLFEGVEVEKGKLAKG----------QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSS 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 689 LVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAsAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFKA 768
Cdd:PTZ00014 681 KVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDL-AVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKK 759
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 769 GLLGTLEEMRDERLAK---LITRTQAVCRGFLMRvefQKMMQRRESIFCIQYNIRAFMNVK 826
Cdd:PTZ00014 760 DAAKELTQIQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLRRHLVIA 817
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
102-767 |
3.65e-139 |
|
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: 448.97 E-value: 3.65e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFML----TDRENQSILI 177
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 178 TGESGAGKTVNTKRVIQYFATIAatgdlakkkdsKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 257
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-----------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQI---LSNKKPELIELLlittNPYDYPFISQGEilvasidDREELLAT- 333
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGA-------GCKREVQYw 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 334 -------DSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKTAYLMGLNSSDLLKALCFPRV 405
Cdd:cd14889 220 kkkydevCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 406 KVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLdtkLPRQHF------IGVLDIAGFEIFEYNSLEQLCI 479
Cdd:cd14889 300 FTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIEL-IEKPMGIFSILEEECMFPKATDTSFKNKLyDQHL 558
Cdd:cd14889 377 NLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 559 GKSNNFqkpKVVKGKAEAhFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY-ATFATTDADGGKKKV 637
Cdd:cd14889 455 KGNSYY---GKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtATRSRTGTLMPRAKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 638 AKKKGSSF-----QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPN 712
Cdd:cd14889 531 PQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSW 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 713 RILYGDFKQRYRVLnasaIPEGQFIDSKKACEKLLASIDIdhTQYKFGHTKVFFK 767
Cdd:cd14889 611 RPSFAEFAERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-767 |
1.50e-134 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 437.03 E-value: 1.50e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYR--GKKRQ---EAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 170 RENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM-KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELgKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 249 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIL---SNKKPELIELLLITTN----PYDYPFISQGEIL- 320
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggDEEEHEKYEFHDGITGglqlPNEFHYTGQGGAPd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 321 VASIDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQRE---EQAEPDGTEVADKTAYLMGLNSSDLL 397
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEEGNEKCLARVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 398 KALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--DTKLPRQHFIGVLDIAGFEIFEYNSLE 475
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFP-KATDTSFKNKL 553
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 554 YDQHLGKSNN-------FQKPKVVKGKaeAHFSLIHYAGTVDYSV-SGWLEKNKDPLNETVVGLYQKSSNrllahlyatf 625
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ---------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 626 attdadggkkkvakkkgssfqtvsalFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRI 705
Cdd:cd14908 548 --------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 706 CRKGFPNRILYGDFKQRYRVLnASAIPE-----------GQFIDSKKACEKLLASI---------DIDHTQYKFGHTKVF 765
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRML-LPLIPEvvlswsmerldPQKLCVKKMCKDLVKGVlspamvsmkNIPEDTMQLGKSKVF 680
|
..
gi 6981234 766 FK 767
Cdd:cd14908 681 MR 682
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
100-767 |
2.37e-130 |
|
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: 423.69 E-value: 2.37e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRY--TSWMIYTYSGLFCVTVNPYKWLPvyTPEVVDgYRGKKRQEAPPHIFSISDNAYQFMLTDRE---NQS 174
Cdd:cd14891 1 AGILHNLEERSklDNQRPYTFMANVLIAVNPLRRLP--EPDKSD-YINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 175 ILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKG--------TLEDQIISANPLLEAFGNAKTVRNDNSSRFG 246
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSkkrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 247 KFIRIHFGTTG-KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQ-GEILVASI 324
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 325 DDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKAL 400
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 401 CFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFE-YNSLEQLCI 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 480 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHl 558
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 559 GKSNNFQKPKVvKGKAEAhFSLIHYAGTVDYSVSGWLEKNKDplnetvvglyqkssnRLLAHLYATFATtdadggkkkva 638
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNND---------------IIPEDFEDLLAS----------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 639 kkkgssfqtvSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 718
Cdd:cd14891 527 ----------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 719 FKQRYRVLNASAI------PEGQFIdskkacEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14891 597 LVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-723 |
2.28e-128 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 420.84 E-value: 2.28e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP---------VYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 170 RENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-EIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 250 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILVA-----SI 324
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQ-KGGKYELLNSYGPSFArkravAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 325 DDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKqkqrEEQAEPDGTEVA-------DKTAYLMGLNSSDLL 397
Cdd:cd14902 239 KYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDKLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 398 KALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF---------IGVLDIAGFEI 468
Cdd:cd14902 315 TLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFES 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 469 FEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDT 547
Cdd:cd14902 395 LNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 548 SFKNKLYDQHLGksnnfqkpkvvkgkaEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT 627
Cdd:cd14902 474 ALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 628 TDADGGKKKVAKKKGSSFQT--VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRI 705
Cdd:cd14902 539 DSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650
....*....|....*...
gi 6981234 706 CRKGFPNRILYGDFKQRY 723
Cdd:cd14902 619 ARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-767 |
3.22e-126 |
|
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: 412.46 E-value: 3.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRG-KKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATiaatgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS---------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTnPYDYPFISQGEILVASIDDREELLATDSAID 338
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLG-LKEYKFLNPKCLDVPGIDDVADFEEVLESLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ-----AEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd14876 231 SMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 414 KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHH 493
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 494 MFVLEQEEYKKEGI-----EWTfidfgmDLAACIE-LIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKP 567
Cdd:cd14876 391 VFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKL--KSNGKFKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 568 kvVKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDAdggkkkvakkKGSSFQT 647
Cdd:cd14876 463 --AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------KIAKGSL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 648 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 727
Cdd:cd14876 531 IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 6981234 728 AsAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14876 611 L-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-767 |
9.69e-125 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 410.11 E-value: 9.69e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTpevVDGYRGK--KRQEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 170 RENQSILITGESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTT-ATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 250 RIHFG-----TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPE-LIELLLITTNPYDYPFISQGEILVAS 323
Cdd:cd14895 157 RMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQRN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 324 --IDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVA------------------D 383
Cdd:cd14895 237 dgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 384 KTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQ---QLDTKLPRQH---- 456
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSaspQRQFALNPNKaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 457 ----FIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGI 531
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 532 FSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKvvKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQ 611
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 612 KSSNRLLAHLYATF-ATTDADGGKKKVAKKKGSSFQT---VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEH 687
Cdd:cd14895 553 KTSDAHLRELFEFFkASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 688 SLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPegqfidSKKACEKLLASIDIDHTQykFGHTKVFFK 767
Cdd:cd14895 633 AKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-767 |
4.58e-117 |
|
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: 386.06 E-value: 4.58e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATiaatgdLAKKKDSKMKGTLEDQIisanPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTGKL 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSS------LYQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLItTNPYDYPFISQGEIL-VASIDDREELLATDSAID 338
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGACrLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ---AEPDGTEVadKTAYLMGLNSSDLLKALCFPRVKVGN-EYVTK 414
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEI--HTAARLLQVPPERLEGAVTHRVTETPyGRVSR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 415 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF--IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNH 492
Cdd:cd14896 307 PLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 493 HMFVLEQEEYKKEGIEWTFIDfGMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVvk 571
Cdd:cd14896 387 TLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 572 gkAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfattdadgGKKKVAKKKGSSFQTVSAL 651
Cdd:cd14896 463 --PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF----------QEAEPQYGLGQGKPTLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 652 FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAI 731
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*..
gi 6981234 732 PEgqfIDSKKACEKLLASIDIDHTQ-YKFGHTKVFFK 767
Cdd:cd14896 611 EA---LSDRERCGAILSQVLGAESPlYHLGATKVLLK 644
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-726 |
3.76e-114 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 378.42 E-value: 3.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKR-QEAPPHIFSISDNAYQFMLTDRE--NQSILI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 178 TGESGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAS--PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYPFISQGEIlvasidDREELLATDSA 336
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHLPEGAAFSWLPNPERNL------EEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQA---EPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 414 --KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR-QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 490
Cdd:cd14880 315 fkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 491 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKV 569
Cdd:cd14880 395 VAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 570 VKgkaEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATTDADGGKKKVAKKKGSSFQTVS 649
Cdd:cd14880 474 SR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKL---FPANPEEKTQEEPSGQSRAPVLTVV 547
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 650 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 726
Cdd:cd14880 548 SKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-729 |
2.59e-113 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 377.78 E-value: 2.59e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKR-QEAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF-GTTGK 258
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 259 LASADIETYLLEKSRVTFQL-KAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASI------------- 324
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 325 --DDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ---REEQAEPDGTEVADKTAYLMGLNSSDLLKA 399
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 400 LCFPRVKVGNE--YVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQH-----------FIGVLDIAGF 466
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNDlaggsnkknnlFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 467 EIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKAT 545
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 546 DTSFKNKlYDQHLGKSNNFQKPKVVKGKaeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF 625
Cdd:cd14906 482 EQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 626 ATTDADggkkkvAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRI 705
Cdd:cd14906 557 ITSTTN------TTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKV 630
|
650 660
....*....|....*....|....
gi 6981234 706 CRKGFPNRILYGDFKQRYRVLNAS 729
Cdd:cd14906 631 RKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
101-724 |
1.13e-112 |
|
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: 375.97 E-value: 1.13e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGY----------RGKKRQEAPPHIFSISDNAYQFMLTD 169
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 170 RENQSILITGESGAGKTVNTKRVIQYFA-------TIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNS 242
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 243 SRFGKFIRIHF-GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNK----KPELIELLLITTNPYDYPFISQG 317
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 318 --EILVASIDDREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQ--KQREEQAEPDGTEVA----------D 383
Cdd:cd14899 242 lcSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 384 KTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL--------------- 448
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 449 DTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDlAACIELIE-K 527
Cdd:cd14899 402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 528 PMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVV 607
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 608 GLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSFQTVSAL--------FRENLNKLMSNLRTTHPHFVRCIIPNET 679
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 6981234 680 KTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-767 |
8.36e-109 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 362.67 E-value: 8.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 106 LKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQ-----EAPPHIFSISDNAYQFMLTDRENQSILITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYFATIAATGDlakkkdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSS----------TDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVA-SIDDREELLATDSAID 338
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCYDApGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 339 ILgFTPEEKSGLYKLTGAVMHYGNMKFKQKQR---EEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 415
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 416 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 496 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKP-MGIFSILEEECMFPKATDTSFKNKLyDQHLgKSNNFqkpkvVKGK- 573
Cdd:cd14886 395 KSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPGKg 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 574 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKkkvakkkgssfQTVSALFR 653
Cdd:cd14886 467 SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG-----------KFLGSTFQ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL---NASA 730
Cdd:cd14886 536 LSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSS 615
|
650 660 670
....*....|....*....|....*....|....*..
gi 6981234 731 IPEGQfiDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14886 616 QNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-767 |
7.64e-104 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 348.72 E-value: 7.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMI-YTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEA-PPHIFSISDNAY-QFMLTDRENQSILIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIIS----ANPLLEAFGNAKTVRNDNSSRFGKFIRIHF- 253
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSYM-----HSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 254 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILV------ASIDDR 327
Cdd:cd14875 158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 328 EELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQReeqaepDGTEVADKTAYLMGLNSSDLLKAL---CFpR 404
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN------DKAQIADETPFLTACRLLQLDPAKlreCF-L 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 405 VKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKL--PRQHFIGVLDIAGFEIFEYNSLEQLCINFT 482
Cdd:cd14875 311 VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 483 NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGmDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKS 561
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 562 NNFQKPkvvKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGgkkkvakkk 641
Cdd:cd14875 470 PYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK--------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 642 gssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF-K 720
Cdd:cd14875 538 ----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 6981234 721 QRYRVLNASAIPEGQFIDSKKACEKLLAS----IDIDHTQYKFGHTKVFFK 767
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-767 |
1.34e-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: 345.83 E-value: 1.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 182 GAGKTVNTKRVIQYFATIAATGDLAKKKdskmkgtleDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGVLSV---------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELI-ELLLITTNPYDYPFISqgeiLVASIDDRE----ELLATDSA 336
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRtELHLNQLAESNSFGIV----PLQKPEDKQkaaaAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDILGFTPEEKSGLYKLTGAVMHYGN---MKFKQKQREEQAEPdgtEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVT 413
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 414 KGQTVDQVHH------------AVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLE 475
Cdd:cd01386 307 TSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 476 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEECM 540
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 541 FPKATDTSFKNKLYdQHLGKSNNFQKPKVVKgKAEA--HFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQKSSN 615
Cdd:cd01386 467 YPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 616 RLLAHlyatfattdadggkkkvakkKGSSFqtvSALFRENLNKLMSNLRTTHPHFVRCIIPN------ETKTPGA----- 684
Cdd:cd01386 545 ETAAV--------------------KRKSP---CLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPaagde 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 685 -MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL----NASAIPEGQFIDSKKACEKLLASIDIDHTQYKF 759
Cdd:cd01386 602 lLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKSSYRI 681
|
....*...
gi 6981234 760 GHTKVFFK 767
Cdd:cd01386 682 GLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
101-767 |
6.84e-96 |
|
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: 325.62 E-value: 6.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYR---GKKRQEAPPHIFSISDNAYQFMLTDRENQSILI 177
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 178 TGESGAGKTVNTKRVIQYFATiaatgdlakkKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 257
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 K-LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFISQGE----ILVASIDDREELLA 332
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEE-KYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 333 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYV 412
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 413 TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRIN----QQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQ 488
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 489 FFNHHMFVLEQEEYKKEGIEW-TFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP 567
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMeTAYSPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAVYS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 568 KVVKGKAE-------AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYatfattdadggkkkvakk 640
Cdd:cd14878 471 PMKDGNGNvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF------------------ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 641 kGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 720
Cdd:cd14878 533 -QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFL 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 6981234 721 QRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQykFGHTKVFFK 767
Cdd:cd14878 612 SRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQ--MGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-767 |
1.23e-92 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 315.42 E-value: 1.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEvvdgYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 182 GAGKTVNTKRVIQYFATiaatgdlAKKKDSKMKGTLEDqiisANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd14937 79 GSGKTEASKLVIKYYLS-------GVKEDNEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPyDYPFISQGEILVASIDDREELLATDSAIDILG 341
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 342 FTpEEKSGLYKLTGAVMHYGNMKFKQ-----KQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 416
Cdd:cd14937 227 MH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 417 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 496
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 497 LEQEEYKKEGIEWTFIDFGMDlAACIELIEKPMGIFSILEEECMFPKATDTSfknkLYDQHLGKSNNFQKPKVVKGKAEA 576
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 577 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDAdggkkkvakkkGSSFQTVSALFRENL 656
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-----------LGRKNLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 657 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIcRKGFPNRILYGDFKQRYRVLNASAIPEGQF 736
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 6981234 737 IDSKKACEKLLASIDIDhtQYKFGHTKVFFK 767
Cdd:cd14937 609 TDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
101-730 |
8.56e-92 |
|
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: 311.06 E-value: 8.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvytpEVVDGYRGKKRQE-----APPHIFSISDNAYQFMLTdRENQSI 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPY--------ETIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 176 LITGESGAGKTVNTKRVIQYFAtiaatgdlakkKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgt 255
Cdd:cd14898 73 VISGESGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 256 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpelielLLITTNPYDYPFISQGEilVASIDDREELLATDS 335
Cdd:cd14898 140 DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNK--ESIVQLSEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 336 AIDILGFTPEEKsgLYKLTGAVMHYGNMKFKQkqrEEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKG 415
Cdd:cd14898 212 AMKSLGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 416 QTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlpRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 495
Cdd:cd14898 287 NTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 496 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKAT--DTSFKNKLYDQHLgksnnfqkpkvVKGK 573
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGF-----------INTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 574 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGlyqkssNRLLAhlyatfattdadggkkkvakkKGSSFQTVSALFR 653
Cdd:cd14898 433 ARDKIKVSHYAGDVEYDLRDFLDKNREKGQLLIFK------NLLIN---------------------DEGSKEDLVKYFK 485
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 654 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASA 730
Cdd:cd14898 486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-767 |
1.19e-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: 303.49 E-value: 1.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTS--------WMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 172 NQSILITGESGAGKTVNTKRVIQYfatIAATGDLAKKKDSKmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRHGADSQ---GLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 252 HFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtnpYDYPFISQGEILVAsiddreell 331
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAG---EGDPESTDLRRITA--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 332 atdsAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADK---TAYLMGLNS------- 393
Cdd:cd14887 223 ----AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADrshSSEVKCLSSglkvtea 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 394 -----SDLLKALCFPRVKVGNEYV------------TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-------- 448
Cdd:cd14887 299 srkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpse 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 449 -----DTKLPRQ-HFIGVLDIAGFEIFE---YNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFI----DFG 515
Cdd:cd14887 379 sdsdeDTPSTTGtQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsafPFS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 516 MDLAAC--------IELIEKP--------------MGIFSILEEE-CMFPKATDTSFKNKLYDQHLGK----SNNFQKPK 568
Cdd:cd14887 459 FPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 569 VVKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVvglyqkssNRLLahLYATFATTDADGGKKKVAKKKGSSFQTV 648
Cdd:cd14887 539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDEL--------ERLF--LACSTYTRLVGSKKNSGVRAISSRRSTL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 649 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 728
Cdd:cd14887 609 SAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLP 688
|
730 740 750
....*....|....*....|....*....|....*....
gi 6981234 729 SAIPEgqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 767
Cdd:cd14887 689 MALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
97-766 |
4.10e-84 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 290.61 E-value: 4.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 97 LNEPAVLYNLKDRYTSWMIYTY---SGLfcVTVNPYKWLPVYTPEVVDGYR-------GKKRQEAPPHIFSISDNAYQFM 166
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 167 LTDRENQSILITGESGAGKTVNTKRVIQYFATIAAtgdlAKKKDSKmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFG 246
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSS----HSKKGTK----LSSQISAAEFVLDSFGNAKTLTNPNASRFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 247 KFIRIHFGTTGKLASADIETYLLEKSRVTfQLKA-ERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQG---EILVA 322
Cdd:cd14879 151 RYTELQFNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchpLPLGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 323 SIDDRE--ELLATdsAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLLK 398
Cdd:cd14879 230 GSDDAEgfQELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 399 ALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQL-DTKLPRQHFIGVLDIAGFEIF---EYNSL 474
Cdd:cd14879 308 SLTYKTKLVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRsstGGNSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 475 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEEC-MFPKATDTSFKNK 552
Cdd:cd14879 388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLEA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 553 LyDQHLGKSNNF-QKPKVVKGKAEAHFSLIHYAGTVDYSVSGWLEKNKDplnetvvglyqkssnrllahlyatfaTTDAD 631
Cdd:cd14879 467 L-RKRFGNHSSFiAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGD--------------------------VLSPD 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 632 ggkkkvakkkgssfqTVSAL-----FRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRIC 706
Cdd:cd14879 520 ---------------FVNLLrgatqLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 707 RKGFPNRILYGDFKQRYrvlnasaIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFF 766
Cdd:cd14879 585 RVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-715 |
1.00e-73 |
|
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: 261.38 E-value: 1.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYRGKKRQEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 172 NQSILITGESGAGKTVNTKRVIQYFATIaatgdlakKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI--------QTDSQMT-ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 252 HFGT---------TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGE---- 318
Cdd:cd14884 152 IFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 319 --------ILVASIDDREELLATDSA-----IDILGFTPEEK---SGLYKLTGAVMHYGNMKFKQkqreeqaepdgteva 382
Cdd:cd14884 232 rsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDErqiNEFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 383 dkTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRIN----------QQLDTKL 452
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekdESDNEDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 453 PR--QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDfgmdLAACIELIEKPMG 530
Cdd:cd14884 375 YSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDV----APSYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 531 IFSILEEECMFP----KATDTSFKNKLYD----QHLGKSNNFQK--PKVVKGKAEAH------FSLIHYAGTVDYSVSGW 594
Cdd:cd14884 451 IFRRLDDITKLKnqgqKKTDDHFFRYLLNnerqQQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRINNW 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 595 LEKNKDPLNETVVGLYQKSSNRLLahlyatfattdadggKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCI 674
Cdd:cd14884 531 IDKNSDKIETSIETLISCSSNRFL---------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 6981234 675 IPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRIL 715
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
101-749 |
8.50e-70 |
|
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: 248.49 E-value: 8.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPvyTPEVVDGYRGKKRQeapPHIFSISDNAYQFMLTDRENQSILITGE 180
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 181 SGAGKTVNTKRVIQYFATIAATG---DLAKkkdskmkgtledQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFgTTG 257
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGGpetDAFK------------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 258 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKP-ELIELLLITTNPYDYPFISQGEILVASIDDREELLATDSA 336
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQeERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 337 IDILG--FTpeeksGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVaDKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 414
Cdd:cd14881 224 LGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 415 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQqldtkLPRQH----------FIGVLDIAGFEIFEYNSLEQLCINFTNE 484
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANS-----LKRLGstlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 485 KLQQFFNHHMFVLEQEEYKKEGIEwTFIDFG-MDLAACIELIEK-PMGIFSILEEECMfPKATDTSFKNKLYDQHlgKSN 562
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQH--RQN 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 563 N-FQKPKVVKGKAeahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLlahlyaTFATTDADggkkkvakkk 641
Cdd:cd14881 449 PrLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------GFATHTQD---------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 642 gssFQTvsalfreNLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 721
Cdd:cd14881 510 ---FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNA 579
|
650 660
....*....|....*....|....*...
gi 6981234 722 RYRVLnASAIPEGQFIDSKKACEKLLAS 749
Cdd:cd14881 580 RYRLL-APFRLLRRVEEKALEDCALILQ 606
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-719 |
6.43e-68 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 243.85 E-value: 6.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 106 LKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYTPEVVDGYrgKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 185 KTVNTKRVIQYFATIaatgDLAKKKdskmkgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADI 264
Cdd:cd14905 85 KSENTKIIIQYLLTT----DLSRSK------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 265 ETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYpfISQ-GEILVASIDDREELLATDSAIDILGF 342
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGiTDEEKAAYQLGDINSYHY--LNQgGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 343 TPEEKSGLYKLTGAVMHYGNMKFKQKQREeqaepdgTEVADKTAYlmglnsSDLLKALCFPRVKVGNEYVT-KGQTVDQV 421
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISdRSMPVNEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 422 HHAVNALSKSVYEKLFLWMVTRINQQLDtklPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 499
Cdd:cd14905 300 VENRDSLARSLYSALFHWIIDFLNSKLK---PTQysHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 500 EEYKKEGIEW-TFIDFgMDLAACIELIEKpmgIFSILEEECMFPKATDTSFKNKLydqhlgksNNFQKPKVVKGKAEAHF 578
Cdd:cd14905 377 REYQTERIPWmTPISF-KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKPNKF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 579 SLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF----ATTDADGGKKKVAKKKGSSFQTVSALFR- 653
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDGVFninaTVAELNQMFDAKNTAKKSPLSIVKVLLSc 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 654 -----ENLNKLMSN-------------------LRTTHP-------------HFVRCIIPNETKTPGAMEHSLVLHQLRC 696
Cdd:cd14905 525 gsnnpNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKS 604
|
650 660
....*....|....*....|....*..
gi 6981234 697 NGVLEGIRICRKGFP----NRILYGDF 719
Cdd:cd14905 605 LCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
101-726 |
1.63e-66 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 238.62 E-value: 1.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 101 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYrgkkrqeappHIFSISDNAYQFMLTDREN-QSILITG 179
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 180 ESGAGKTVNTKRVIQYfatiaatgdLAKKKDSKMKGTLEDQIISanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 259
Cdd:cd14874 72 ESGSGKSYNAFQVFKY---------LTSQPKSKVTTKHSSAIES---VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 260 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILVASIDDREELLATDSAIDI 339
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 340 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKqREEQAEPDGTEVADKT-----AYLMGLNSSDLLKALcFPRVKVGNEYvtk 414
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMSevkwvAFLLEVDFDQLVNFL-LPKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 415 gqTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLpRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 494
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 495 FVLEQEEYKKEGIEwtfIDFGM----DLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSnnfqkpkv 569
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-------- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 570 VKGKAEA----HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATTDADGGKKKVAKKKGSSF 645
Cdd:cd14874 440 SYGKARNkerlEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVSQAQFILRGAQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 646 QTVsalfrENLNKlmsnlrtTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 725
Cdd:cd14874 520 EIA-----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
.
gi 6981234 726 L 726
Cdd:cd14874 588 L 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-767 |
4.24e-64 |
|
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: 231.55 E-value: 4.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 102 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 182 GAGKTVNTKRVIQYFATIAatgdlakkkdsKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 261
Cdd:cd14882 83 YSGKTTNARLLIKHLCYLG-----------DGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 262 ADIETYLLEKSRVTFQLKAERSYHIFYQILS--NKKPELIELLLITTNPYDYPFISQG-------------EILVASIDD 326
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 327 REELLAtdsaidILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREeqAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVK 406
Cdd:cd14882 232 FEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 407 VGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLdtKLPR-----QHFIGVLDIAGFEIFEYNSLEQLCINF 481
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 482 TNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEecmfpKATDTSFKNKLYDQHLGKS 561
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 562 NNFQKPkvvkgkAEAH-FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATtdadggkkkvakk 640
Cdd:cd14882 457 SQFVKK------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 641 kgSSFQTVSALFR----ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILY 716
Cdd:cd14882 518 --RNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 717 GDFKQRYRVLnasAIPEGQFID-SKKACEKLLasIDIDHTQYKFGHTKVFFK 767
Cdd:cd14882 596 QEFLRRYQFL---AFDFDETVEmTKDNCRLLL--IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-724 |
3.07e-63 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 231.40 E-value: 3.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 103 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQ----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 173 QSILITGESGAGKTVNTKRVIQYFATIAATGDLA--KKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIR 250
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 251 IHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKK--PELIELLLITTNPYDYPFISQGEILVA--SIDD 326
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATnfALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 327 RE--ELLATDSAIDIlgfTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDG--TEVADKTAYLMGLNSSDLLKALCF 402
Cdd:cd14893 244 RDyrDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALKDPAQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 403 ---PRV------------KVGNEYVT--KGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPR---------QH 456
Cdd:cd14893 321 evePVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 457 FIGVLDIAGFEIFE--YNSLEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG--IEWTFIDFGMDLAACIELIE- 526
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEd 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 527 KPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVVKGKAEAH----------FSLIHYAGTVDYSVSGWLE 596
Cdd:cd14893 481 KPFGIFDLLTENCKVRLPNDEDFVNKLFSGN-EAVGGLSRPNMGADTTNEYlapskdwrllFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 597 KNKDPLNETVVGLYQKSSNRLLAHLYA---TFATTDADGGKKKVAKKKGSSFQTVSALFRENLN--------------KL 659
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAVGAaqmAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadAL 639
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 660 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 724
Cdd:cd14893 640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-251 |
7.07e-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: 206.43 E-value: 7.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 122 FCVTVNPYKWLPVYTPEVVDG-YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 201 ATGDLAKKKD-----SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRI 251
Cdd:cd01363 81 FNGINKGETEgwvylTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-765 |
7.12e-48 |
|
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: 184.65 E-value: 7.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 100 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYR-GKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 178
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 179 GESGAGKTVNTKRVIQYFATIA------ATGDLAKKKDSKM-------KGTLEDQIISANPLLEAFGNAKTVRNDNSSRF 245
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVkgsrrlPTNLNDQEEDNIHneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 246 GKFIRIHFGTTgKLASADIETYLLEKSRVTFQLKAERSYHIFYQILsNKKPELIELLLITTNPYDYPFISQGEILVASID 325
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII-NGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 326 DREELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGN-------------MKFKQKQRE----------EQAEPDGTEVA 382
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 383 DKTAYL----MGLNSSDLLKAlcFPRVKVGNEYV-TKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQ---QLDTKLPR 454
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKY--FTTNYIFNDSIlIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 455 QHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM--GIF 532
Cdd:cd14938 397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 533 SILEEECMfPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGKAEAhFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQK 612
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 613 SSNRLLAHLYATFattDADGGKKKVAKKKGSSFQTVSALF---------------RENLNKLMSNLRTTHPHFVRCIIPN 677
Cdd:cd14938 555 SENEYMRQFCMFY---NYDNSGNIVEEKRRYSIQSALKLFkrrydtknqmavsllRNNLTELEKLQETTFCHFIVCMKPN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 678 ETKTP-GAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAsaipegqfiDSKKACEKLLASIDIDHTQ 756
Cdd:cd14938 632 ESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYE 702
|
....*....
gi 6981234 757 YKFGHTKVF 765
Cdd:cd14938 703 WMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1173-1924 |
4.92e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 130.56 E-value: 4.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1173 LKLRRDLEEATLQHEATVATLrKKHADSAAELAEQIDNLQRVKQKLEK-----------EKSEFKLEIDDLSSSVESVSK 1241
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1242 SKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLE 1321
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1322 EENKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRlqds 1401
Cdd:TIGR02168 327 ELESKLDELAEELAE-------LEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQL---- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1402 EEQVEAVNAKCASLEKTKQRLQGEVEDLmvdVERANSLAAALDKKQrnfdkvLAEWKTKCEESQAELEAALKESRSLSTE 1481
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1482 LFKLKNAYEEALDQLETVKRENKNLEQEIA---DLTEQIAENGKSIHELEKSRKQM---------------ELEKADIQM 1543
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDsleRLQENLEGFSEGVKALLKNQSGLsgilgvlselisvdeGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1544 ALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDL 1623
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1624 NEIEI--QLSHANRQAAETIKHLRSVqgQLKDTQLHLDDALRGQEDlKEQLAIVERRANL--LQAEVEELRATLEQTERA 1699
Cdd:TIGR02168 623 GGVLVvdDLDNALELAKKLRPGYRIV--TLDGDLVRPGGVITGGSA-KTNSSILERRREIeeLEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1700 RKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAH 1779
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1780 LERMKKNLEQTVKDLQHRLDEAEQlALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDR 1859
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1860 KNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
840-1453 |
4.39e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.43 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 840 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAK 919
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 920 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKA 999
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1000 LQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDE 1079
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1080 RLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQ--RSDYARELEELSERLEEAGGV 1157
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvlIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1158 TSTQIELNKKREAEFLKLRRDLEEATLQHEAtvatLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVE 1237
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDK----IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1238 SVSKSKANLEKICRTLEDQLSEARGknEETQRSLSELTTQKSRLQTEAGELSRQLEEKEsivsqLSRSKQAFTQQIEELK 1317
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTL--EGEGGSAGGSLTGGSRRELLAALLEAEAELEE-----LAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1318 RQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQR 1397
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1398 LQD-------SEEQVEAVNAKCASLEKTKQRLQGEVEDLM-----VDVERANSLAAALDKKQRNFDKV 1453
Cdd:COG1196 776 IEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNENFQEL 843
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
221-707 |
2.43e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 114.84 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 221 IISANPLLEAFGNAKTVRNDNSSRFGKF--IRIHFGTTG---KLASADIETYLLEKSRVTFQL------KAERSYHIFYQ 289
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 290 ILS--NKKPEL----IELLLITTNPYDYPFISQGEILVASIDDREELLATD--------SAIDILGFTPEEKSGLYKLTG 355
Cdd:cd14894 329 MVAgvNAFPFMrllaKELHLDGIDCSALTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 356 AVMHYGNMKFKQKQREEQAEPDGT---EVADKTAYLMGLNSSDLLKALCFPR-VKVGNEYVTKGQTVD--QVHHAVNALS 429
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 430 KSVYEKLFLWMVTRINQ--------------QLDTKLPRQHFIGVL---DIAGFEIFEYNSLEQLCINFTNEKLqqFFNH 492
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--YARE 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 493 HMFVLEQEEYKKEGIEWtfiDFGMDLaacIELIEKPMGIFSILEEECMFPKATDTSF-----KNKLYDQHLGKSNN--FQ 565
Cdd:cd14894 567 EQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRNSsrLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 566 KPKVVKGKAEAH---------FSLIHYAGTVDYSVSGWLEKNKDPL-NETVVGLYQKSSN---RLLAHLYATFATTDADG 632
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSShfcRMLNESSQLGWSPNTNR 720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 633 GKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICR 707
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
964-1852 |
5.99e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.00 E-value: 5.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 964 KVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLD--DLQAEEDKVnSLSKLKSKLEQQVDDLESSLEQ 1041
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELREL-ELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1042 EKKLRVDLERnkrkLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDeqtlslqLQKKIKELQARIEELEE 1121
Cdd:TIGR02168 248 LKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1122 EIEAERATRAKTEKQRSDYARELEELSERLeeagGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHAD-- 1199
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKL----EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQle 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1200 -SAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVEsvskskanlekicrtlEDQLSEARGKNEETQRSLSELTTQK 1278
Cdd:TIGR02168 393 lQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE----------------EAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1279 SRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENK----AKNALAHALQSSRHDcDLLREQYEEEQEG 1354
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLSGIL-GVLSELISVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1355 KAELQRALSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQDSEEQVEAVNAKCASLEKTKQ 1420
Cdd:TIGR02168 536 EAAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1421 RLQGEVEDLMVDVERANSLAAALDKKQrnfdkvlaewKTKCEESQAELEAALKESRSLSTelfklKNAYEEALDQLETvK 1500
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELAK----------KLRPGYRIVTLDGDLVRPGGVIT-----GGSAKTNSSILER-R 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1501 RENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEK 1580
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1581 DEEIEQLKRNYQRtvetmqgaldaevrsRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDD 1660
Cdd:TIGR02168 757 TELEAEIEELEER---------------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1661 ALRGQEDLKEQLAIVERRANLLQAEVEELRATLEqterarklaeqelldsnervqllhtqntSLIHTKKKLETDLTQLQS 1740
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIE----------------------------SLAAEIEELEELIEELES 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1741 EVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLETRI 1820
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV--------RIDNLQERL 945
|
890 900 910
....*....|....*....|....*....|...
gi 6981234 1821 RELEFELEGEQKRNTESVKG-LRKYERRVKELT 1852
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDdEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1609 |
6.30e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.00 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTL---VQEKNDLQLQVQAESENLLDAEERCD---QLIKAKF-QLEAK 919
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEqqkQILRERLaNLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 920 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKA 999
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1000 LQEAHQQTLDDLQAEEDKVNSLSK-----LKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDK 1074
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1075 QQLDERLKKKDFEYSQLQSKVEDEQTLSLQLqKKIKELQARIEELEEEIEAERATRAKTEKQ--------------RSDY 1140
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEGYEAAieaalggrlqavvvENLN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1141 ARELEELSERLEEAGGVTStqIELNKKREAEFLKLRRDleeaTLQHEATVATLRKKHADSAAEL-------------AEQ 1207
Cdd:TIGR02168 557 AAKKAIAFLKQNELGRVTF--LPLDSIKGTEIQGNDRE----ILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvVDD 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1208 IDNLQRVKQKLEKEKSEFKLEID-------------DLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSEL 1274
Cdd:TIGR02168 631 LDNALELAKKLRPGYRIVTLDGDlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1275 TTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSsrhdcdlLREQYEEEQEG 1354
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-------AEEELAEAEAE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1355 KAELQRALSKANSEVAQWRTKYetdaiqrtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVE 1434
Cdd:TIGR02168 784 IEELEAQIEQLKEELKALREAL--------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1435 RANslaaaldkkqrnfdKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLT 1514
Cdd:TIGR02168 856 SLA--------------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1515 EQIAEngksiHELEKSRKQMELEK------ADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDR------------- 1575
Cdd:TIGR02168 922 EKLAQ-----LELRLEGLEVRIDNlqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeye 996
|
810 820 830
....*....|....*....|....*....|....*..
gi 6981234 1576 KIAEKDEEIEQLKRNYQRTVETMQGA---LDAEVRSR 1609
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAieeIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1639 |
7.92e-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: 113.61 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 845 ETEKEMATMKEEFQKTKDELAKSEAKRKELE------EKLVTLVQEKNDLQLQVQAESenLLDAEERCDQLIKAKFQLEA 918
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLVLR--LEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 919 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKK 998
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 999 ALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLD 1078
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1079 ERLKKKDFEYSQLQSKVE--DEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGG 1156
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1157 VTSTQ------------IELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAelaeqIDNLQRVKQKLE--KEK 1222
Cdd:TIGR02168 494 LERLQenlegfsegvkaLLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAflKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1223 SEFKLEIDDLSSSVEsvskskanlekicRTLEDQLSEARGKNEETQRSLSELTTQKSRLQ----------------TEAG 1286
Cdd:TIGR02168 569 ELGRVTFLPLDSIKG-------------TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNAL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1287 ELSRQLEEKESIVSQ----------LSRSKQAFTQQIEELKRQLEEENKAKNALAhalqssrhdcdllreqyEEEQEGKA 1356
Cdd:TIGR02168 636 ELAKKLRPGYRIVTLdgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELE-----------------EKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1357 ELQrALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdsEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERA 1436
Cdd:TIGR02168 699 ALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARL----EAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1437 NSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQ 1516
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1517 IAENGKSIHELEKSRKQM--ELEKADIQMALEEAEAALEHEEAKILRIQL-ELTQVKSEIDRKIAEKDEEIEQLKRNYQR 1593
Cdd:TIGR02168 854 IESLAAEIEELEELIEELesELEALLNERASLEEALALLRSELEELSEELrELESKRSELRRELEELREKLAQLELRLEG 933
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 6981234 1594 T---VETMQGALDAEVR-SRNEAIRLKKKMEGDLNEIEIQLSHANRQAAE 1639
Cdd:TIGR02168 934 LevrIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1732 |
1.56e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.46 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 836 KIKPLLKSAETEKEMATMKEEfqKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ 915
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAE--LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 916 LEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGL----DETIA 991
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELkeelESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 992 KLTREKKALQEAHQQtlddLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILdlE 1071
Cdd:TIGR02168 359 ELEELEAELEELESR----LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--E 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1072 NDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQR------SDYARELE 1145
Cdd:TIGR02168 433 AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfSEGVKALL 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1146 ELSERLEEAGGVTSTQIELNKKREAEFLK---------LRRDLEEAtlqhEATVATLRKKHADSAAELAEQIDNlqrvKQ 1216
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavVVENLNAA----KKAIAFLKQNELGRVTFLPLDSIK----GT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1217 KLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEArgKNEETQRSLSELTTQKSRLQTEAGEL-------S 1289
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV--DDLDNALELAKKLRPGYRIVTLDGDLvrpggviT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1290 RQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEV 1369
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1370 AQWRTKYETDAIQRTEeLEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLmvdveranslaaaldkkqrn 1449
Cdd:TIGR02168 743 EQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-------------------- 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1450 fdkvlaewktkcEESQAELEAALKEsrsLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEK 1529
Cdd:TIGR02168 802 ------------REALDELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1530 SRKQMELEKAdiqmaleeaeaaleheeakilriqlELTQVKSEIDRKIAEKDEEIEQLkRNYQRTVETMQGALDAEVRSR 1609
Cdd:TIGR02168 867 LIEELESELE-------------------------ALLNERASLEEALALLRSELEEL-SEELRELESKRSELRRELEEL 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1610 NEAIrlkKKMEGDLNEIEIQLSHANRQAAEtikhlrsvqgqlkDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEEL 1689
Cdd:TIGR02168 921 REKL---AQLELRLEGLEVRIDNLQERLSE-------------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 6981234 1690 -RATLEqterarklAEQELLDSNERVQLLHTQNTSLIHTKKKLE 1732
Cdd:TIGR02168 985 gPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1166-1828 |
3.65e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1166 KKREAEfLKLrrdleEATLQHEATVATLRkkhadsaAELAEQIDNLQR----------VKQKL-EKEKSEFKLEIDDLSS 1234
Cdd:COG1196 173 RKEEAE-RKL-----EATEENLERLEDIL-------GELERQLEPLERqaekaeryreLKEELkELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1235 SVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIE 1314
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1315 ELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetdaiqrtEELEEAKKKL 1394
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-----------EELEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1395 AQRLQDSEEQveavnakcaslEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdkvlaewktkcEESQAELEAALKE 1474
Cdd:COG1196 389 LEALRAAAEL-----------AAQLEELEEAEEALLERLERLEEELEELEEAL--------------AELEEEEEEEEEA 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEH 1554
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1555 EEAKILRiqleltqvkseIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAevrsrneAIRLKKKMEGDLNeiEIQLSHAN 1634
Cdd:COG1196 524 GAVAVLI-----------GVEAAYEAALEAALAAALQNIVVEDDEVAAAA-------IEYLKAAKAGRAT--FLPLDKIR 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1635 RQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERV 1714
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1715 QLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDL 1794
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
650 660 670
....*....|....*....|....*....|....
gi 6981234 1795 QHRLDEAEQLALKGGKKQIQKLETRIRELEFELE 1828
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1313-1924 |
1.18e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1313 IEELKRQLEE-ENKAKNAL-AHALQSSRHDCDL---------LREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtdai 1381
Cdd:COG1196 195 LGELERQLEPlERQAEKAErYRELKEELKELEAellllklreLEAELEELEAELEELEAELEELEAELAELEAELE---- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1382 qrteELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKC 1461
Cdd:COG1196 271 ----ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1462 EESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADI 1541
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1542 QmaleeaeaaleHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEG 1621
Cdd:COG1196 427 E-----------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1622 DLNEIEiqlshANRQAAETIKHLRSVQGQLKdtqLHLDDALRGQEDLKEQLAIVERRANLLQAEVeelratLEQTERARK 1701
Cdd:COG1196 496 LLEAEA-----DYEGFLEGVKAALLLAGLRG---LAGAVAVLIGVEAAYEAALEAALAAALQNIV------VEDDEVAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1702 LAEQELLDSNERVQLLHtqnTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE 1781
Cdd:COG1196 562 AIEYLKAAKAGRATFLP---LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1782 RMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESvkgLRKYERRVKELTYQSEEDRKN 1861
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE---LEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1862 VLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLtkfRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELL---EEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
866-1429 |
6.74e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 866 KSEAKRKELEEklvtLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLE 945
Cdd:COG1196 219 KEELKELEAEL----LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 946 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLK 1025
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1026 SKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQL 1105
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1106 QKKIKELQARIEELEEEIEAE----RATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEE 1181
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLeaalAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1182 A--TLQHEATVATLRKKHADSAAELAEQIDNLQRVKQK------LEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTL 1253
Cdd:COG1196 535 AyeAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1254 EDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHA 1333
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1334 LQSsrhdcDLLREQYEEEQEGKAELQRALSKANSEVAQwRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAvnakcA 1413
Cdd:COG1196 695 LEE-----ALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEEELLEEEALEELPEPPDL-----E 763
|
570
....*....|....*.
gi 6981234 1414 SLEKTKQRLQGEVEDL 1429
Cdd:COG1196 764 ELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
832-1529 |
9.48e-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: 106.68 E-value: 9.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 832 KLFFKIKPLLKSAETEKEMAtmKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIK 911
Cdd:TIGR02168 288 KELYALANEISRLEQQKQIL--RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 912 AKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKE-----KHATENKVKNLTEELAGL 986
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEieellKKLEEAELKELQAELEEL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 987 DETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVD---LERNKRKLEGDLKLA 1063
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkaLLKNQSGLSGILGVL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1064 QESILDLENDKQQLDERLKkkdfeySQLQSKVEDEQTLSLQLQKKIKE-------LQARIEELEEEIEAERATRAKTEKQ 1136
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALG------GRLQAVVVENLNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQGNDREILKNIEG 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1137 RSDYARELEELSERLEEAGG--------VTSTQIELNKKREAEFLKL------------------RRDLEEATLQHEATV 1190
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKALSyllggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggSAKTNSSILERRREI 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1191 ATLRKKHADSAAELAEQIDNLQRVKQK---LEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEET 1267
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKEleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1268 QRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQ 1347
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1348 YEEEQEGKAELQRALSKANSEVAQWRTKYETdAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVE 1427
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1428 DLMVDVERAN-SLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEE-------ALDQLETV 1499
Cdd:TIGR02168 919 ELREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEEL 998
|
730 740 750
....*....|....*....|....*....|
gi 6981234 1500 KRENKNLEQEIADLTEQIAENGKSIHELEK 1529
Cdd:TIGR02168 999 KERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1535 |
8.22e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 103.61 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 841 LKSAETEKEMAtmkEEFQKTKDELAKSEAKrkELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLKEKREYEGY--ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 921 KEVTERAED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAK 992
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 993 LTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEN 1072
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1073 DKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLE 1152
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1153 EAG----GVTSTQIELNKKREA----------------------------EFLKlRRDLEEATL-------QHEATVATL 1193
Cdd:TIGR02169 515 VLKasiqGVHGTVAQLGSVGERyataievaagnrlnnvvveddavakeaiELLK-RRKAGRATFlplnkmrDERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1194 RKKHA-DSAAELAEQIDNLQR----------VKQKLEKEKS---EFKL-----EIDDLSSSVESVSKSKANLEKICRTLE 1254
Cdd:TIGR02169 594 SEDGViGFAVDLVEFDPKYEPafkyvfgdtlVVEDIEAARRlmgKYRMvtlegELFEKSGAMTGGSRAPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1255 DQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHAL 1334
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1335 QSSRHDCDLLREQYEEEQEGKAELQRALSKAnsevaqwrtkYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCAS 1414
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDL----------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1415 LEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALD 1494
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 6981234 1495 QLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQME 1535
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1174-1927 |
4.07e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 101.30 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1174 KLRRDLEEAtlqhEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTL 1253
Cdd:TIGR02169 202 RLRREREKA----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1254 EDQLsEARGKNE--ETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALA 1331
Cdd:TIGR02169 278 NKKI-KDLGEEEqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1332 HALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrTKYETDAIQRTEE-LEEAKKKLAQRLQDSEEQVEAVNA 1410
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK--LKREINELKRELDrLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1411 KCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYE 1490
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1491 EALDQLETVK---RENKNLEQEIADLTEQIAEN------------GKSIHELEKSRKQMELEKADIQMALEEAEAALEHE 1555
Cdd:TIGR02169 515 VLKASIQGVHgtvAQLGSVGERYATAIEVAAGNrlnnvvveddavAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1556 EAKILRIQLELTQVKSEI---------DRKIAEKDEEIEQLKRNYqRTVeTMQG-------ALDAEVRSRNEAIRLKKKM 1619
Cdd:TIGR02169 595 EDGVIGFAVDLVEFDPKYepafkyvfgDTLVVEDIEAARRLMGKY-RMV-TLEGelfeksgAMTGGSRAPRGGILFSRSE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1620 EGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERA 1699
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1700 RKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLtqLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAH 1779
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1780 LERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDR 1859
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEK--------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1860 KNVLRLQDLVDKLQVKVKSYKRQAEEADEQanvhLTKFRKAQHELEEAEERADIAESQVNKLRAKTRD 1927
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1254-1932 |
4.69e-20 |
|
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: 97.94 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1254 EDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLE-------EKESIVSQLSRSKQAFTQQIEELKRQLEEENKA 1326
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1327 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQDSEEQVE 1406
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1407 AVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLK 1486
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1487 NAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLEL 1566
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1567 TQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRS 1646
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1647 VQGQLKDTQLHLDDALRGQEDLKEqlaiverRANLLQAEVEELRATLEQTE-RARKLA------EQELLDSNERVQLLHT 1719
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1720 QNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD 1799
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1800 EAEQLALKggkkqIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTyqsEEDRKNVLRLQDLVDKLQvkvksy 1879
Cdd:pfam01576 563 EKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDRAE------ 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1880 kRQAEEADeqanvhlTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSR 1932
Cdd:pfam01576 629 -AEAREKE-------TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
918-1762 |
7.81e-20 |
|
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: 97.06 E-value: 7.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 918 AKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEELAGLDETIAK 992
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 993 LTREkkalqeahqqtlddLQAEEDKVNSLSKLKSKLEQQVDDL--ESSLEQEKKLRvDLERNKRKLEGDLKLAQESILDL 1070
Cdd:TIGR02169 256 LTEE--------------ISELEKRLEEIEQLLEELNKKIKDLgeEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1071 ENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSER 1150
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1151 LEEAGGVTSTQIELNKKREAEFLKLRRDLEEAtlqhEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKleid 1230
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY---- 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1231 dlsssvesvskskaNLEKICRTLEDQLSEArgkneetQRSLSELTTQKSRLQTEAGELSRQLEEKES-------IVSQLS 1303
Cdd:TIGR02169 473 --------------DLKEEYDRVEKELSKL-------QRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1304 RSKQAFTQQIEELKRQ------LEEENKAKNALAHA---------------LQSSRHDCDLLRE-----------QYEEE 1351
Cdd:TIGR02169 532 SVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIELLkrrkagratflplnkMRDERRDLSILSEdgvigfavdlvEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1352 QE-------GKAELQRALSKANSEVAQWR------------------TKYETDAIQRTEELEEAKKKLAQRLQDSEEQVE 1406
Cdd:TIGR02169 612 YEpafkyvfGDTLVVEDIEAARRLMGKYRmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1407 AVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKL- 1485
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELe 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1486 --KNAYEEALDQLETVKREN--KNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQmaleeaeaaleHEEAKILR 1561
Cdd:TIGR02169 772 edLHKLEEALNDLEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-----------KEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1562 IQLELTQVKSEIDRKIAE---KDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAA 1638
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1639 ETIKHLRSVQGQLKdtqlHLDDALRGQEDLKEQLAIVERranlLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLH 1718
Cdd:TIGR02169 921 ELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLED----VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 6981234 1719 TQntslihtKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITD 1762
Cdd:TIGR02169 993 EK-------RAKLEEERKAILERIEEYEKKKREVFMEAFEAINE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1542 |
1.83e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.91 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKND--------------------------------LQLQ 891
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkekreyegyellkekealerqkeaIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 892 VQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAED--EEEIN------AELTAKKRKLEDECSELKKDIDDLELTLA 963
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLrvkekiGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 964 KVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDK----VNSLSKLKSKLEQQVDDLESSL 1039
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1040 EQEKKLRVDLERNK---RKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARI 1116
Cdd:TIGR02169 406 RELDRLQEELQRLSeelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1117 EELEEEIEAERATRAKTEKQRSDYARELEELSERLE---------------------EAGG------------VTSTQIE 1163
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryataieVAAGnrlnnvvveddaVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1164 LNKKRE---AEFLKLRR---------------------DLEEATLQHEATVA-----TLRKKHADSAAELAEQI------ 1208
Cdd:TIGR02169 566 LLKRRKagrATFLPLNKmrderrdlsilsedgvigfavDLVEFDPKYEPAFKyvfgdTLVVEDIEAARRLMGKYrmvtle 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1209 -----------------DNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSL 1271
Cdd:TIGR02169 646 gelfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1272 SELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALqsSRHDCDLLREQYEEE 1351
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1352 QEGKAELQRALSKANSEVA--QWRTKYETDAIQ----RTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE 1425
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNrlTLEKEYLEKEIQelqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1426 VEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDqLETVKRENKN 1505
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQR 962
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 6981234 1506 LEQEIADL-------TEQIAENGKSIHELEKSRKQMELEKADIQ 1542
Cdd:TIGR02169 963 VEEEIRALepvnmlaIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1388-1922 |
3.15e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1388 EEAKKKLAQ------RLQDSEEQVEAvnaKCASLEK------TKQRLQGEVEDLmvdveRANSLAAALDKKQRNFDKV-- 1453
Cdd:COG1196 175 EEAERKLEAteenleRLEDILGELER---QLEPLERqaekaeRYRELKEELKEL-----EAELLLLKLRELEAELEELea 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1454 -LAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRK 1532
Cdd:COG1196 247 eLEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1533 QMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEA 1612
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1613 IRL------KKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEV 1686
Cdd:COG1196 407 EAEeallerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1687 EELRATLEQTERARKLAEQEL-----LDSNERVQLLHTQNTSLIHTKKKLETDLT-----QLQSEVEDASRDARNAEEKA 1756
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEaalaaALQNIVVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1757 KKA-------ITDAAMMAEELKKEQDTSA--HLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFEL 1827
Cdd:COG1196 567 KAAkagratfLPLDKIRARAALAAALARGaiGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1828 EGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEA 1907
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570
....*....|....*
gi 6981234 1908 EERADIAESQVNKLR 1922
Cdd:COG1196 727 EEQLEAEREELLEEL 741
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1002-1802 |
5.16e-19 |
|
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: 94.41 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1002 EAHQQTLDDLQAEEDKVNSL-SKLKSKLEQQVDDLESSLEQ---EKKLRVDLERNKRKLEGDLK-LAQESILDLENDKQQ 1076
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRnQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1077 LDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARieeleeeieaeratrakteKQRSDYARELEELSERLEEAGG 1156
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEA-------------------SGKKIYEHDSMSTMHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1157 VTSTQIELNKkrEAEFLKLRrdleeaTLQHEATVATLRKKHADSAAELaeqidnLQRVKQKLEKEKSEFKLEIDDLSSSV 1236
Cdd:pfam15921 222 ISKILRELDT--EISYLKGR------IFPVEDQLEALKSESQNKIELL------LQQHQDRIEQLISEHEVEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1237 ESVSKSKANLEKICRTLEDQlseARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEK-ESIVSQLSRSKQAFTQQIEE 1315
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1316 LKRQLEEENKAKNALAHAL---QSSRHDCDLLREQYE---EEQEGKA----ELQRALSKANSEVaqwrtkyetdaiQRTE 1385
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLadlHKREKELSLEKEQNKrlwDRDTGNSitidHLRRELDDRNMEV------------QRLE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1386 ELEEAKKKLAQ--------RLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDL------MVDVERANS-LAAALDKKQRNF 1450
Cdd:pfam15921 433 ALLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtLESSERTVSdLTASLQEKERAI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1451 DKVLAEwktkCEESQAELEAALKESRSLSTELFKLKNAYEE--ALD-QLETVKRENKNLEQEIADLTEQIAENGKSIHEL 1527
Cdd:pfam15921 513 EATNAE----ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEceALKlQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1528 EKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQ-----LELTQVK-----SEIDRKIAEKDEEIEQLKRNYQRTVET 1597
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQLLNEVKTSRNE 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1598 MQG-ALDAEVRSRNeaIRLK-KKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGqlkdTQLHlddALRGQEDLKEQLAIV 1675
Cdd:pfam15921 669 LNSlSEDYEVLKRN--FRNKsEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEG----SDGH---AMKVAMGMQKQITAK 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1676 ERRANLLQAEVEELRATLEQTERARKLAEQElldSNERVQLLHTQNTSlihtKKKLETDLTQLQSEVEDASRDARNAEEK 1755
Cdd:pfam15921 740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEE---KNKLSQELSTVATE----KNKMAGELEVLRSQERRLKEKVANMEVA 812
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 6981234 1756 AKKAITDAAMMAEELKKEQDTSAHLErmkknleqtvkdLQHRLDEAE 1802
Cdd:pfam15921 813 LDKASLQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1247-1924 |
1.07e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.59 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1247 EKICRTLEDqLSEARGKNEETQRSLSELTTQKSRLQTEAG------ELSRQLEEKE-----SIVSQLSRSKQAFTQQIEE 1315
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEgyellKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1316 LKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKA-ELQRALSKANSEVAQWRtkyetDAIqrtEELEEAKKKL 1394
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIASLE-----RSI---AEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1395 AQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKE 1474
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQmaleeaeAALEH 1554
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE-------QELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1555 EEAKILRIQLELTQVKSEIDRKIAEKDE---------------------------EIEQLKRNYQRTVETMQGA-LDAEV 1606
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARAseervrggraveevlkasiqgvhgtvaQLGSVGERYATAIEVAAGNrLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1607 RSRN----EAIRLKKKMEG-------------------------------DLNEIEIQLSHANRQA------AETIKHLR 1645
Cdd:TIGR02169 554 VEDDavakEAIELLKRRKAgratflplnkmrderrdlsilsedgvigfavDLVEFDPKYEPAFKYVfgdtlvVEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1646 SVQGQLKDTQLHLD------------DALRGQE----DLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLD 1709
Cdd:TIGR02169 634 RLMGKYRMVTLEGElfeksgamtggsRAPRGGIlfsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1710 SNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknleq 1789
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR------ 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1790 tvkDLQHRLDEAEQLALKgGKKQIQKLETRIRELE-------FELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNV 1862
Cdd:TIGR02169 788 ---LSHSRIPEIQAELSK-LEEEVSRIEARLREIEqklnrltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1863 LRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
831-1435 |
1.45e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 831 MKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDlQLQVQAEsENLLDAEERCDQLI 910
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAE-EAKKKADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 911 KAKFQLEAKIKEvTERAEDEEEINAEltaKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKnlTEELAGLDETI 990
Cdd:PTZ00121 1340 EAKKAAEAAKAE-AEAAADEAEAAEE---KAEAAEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADEL 1410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 991 AKLTREKKALQEAHQqtlddlQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKlrvdLERNKRKLEgDLKLAQESILDL 1070
Cdd:PTZ00121 1411 KKAAAAKKKADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK----AEEAKKKAE-EAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1071 ENDKQQldERLKKKDFEysqlQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEaeratRAKTEKQRSDYARELEELSER 1150
Cdd:PTZ00121 1480 EEAKKA--DEAKKKAEE----AKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-----KKAEEAKKADEAKKAEEKKKA 1548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1151 LeeaggvtstqiELNKKREAEFLKLRRDLEEATLQHEATVATLRKkhadsaAELAEQIDNlQRVKQKLEKEKSEFKLEID 1230
Cdd:PTZ00121 1549 D-----------ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKAEE-ARIEEVMKLYEEEKKMKAE 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1231 DLSSSVESVSKskanlekicrtledqlSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFT 1310
Cdd:PTZ00121 1611 EAKKAEEAKIK----------------AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1311 QQIEELKRQLEEENKAKNALAHALQSSRhDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEEL--- 1387
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkd 1752
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 6981234 1388 EEAKKKLAQRLQDSEEQVEAVNAKCASLekTKQRLQGEVEDLMVDVER 1435
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDK 1798
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
973-1591 |
1.54e-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: 89.31 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 973 ENKVKNLTEELAGLDETIAKLTREKKALQEahqqtlDDLQAEEDKVNSLSKLKsKLEQQVDDLESSLEQEKKLRVDLERN 1052
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDK------NLNKDEEKINNSNNKIK-ILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1053 KRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAK 1132
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1133 TEKQRSDyareleelserleeaggvtstqieLNKKREAEFLKLrrdleeatlqheATVATLRKKHAdsaaELAEQIDNLQ 1212
Cdd:TIGR04523 185 IQKNIDK------------------------IKNKLLKLELLL------------SNLKKKIQKNK----SLESQISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1213 RVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQL 1292
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1293 EEkeSIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQW 1372
Cdd:TIGR04523 305 EQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1373 RtkyetdaiQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDK 1452
Cdd:TIGR04523 383 K--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1453 VLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRK 1532
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981234 1533 QMELEKADIQmaleeaeaaleheeAKILRIQLELTqvKSEIDRKIAEKDEEIEQLKRNY 1591
Cdd:TIGR04523 535 EKESKISDLE--------------DELNKDDFELK--KENLEKEIDEKNKEIEELKQTQ 577
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
845-1535 |
5.07e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.27 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 845 ETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQlEAKIKEVT 924
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 925 ERAEDEEEINAELTAKK-------RKLED--------------ECSELKKDIDDLEL-TLAKVEKEKHATE-----NKVK 977
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEvrkaeelRKAEDarkaeaarkaeeerKAEEARKAEDAKKAeAVKKAEEAKKDAEeakkaEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 978 NLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKK---LRVDLERNKR 1054
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1055 KLEGDLKLAQESILDLENDKQQldERLKKKDFEYSQLQS-----KVEDEQTLSLQLQKKIKELQARIEELEEEIEAERAT 1129
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAE--AEAAADEAEAAEEKAeaaekKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1130 ----RAKTEKQRSDYARELEELSERLEEAggvtstQIELNKKREAEflKLRRDLEEATLQHEATVATLRKKHADSAAELA 1205
Cdd:PTZ00121 1408 delkKAAAAKKKADEAKKKAEEKKKADEA------KKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1206 EQIDNLQRVKQKLE---------KEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELtt 1276
Cdd:PTZ00121 1480 EEAKKADEAKKKAEeakkkadeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL-- 1557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1277 QKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYE------- 1349
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkveq 1637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1350 -----EEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEEL---EEAKKKLAQRLQDSEEQ---VEAVNAKCASLEKT 1418
Cdd:PTZ00121 1638 lkkkeAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKK 1717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1419 KQRLQGEVEDLMVDVERAnslaaaldKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAY-EEALDQLE 1497
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEED 1789
|
730 740 750
....*....|....*....|....*....|....*....
gi 6981234 1498 TVKR-ENKNLEQEIADLTEQIAENGKSIHELEKSRKQME 1535
Cdd:PTZ00121 1790 EKRRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME 1828
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1301-1906 |
1.16e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 86.71 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1301 QLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVaqwrtkyeTDA 1380
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1381 IQRT-EELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQrlqgEVEDLMVDVERANSlaaaldkkqrnfdKVLAEWKT 1459
Cdd:pfam15921 147 LQNTvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG-------------KKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1460 KCEESQAELEAAL-KESRSLSTELFKLKNAYEEALDQLETVKRENKN----LEQEIADLTEQIAengkSIHELE------ 1528
Cdd:pfam15921 210 MSTMHFRSLGSAIsKILRELDTEISYLKGRIFPVEDQLEALKSESQNkielLLQQHQDRIEQLI----SEHEVEitglte 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1529 ---KSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAE 1605
Cdd:pfam15921 286 kasSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1606 VRSRNEAIRLK---KKMEGDLNEIEIQLSHANRQAAE----------TIKHLR----------------------SVQGQ 1650
Cdd:pfam15921 366 DQFSQESGNLDdqlQKLLADLHKREKELSLEKEQNKRlwdrdtgnsiTIDHLRrelddrnmevqrleallkamksECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1651 LKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRA---TLEQTERARKLAEQELldsNERVQLLHTQNTSLIHT 1727
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAkkmTLESSERTVSDLTASL---QEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1728 KKKLETDLTQLQ--SEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQD-----------TSAHLERMKKNLEQTVKDL 1794
Cdd:pfam15921 523 RSRVDLKLQELQhlKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrTAGAMQVEKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1795 QHRLDEAEQLALKGGKKqIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNvlrLQDLVDKLQV 1874
Cdd:pfam15921 603 RLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE---LNSLSEDYEV 678
|
650 660 670
....*....|....*....|....*....|..
gi 6981234 1875 KVKSYKRQAEEADEQANVHLTKFRKAQHELEE 1906
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
842-1596 |
2.32e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKElEEKLVTL---VQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEA 918
Cdd:PTZ00121 1118 EEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIarkAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKA 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 919 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKdiddleLTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKK 998
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK------AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 999 ALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKK---LRVDLERNKRKLEGDLKLAQESILDLENDKQ 1075
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1076 QldERLKKKDFEYSQLQSKVEDEQTLslQLQKKIKELQARIEELEEEIEAERatRAKTEKQRSDYARELEELSERLEEAg 1155
Cdd:PTZ00121 1351 E--AEAAADEAEAAEEKAEAAEKKKE--EAKKKADAAKKKAEEKKKADEAKK--KAEEDKKKADELKKAAAAKKKADEA- 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1156 gvtstQIELNKKREAEflKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKsefkleiddlsss 1235
Cdd:PTZ00121 1424 -----KKKAEEKKKAD--EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK------------- 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1236 vesvskskanlekicrtledQLSEARGKNEETQRSLSELTtQKSRLQTEAGELSRQLEEKESivSQLSRSKQAftQQIEE 1315
Cdd:PTZ00121 1484 --------------------KADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAKKA--DEAKKAEEA--KKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1316 LKRQlEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLA 1395
Cdd:PTZ00121 1539 AKKA-EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1396 QRLQDSE-EQVEAVNAKCASLEKTKQRLQGEVEDLMvDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKE 1474
Cdd:PTZ00121 1618 AKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSrkqmELEKADIQMALEEAEAALEH 1554
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEE 1772
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 6981234 1555 EEAKILRIQLEltQVKSEIDRKIAEKDEEIEQLKRNYQRTVE 1596
Cdd:PTZ00121 1773 IRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1078-1839 |
2.40e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1078 DERLK--KKDFEYSQLQSKVEDEQTLslQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAg 1155
Cdd:PTZ00121 1069 DEGLKpsYKDFDFDAKEDNRADEATE--EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEA- 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1156 gvtstqielNKKREAEFLKLRRDLEEATLQHEATVATLRKKHadSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSS 1235
Cdd:PTZ00121 1146 ---------RKAEDAKRVEIARKAEDARKAEEARKAEDAKKA--EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1236 VESVSKSKANLEKICRTLEdqlsEARGKNEETQRSLSELTTQKSRLQTEA-------------GELSRQLEE---KESIV 1299
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAE----EAKKDAEEAKKAEEERNNEEIRKFEEArmahfarrqaaikAEEARKADElkkAEEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1300 SQLSRSKQAFTQQIEELKRQLEEENKAKNALAHAlQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETD 1379
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1380 AIQRTEE---LEEAKKKLAQRLQDSEEQVEAVNAKCASLE-KTKQRLQGEVEDLMVDVERANSLAAAldKKQRNFDKVLA 1455
Cdd:PTZ00121 1370 EKKKEEAkkkADAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1456 EWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEiADLTEQIAENGKSIHELEKSRKQME 1535
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1536 LEKADIQMALEEAEAALEHEEAKILRIQLELTqvKSEIDRKIAEKDEEiEQLKRNYQRTVETMQGALDAEVRSRNEAIRL 1615
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1616 KKKMEGDlneiEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQ 1695
Cdd:PTZ00121 1604 EKKMKAE----EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1696 TERA----RKLAEQELLDSNErvqllhtqntslihtKKKLEtdltQLQSEVEDASRDArnaeEKAKKAITDAAMMAEELK 1771
Cdd:PTZ00121 1680 AKKAeedeKKAAEALKKEAEE---------------AKKAE----ELKKKEAEEKKKA----EELKKAEEENKIKAEEAK 1736
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1772 KEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVK 1839
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1188-1696 |
5.98e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1188 ATVATLRKKhadsAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKicrtLEDQLSEARGKNEET 1267
Cdd:PRK02224 206 ERLNGLESE----LAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED----LRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1268 QRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQ 1347
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1348 YEEEQEGKAELQRALSKANSEVAQWRTkyetdaiqRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVE 1427
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRRE--------EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1428 DLMVDVEranSLAAALDKKQRNFDK-----------------VLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAyE 1490
Cdd:PRK02224 430 ELEATLR---TARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-V 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1491 EALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVK 1570
Cdd:PRK02224 506 EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1571 SEIDR--KIAEKDEEIEQLKRNYQRTVETMQG--ALDAEVRSRNEAIRLKKK-MEGDLNEIEIQLSHANRQAAETikHLR 1645
Cdd:PRK02224 586 ERIESleRIRTLLAAIADAEDEIERLREKREAlaELNDERRERLAEKRERKReLEAEFDEARIEEAREDKERAEE--YLE 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1646 SVQGQLKDTQLHLDD----------ALRGQEDLKEQLAIVER----------------------RANLLQAEVEELRATL 1693
Cdd:PRK02224 664 QVEEKLDELREERDDlqaeigavenELEELEELRERREALENrvealealydeaeelesmygdlRAELRQRNVETLERML 743
|
...
gi 6981234 1694 EQT 1696
Cdd:PRK02224 744 NET 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
979-1794 |
2.57e-15 |
|
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: 82.42 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 979 LTEELAGLDETIAKLtrekkalqeahQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESslEQEKKLRVD-LERNKRKLE 1057
Cdd:TIGR02169 158 IIDEIAGVAEFDRKK-----------EKALEELEEVEENIERLDLIIDEKRQQLERLRR--EREKAERYQaLLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1058 GDLKLAQesILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQarieeleeeieaeratrAKTEKQR 1137
Cdd:TIGR02169 225 GYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN-----------------KKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1138 SDYARELEELSerleeagGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQidnlQRVKQK 1217
Cdd:TIGR02169 286 EEEQLRVKEKI-------GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE----RKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1218 LEKEKSEFKLEIDDLsssvesvSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKES 1297
Cdd:TIGR02169 355 LTEEYAELKEELEDL-------RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1298 IVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1377
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1378 TDAIQRTE-------------ELEEAKKKLA--------QRLQDSEEQVEAVNAKCASLEKTKQ----------RLQGEV 1426
Cdd:TIGR02169 508 GGRAVEEVlkasiqgvhgtvaQLGSVGERYAtaievaagNRLNNVVVEDDAVAKEAIELLKRRKagratflplnKMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1427 EDL--------------MVDVER---------------ANSLAAA----------------LDK---------KQRNFDK 1452
Cdd:TIGR02169 588 RDLsilsedgvigfavdLVEFDPkyepafkyvfgdtlvVEDIEAArrlmgkyrmvtlegelFEKsgamtggsrAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1453 VLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRK 1532
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1533 QMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDR-KIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNE 1611
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1612 AIRLKKKMEG---DLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLddalrgqEDLKEQLAIVERRANLLQAEVEE 1688
Cdd:TIGR02169 828 KEYLEKEIQElqeQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------RDLESRLGDLKKERDELEAQLRE 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1689 LRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLET------DLTQLQSEVEDASRDARNAEEKAKKAITD 1762
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQE 980
|
890 900 910
....*....|....*....|....*....|..
gi 6981234 1763 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDL 1794
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1205-1908 |
3.21e-15 |
|
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: 81.94 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1205 AEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARgKNEETQRSLSELTTQKSRLQTE 1284
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1285 AGELSRQLEEKESIVSQLSRSKQAFTQQ-----IEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQ 1359
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRArkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1360 RALSKANSEVAQW-RTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVedlmvdveranS 1438
Cdd:TIGR00618 342 EQRRLLQTLHSQEiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ-----------A 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1439 LAAALDKKQRNFDKVLAEWKTKCEESQAELEaalkESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIA 1518
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAE----LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1519 ENGKSIHE--LEKSRKQMELEKADIQMALEEAEAALE-HEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKR---NYQ 1592
Cdd:TIGR00618 487 RKKAVVLArlLELQEEPCPLCGSCIHPNPARQDIDNPgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASlkeQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1593 RTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQL 1672
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1673 AIVERRANLLQAEVEE-LRATLEQTERARKLAEQELLDSNERVQllhtqntSLIHTKKKLETDLTQLQSEVEDASRDARN 1751
Cdd:TIGR00618 647 ALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKE-------QLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1752 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ---IQKLETRIRELEfELE 1828
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAEIQFFNRLRE-EDT 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1829 GEQKRNTESVKGLRKYERRVKELT-YQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEA 1907
Cdd:TIGR00618 799 HLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
.
gi 6981234 1908 E 1908
Cdd:TIGR00618 879 N 879
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
964-1864 |
4.10e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 81.56 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 964 KVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAhqqtlDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEK 1043
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEET-----ENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1044 KLRVDLER----NKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEEL 1119
Cdd:pfam02463 218 KLELEEEYllylDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1120 EEEIEAERATRAKTEKQRSDYARELEELSERleeaggvtstQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHAD 1199
Cdd:pfam02463 298 LKSELLKLERRKVDDEEKLKESEKEKKKAEK----------ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1200 SAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKS 1279
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1280 RLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQ 1359
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1360 RALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQ--VEAVNAKCASLEKTKQRLQGEVEDLMVDVERAN 1437
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElpLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1438 SLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLS--TELFKLKNAYEEALDQLETVKRENKNLEQEIADLTE 1515
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRkgVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1516 QIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTV 1595
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1596 ETMQGALDAEVRsRNEAIRLKKKMEGDLNEIEIQLSHANRQAAEtikhlrsvqgQLKDTQLHLDDALRGQEDLKEQLAIV 1675
Cdd:pfam02463 768 ELSLKEKELAEE-REKTEKLKVEEEKEEKLKAQEEELRALEEEL----------KEEAELLEEEQLLIEQEEKIKEEELE 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1676 ERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDarnaEEK 1755
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL----NLL 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1756 AKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNT 1835
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
890 900
....*....|....*....|....*....
gi 6981234 1836 ESVKGLRKYERRVKELTYQSEEDRKNVLR 1864
Cdd:pfam02463 993 DELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
842-1456 |
6.25e-15 |
|
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: 80.88 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIK 921
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 922 EVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQ 1001
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYA 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1002 EAHQQTL----------DDLQAEE------------------DKVNSLSKLKSKLEQQ--VDDLESSLEQEKKLRV---- 1047
Cdd:TIGR02169 539 TAIEVAAgnrlnnvvveDDAVAKEaiellkrrkagratflplNKMRDERRDLSILSEDgvIGFAVDLVEFDPKYEPafky 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1048 ---------DLERNKR--------KLEGDL--------------KLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVE 1096
Cdd:TIGR02169 619 vfgdtlvveDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1097 DEQTLSLQLQKKIKELQarieeleeeieaeratrAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLR 1176
Cdd:TIGR02169 699 RIENRLDELSQELSDAS-----------------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1177 rDLEEATLQHEATVATLRKKHADSAAELA-EQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLED 1255
Cdd:TIGR02169 762 -ELEARIEELEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1256 QLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEenkaknalahalq 1335
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE------------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1336 ssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQ-----WRTKYETDAIQRTEELEEAKKKLAQRLQDSE-------E 1403
Cdd:TIGR02169 908 --------LEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQ 979
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1404 QVEAVNAKCASLEKTKQRLQGEVEDL-----MVDVERANSLAAALDKKQRNFDKVLAE 1456
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
850-1701 |
1.23e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.02 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 850 MATMKEEFQKTKDELA---KSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLD-AEERCDQLIKAKFQLEAKIKEVTE 925
Cdd:pfam02463 147 IAMMKPERRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 926 RAEDEEEINAE----LTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQ 1001
Cdd:pfam02463 227 LYLDYLKLNEEridlLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1002 EAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSL-------EQEKKLRVDLERNKRKLEgdlkLAQESILDLENDK 1074
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELkeleikrEAEEEEEEELEKLQEKLE----QLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1075 QQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEA 1154
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1155 GGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSS 1234
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1235 SVESVSKSKANLEKICRTLEDQLSEARG-----------------KNEETQRSLSELTTQKSRLQTEAGELSRQLEEKES 1297
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALtelplgarklrllipklKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1298 IVSQLSRSKQAFTQQIEELKRqLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE 1377
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKA-KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1378 TDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVEranslaaALDKKQRNFDKVLAEW 1457
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK-------KEEKEEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1458 KTKCEESQAELEAALKESRSLSTEL-FKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMEL 1536
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQeEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1537 EKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKR--NYQRTVETMQGALDAEVRSRNEAIR 1614
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQklNLLEEKENEIEERIKEEAEILLKYE 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1615 LKKKMEGDLNEIEIQLSHANRQAAEtIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLE 1694
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEE-ERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
....*..
gi 6981234 1695 QTERARK 1701
Cdd:pfam02463 1014 ETCQRLK 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
897-1483 |
1.42e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 897 ENLLDAEERCDQLIKAKFQ-LEAKIKEVTERAEDEEEINAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 975
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 976 VKNLTEELAGLDETIAKLTREKK-------------ALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLES---SL 1039
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKelkelkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1040 EQEKKLRVDLERNKRKLEGDLKLAQEsILDLENDKQQLDERLKKKDFEysQLQSKVEDEQTLSLQLQKKIKELQARIEEL 1119
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEE-AKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1120 EEEIEAERATRAKTEKQRS---------DYARELEELSERLEEAGGVTSTQIELNKKREaeflKLRRDLE--EATLQHEA 1188
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKER----KLRKELRelEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1189 TVATLRkkhadsaaELAEQIDNLQRVKQKLEKEKSEFKLEiddlssSVESVSKSKANLEKICRTLEDQLSEArgknEETQ 1268
Cdd:PRK03918 494 ELIKLK--------ELAEQLKELEEKLKKYNLEELEKKAE------EYEKLKEKLIKLKGEIKSLKKELEKL----EELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1269 RSLSELTTQKSRLQTEAGELSRQLEEKEsivsqlSRSKQAFTQQIEELKRQLEEENKAKNAlAHALQSSRHDCDLLREQY 1348
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELG------FESVEELEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1349 EEEQEGKAELQRALSKANSEVAQWRTKYETDaiqRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVED 1428
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEE---EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1429 LMVDVERANSLAAALDKKQRNFDKVlAEWKTKCEesqaelEAALKESRSLSTELF 1483
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKV-KKYKALLK------ERALSKVGEIASEIF 753
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
836-1330 |
1.70e-14 |
|
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: 79.29 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ 915
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 916 LEAKIKEVTERAEDEEEINAELT---AKKRKLEDECSELKKDIDDLELTLAKVE---------------------KEKHA 971
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 972 TENKVKNLTEELAGLDETIAKLTREKKalQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLER 1051
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1052 NKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRA 1131
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1132 KTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATL------RKKHADSAAELA 1205
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEEKVKDLT 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1206 EQIDNLQRVKQKLEKEKSEFKLEIDDLSS--SVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQT 1283
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 6981234 1284 EAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNAL 1330
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1199-1872 |
1.81e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1199 DSAAELAEQIDNLQRVKQKLEKEKSEfkleIDDLSSSVESVSKSKANLEKIcRTLEDQLSEARGKNEETQRSL-----SE 1273
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQ----IELLEPIRELAERYAAARERL-AELEYLRAALRLWFAQRRLELleaelEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1274 LTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAF-TQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQ 1352
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1353 EGKAELQRALSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQD--------SEEQVEAVNAKCASLEKTKQR 1421
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEealAEAEAALRDLRRELRELEAEIASlerrksniPARLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1422 L----------------QGEVE--------DLMVDVERANSLAAALDK---KQR-NFDKVlaewktkcEESQAELEAALK 1473
Cdd:COG4913 460 LpfvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1474 ESRSLSTEL-FKLKNAYE---------------EALDQLETVKR-------------------------------EN--- 1503
Cdd:COG4913 532 DPDSLAGKLdFKPHPFRAwleaelgrrfdyvcvDSPEELRRHPRaitragqvkgngtrhekddrrrirsryvlgfDNrak 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1504 -KNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQmaleeaeaaleheeaKILRIQLELTQVKSeIDRKIAEKDE 1582
Cdd:COG4913 612 lAALEAELAELEEELAEAEERLEALEAELDALQERREALQ---------------RLAEYSWDEIDVAS-AEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1583 EIEQLKRNyqrtvetmqgaldaevrsrneairlkkkmEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDAL 1662
Cdd:COG4913 676 ELERLDAS-----------------------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1663 RGQEDLKEQLAIVERRANL-LQAEVEELRATLEQTERARKLAEQelldsnervqlLHTQNTSLIHTKKKLETDLTQLQSE 1741
Cdd:COG4913 727 EELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELREN-----------LEERIDALRARLNRAEEELERAMRA 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1742 --------VEDASRDARNAEEKAKkaitdaamMAEELkKEQDTSAHLERMKKNLEQT----VKDLQHRLDEAEQLAlkgg 1809
Cdd:COG4913 796 fnrewpaeTADLDADLESLPEYLA--------LLDRL-EEDGLPEYEERFKELLNENsiefVADLLSKLRRAIREI---- 862
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1810 KKQIQKLETRIRELEF------ELEGEQKRNTEsvkgLRKYERRVKELT-----YQSEEDRKNVLRLQDLVDKL 1872
Cdd:COG4913 863 KERIDPLNDSLKRIPFgpgrylRLEARPRPDPE----VREFRQELRAVTsgaslFDEELSEARFAALKRLIERL 932
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
916-1445 |
1.94e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.31 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 916 LEAKIKEVTERAE--DEEEINAELT--------AKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAG 985
Cdd:PRK02224 211 LESELAELDEEIEryEEQREQARETrdeadevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 986 LDETIAKLtREKKALQEAHQQTLDDLQAEedkvnslsklkskLEQQVDDLESSLEQEkklRVDLERNKRKLEGdlklAQE 1065
Cdd:PRK02224 291 LEEERDDL-LAEAGLDDADAEAVEARREE-------------LEDRDEELRDRLEEC---RVAAQAHNEEAES----LRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1066 SILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDyarele 1145
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE------ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1146 elserleEAGGVTSTQIELNKKREAefLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEF 1225
Cdd:PRK02224 424 -------LREREAELEATLRTARER--VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1226 KLEIDDLSSSVESVSKSKANLEKIcRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRS 1305
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1306 KQAFTQQIEELKRQLEEENKAKNALAhALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIqrtE 1385
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---E 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1386 ELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDK 1445
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
955-1542 |
2.05e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 955 IDDLELTLAKVEKEKHATENKVKNLTEELAGlDETIAKLTREKKalqeahqqtlDDLQAEEDKVNSLSKLKSKLEQQVDD 1034
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKE----------KELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1035 LESSLEQEKKLRV---DLERNKRKLEGDLKlaqesilDLENDKQQLDERLKKKDFEYSQLQSKVEDeqtlslqlQKKIKE 1111
Cdd:PRK03918 226 LEKEVKELEELKEeieELEKELESLEGSKR-------KLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1112 LQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKK-----REAEFLKLRRDLEEATLQH 1186
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKlkeleKRLEELEERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1187 EATVATLRKKHAD-SAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEK---ICRTLEDQLSEARG 1262
Cdd:PRK03918 371 KEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1263 KN--EETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSR--SKQAFTQQIEELKRQLEEENKAKNALAHalqssr 1338
Cdd:PRK03918 451 KEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKA------ 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1339 hdcdllrEQYEEEQEGKAELQRALSKANSEvaqwrtkyetdaIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLE-K 1417
Cdd:PRK03918 525 -------EEYEKLKEKLIKLKGEIKSLKKE------------LEKLEELKKKLAELEKKLDELEEELAELLKELEELGfE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1418 TKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKvLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEalDQLE 1497
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYE 662
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 6981234 1498 TVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQ 1542
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1287-1804 |
3.87e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1287 ELSRQLEEKES--IVSQLSRSKQAFTQQIEELKRQLEEENKAKnalahalqSSRHDCDLLREQYEEEQEGKAELQRALSK 1364
Cdd:PRK02224 191 QLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEERREELETLEAEIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1365 ANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANS 1438
Cdd:PRK02224 263 LRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1439 LAAALDKKQRNFDKVLAEWKTKCEESQAELEAA---LKESRS----LSTELFKLKNAYEEALDQLETVKRENKNLEQEIA 1511
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAreaVEDRREeieeLEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1512 DLTEQIAENGKSIHELEKSRKQME--------------LEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDR-- 1575
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERae 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1576 KIAEKDEEIEQLKRNYQRTVETMQGAlDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQ 1655
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1656 LHLDDALRGQEDLKEQLAIVERranlLQAEVEELRATLEQ-----TERARKLAEQelldsNERV-QLLHTQNTSLIHTKK 1729
Cdd:PRK02224 582 AELKERIESLERIRTLLAAIAD----AEDEIERLREKREAlaelnDERRERLAEK-----RERKrELEAEFDEARIEEAR 652
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1730 KLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKeqdtsahLERMKKNLEQTVKDLQHRLDEAEQL 1804
Cdd:PRK02224 653 EDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE-------LRERREALENRVEALEALYDEAEEL 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
866-1505 |
5.42e-14 |
|
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: 77.75 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 866 KSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLE 945
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 946 DEC-------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKV 1018
Cdd:TIGR04523 110 SEIkndkeqkNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1019 NSLSKLKSKLEQQVDDLESSLEQEKKLRVDLErnkrKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDE 1098
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQIS----ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1099 QTlslQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSErleeaggvtsTQIELNKKREAEFLKLRRD 1178
Cdd:TIGR04523 266 KK---QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK----------SELKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1179 LEEATLQHEATVATLRKKHADSAAE---LAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLED 1255
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1256 QLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQ 1335
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1336 SSRHDCDLLREQYEEEQEGKAELQRALSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDSEEQVEAV--NAKCA 1413
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI---------------EKLESEKKEKESKISDLEDELNKDdfELKKE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1414 SLEKTKQRLQGEVEDLMVDV-------ERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLK 1486
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQkslkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
650
....*....|....*....
gi 6981234 1487 NAYEEALDQLETVKRENKN 1505
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKE 656
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
867-1535 |
2.02e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 867 SEAKRKELEEKLVTLvqekndLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLED 946
Cdd:TIGR00618 121 LAAKKSETEEVIHDL------LKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 947 ECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLTEELAGLDETIAKLTREKKALQEAH--QQTLDDLQAEEDKVNS 1020
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1021 ----LSKLKSKLEQQVDDLESSLEQEKKLRVD---------LERNKRKLEGDLK-----LAQESILD----LENDKQQLD 1078
Cdd:TIGR00618 275 qeavLEETQERINRARKAAPLAAHIKAVTQIEqqaqrihteLQSKMRSRAKLLMkraahVKQQSSIEeqrrLLQTLHSQE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1079 ERL-----KKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEE 1153
Cdd:TIGR00618 355 IHIrdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1154 AGGVTSTQIEL--------NKKREAEFLKLRRDLEEATlQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEF 1225
Cdd:TIGR00618 435 LQQRYAELCAAaitctaqcEKLEKIHLQESAQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1226 KLEIDDL-------------SSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQL 1292
Cdd:TIGR00618 514 NPARQDIdnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1293 EEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLL--REQYE-----EEQEGKAELQRALSKA 1365
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtaLHALQltltqERVREHALSIRVLPKE 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1366 NSEVAQWRTKYETDAIQRT----EELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLM-----VDVERA 1436
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLtywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNqslkeLMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1437 NSLAAALDKKQRNFDKVLAEWKTKCEESQ--AELEAALKESRSLSTELFKLKNAYEEALDQLETVKR-ENKNLEQEIADL 1513
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHlaAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQF 833
|
730 740
....*....|....*....|..
gi 6981234 1514 TEQIAENGKSIHELEKSRKQME 1535
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYE 855
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1207-1886 |
2.22e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1207 QIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKskanlekicrtLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAG 1286
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN-----------IEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1287 ELSRQLEEKESIVSQlsrskqaftqqIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQ--RALSK 1364
Cdd:PRK03918 225 KLEKEVKELEELKEE-----------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1365 ANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVdveranslaaaLD 1444
Cdd:PRK03918 294 EYIKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-----------LE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1445 KKQRNFDKVLAEwktkceesQAELEAALKESRSLSTElfKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSI 1524
Cdd:PRK03918 359 ERHELYEEAKAK--------KEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1525 HELEKSRKQMELEKADIQMALEeaeaaleheeakiLRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRtvetmqgaLDA 1604
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHR-------------KELLEEYTAELKRIEKELKEIEEKERKLRKELRE--------LEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1605 EVRSRNEAIRLKKKMEgDLNEIEIQLSHAN----RQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRAN 1680
Cdd:PRK03918 488 VLKKESELIKLKELAE-QLKELEEKLKKYNleelEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1681 llqaEVEELRATLEQteRARKLAEQELLDSNERVQLLHTQNTSLIhtkkkletdltqlqsEVEDASRDARNAEEKAKKAI 1760
Cdd:PRK03918 567 ----ELEEELAELLK--ELEELGFESVEELEERLKELEPFYNEYL---------------ELKDAEKELEREEKELKKLE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1761 TDAAMMAEELkkeQDTSAHLERMKKNLEQtvkdLQHRLDEAEQlalkggkkqiQKLETRIRELEFELEGEQKRNTESVKG 1840
Cdd:PRK03918 626 EELDKAFEEL---AETEKRLEELRKELEE----LEKKYSEEEY----------EELREEYLELSRELAGLRAELEELEKR 688
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1841 LRKYERRVKELTYQSEEDRKNVLRLQDL------VDKLQVKVKSYKRQAEEA 1886
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELEKLekalerVEELREKVKKYKALLKER 740
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1404-1888 |
2.99e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.60 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1404 QVEAVNAKCASLEKTKQRLQgEVEDLMVDVERANslAAALDKKQRNFDKVLAEWK--TKCEESQAELEAALKEsrsLSTE 1481
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQ-KAESELKELEKKH--QQLCEEKNALQEQLQAETElcAEAEEMRARLAARKQE---LEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1482 LFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENgksihelEKSRKQMELEKADIQMALEEAEAALEHEEAKILR 1561
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE-------EAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1562 IQLE---LTQVKSEIDRKIAEKDEE---IEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANR 1635
Cdd:pfam01576 150 LSKErklLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1636 QAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQEL-------- 1707
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELealktele 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1708 --LDSNERVQLLHTQ-NTSLIHTKKKLETD------------------LTQLQSEVEDASRdARNAEEKAKKAI-TDAAM 1765
Cdd:pfam01576 310 dtLDTTAAQQELRSKrEQEVTELKKALEEEtrsheaqlqemrqkhtqaLEELTEQLEQAKR-NKANLEKAKQALeSENAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1766 MAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKqIQKLETRIRELEFELEGEQKRNTESVKGLRKYE 1845
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK-LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 6981234 1846 RRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADE 1888
Cdd:pfam01576 468 SQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1386 |
7.54e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKL--VTLVQEKNDLQLQVQAESENLLDAEERcdqLIKAKFQLEA 918
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELRE---IEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 919 KIKEVTERAEDEEEINA---ELTAKKRKLEDECSELKKDIDDLELTLAKVEkekhatenKVKNLTEELAGLdeTIAKLTR 995
Cdd:PRK03918 322 EINGIEERIKELEEKEErleELKKKLKELEKRLEELEERHELYEEAKAKKE--------ELERLKKRLTGL--TPEKLEK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 996 EKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKleGDLKLAQESILDLENDKQ 1075
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1076 QLDERLKKKDFEYSQLQSKVEDEQTLS--LQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEE 1153
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1154 aggvtstQIELNKKREAEFLKLRRDLEE--ATLQHEatvatLRKKHADSAAELAEQIDNLQRVKQKL------EKEKSEF 1225
Cdd:PRK03918 550 -------KLEELKKKLAELEKKLDELEEelAELLKE-----LEELGFESVEELEERLKELEPFYNEYlelkdaEKELERE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1226 KLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGK-NEETQRSLSELTTqksrlqteagELSRQLEEKESIVSQLSR 1304
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYL----------ELSRELAGLRAELEELEK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1305 SKQAFTQQIEELKRQLEEENKAKNALaHALQSSRHDCDLLREQY-----EEEQEGKAELQRALSKANSEVAQwrTKYETD 1379
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGV 764
|
....*..
gi 6981234 1380 AIQRTEE 1386
Cdd:PRK03918 765 RVKAEEN 771
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1254-1912 |
8.57e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1254 EDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHA 1333
Cdd:PTZ00121 1045 KDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1334 LQSSR-------HDCDLLREQYEEEQEGKAELQRALSKAN--------SEVAQWRTKYETDAIQRTEEL---EEAKKKLA 1395
Cdd:PTZ00121 1125 EDARKaeearkaEDARKAEEARKAEDAKRVEIARKAEDARkaeearkaEDAKKAEAARKAEEVRKAEELrkaEDARKAEA 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1396 QRLQDSEEQVEAVN-----AKCASLEKTKQRLQGEVEDLMVDVERANS-----LAAALDKKQRNFDKVLAEWKTKCEESQ 1465
Cdd:PTZ00121 1205 ARKAEEERKAEEARkaedaKKAEAVKKAEEAKKDAEEAKKAEEERNNEeirkfEEARMAHFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1466 AELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLE-QEIADLTEQIAENGKSIHELEKSR---KQMELEKADI 1541
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEaKKKADAAKKKAEEAKKAAEAAKAEaeaAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1542 QMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIR------- 1614
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaeeak 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1615 ----LKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAE----V 1686
Cdd:PTZ00121 1445 kadeAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEeakkA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1687 EELRATLE--QTERARKLAEQELLDSNERV-QLLHTQNTSLIHTKKKLETDLTQLQSEVEDASR-DARNAEEKAKKAITD 1762
Cdd:PTZ00121 1525 DEAKKAEEakKADEAKKAEEKKKADELKKAeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1763 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLR 1842
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1843 KYERRVKELTYQSEEDRKNvlrlqdlVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERAD 1912
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKK-------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1168-1920 |
8.93e-13 |
|
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: 74.10 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1168 REAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQ--IDNLQRVKQKLEKEKSEFK------LEIDDLSSSVESV 1239
Cdd:pfam12128 191 KEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIqaIAGIMKIRPEFTKLQQEFNtlesaeLRLSHLHFGYKSD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1240 SKSKANLEKICRTLEDQL-SEARGKNEETQRSLSELTtqkSRLQTEAGELSRQLEEKESIVSQLSRSKQAftqQIEELKR 1318
Cdd:pfam12128 271 ETLIASRQEERQETSAELnQLLRTLDDQWKEKRDELN---GELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1319 QLEEENKAKNALAhaLQSSRHDCdLLREQYEEEQEGKAELQRALSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRL 1398
Cdd:pfam12128 345 DQEQLPSWQSELE--NLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDRQLAVAEDDLQA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1399 QDSEEQvEAVNAKCASLEKTKQRLQGEVEDLMVdveRANSLAAALDKK--QRNFDkvlaewkTKCEESQAELEAALKESR 1476
Cdd:pfam12128 420 LESELR-EQLEAGKLEFNEEEYRLKSRLGELKL---RLNQATATPELLlqLENFD-------ERIERAREEQEAANAEVE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1477 SLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELekSRKQMELEKADIqmaleeaeaaleheE 1556
Cdd:pfam12128 489 RLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF--LRKEAPDWEQSI--------------G 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1557 AKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIrlkkkmegdlnEIEIQLSHANRQ 1636
Cdd:pfam12128 553 KVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKA-----------EEALQSAREKQA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1637 AAEtiKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLaivERRANLLQAEVeelRATLEQTERARKLAEQELLD-SNERVQ 1715
Cdd:pfam12128 622 AAE--EQLVQANGELEKASREETFARTALKNARLDL---RRLFDEKQSEK---DKKNKALAERKDSANERLNSlEAQLKQ 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1716 LLHTQNTSLIHTKKKLETDLTQLQS---EVEDASRD-------ARNAEEKAKKAITDA--AMMAEELKK---EQDTSAHL 1780
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAywqVVEGALDAqlallkaAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKL 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1781 ERMKKNLEQTVKDLQHRLDEA--------EQLALKGGKKQIQKLETRiRELEfELEGEQKRNTESVKglrkyeRRVKELT 1852
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVlryfdwyqETWLQRRPRLATQLSNIE-RAIS-ELQQQLARLIADTK------LRRAKLE 845
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1853 YQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQheLEEAEERADIAESQVNK 1920
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ--LEDLKLKRDYLSESVKK 911
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1415-1924 |
9.40e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.00 E-value: 9.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1415 LEKTKQRLQGEVEDLMVDVERANSLAaalDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALD 1494
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1495 QLETVKrenknleqeiaDLTEQIAENGKSihELEKSRKQMELEKADIQMALEEAEAALEHEEAKILR----IQLELTQVK 1570
Cdd:pfam15921 153 ELEAAK-----------CLKEDMLEDSNT--QIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEhdsmSTMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1571 SEIDRKIAEKDEEIEQLKRNYqRTVETMQGALDAEVRSRNEAI--RLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQ 1648
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRI-FPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1649 GQLKDTQlhlddalrgqEDLKEQLAIVERRANLLQAEVEELRATLEQterARKLAEQELLDSNERVQLLHTQntslihtk 1728
Cdd:pfam15921 299 SQLEIIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELRE---AKRMYEDKIEELEKQLVLANSE-------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1729 kkletdLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkg 1808
Cdd:pfam15921 358 ------LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM----- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1809 gkkQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKnvlRLQDLVDKLqvkvkSYKRQAEEADE 1888
Cdd:pfam15921 427 ---EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEEL-----TAKKMTLESSE 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 6981234 1889 QANVHLTKfrkaqhELEEAEERADIAESQVNKLRAK 1924
Cdd:pfam15921 496 RTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
842-1601 |
1.04e-12 |
|
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: 73.85 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKEleEKLVTLVQEKNDLQLQVQAESEN--LLDAEERCDQLIKAKFQLEAK 919
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKE--EEKEKKLQEEELKLLAKEEEELKseLLKLERRKVDDEEKLKESEKE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 920 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE----ELAGLDETIAKLTR 995
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlssAAKLKEEELELKSE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 996 EKKALQEAHQ--QTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDL-KLAQESILDLEN 1072
Cdd:pfam02463 403 EEKEAQLLLElaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKsEDLLKETQLVKL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1073 DKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLE 1152
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1153 EAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKS-----EFKL 1227
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTEltklkESAK 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1228 EIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQ 1307
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1308 ---AFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQY--EEEQEGKAELQRALSKANSEVAQWRTKYETDAIQ 1382
Cdd:pfam02463 723 ladRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKseLSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1383 RTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERAN----SLAAALDKKQRNFDKVLAEWK 1458
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErleeEITKEELLQELLLKEEELEEQ 882
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1459 TKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEK 1538
Cdd:pfam02463 883 KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1539 ADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEI-EQLKRNYQRTVETMQGA 1601
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIrAIIEETCQRLKEFLELF 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
845-1404 |
1.60e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 73.23 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 845 ETEKEMATMKEEFQKTKDELaksEAKRKELEEKLVTLVQEKNDLQLQVQAESE-NLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQL---EALKSESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 924 TERAEDE---------------EEINAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEELAGL 986
Cdd:pfam15921 305 QEQARNQnsmymrqlsdlestvSQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 987 DETIAKltREKKALQEAHQQ------------TLDDLQAEEDKVNS--------LSKLKS----KLEQQVDDLE---SSL 1039
Cdd:pfam15921 383 LADLHK--REKELSLEKEQNkrlwdrdtgnsiTIDHLRRELDDRNMevqrlealLKAMKSecqgQMERQMAAIQgknESL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1040 EQEKKLRVDLERNKRKLEG----------DLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKI 1109
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKvveeltakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1110 KELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNK-----KREAEFLKLRRDLEEATL 1184
Cdd:pfam15921 541 DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeindrRLELQEFKILKDKKDAKI 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1185 QH-EATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKAN-------LEKICRTLEDQ 1256
Cdd:pfam15921 621 RElEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseeMETTTNKLKMQ 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1257 LSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEK----ESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAH 1332
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqiDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELST 780
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1333 ALQSSRH---DCDLLREQYEEEQEGKAELQRALSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQDSEEQ 1404
Cdd:pfam15921 781 VATEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKELQ 849
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1923 |
2.60e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1382 QRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKqrlqGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKC 1461
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1462 EESQaELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE---NGKSIHELEKSRKQMELEK 1538
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1539 ADIQmaleeaeaALEHEEAKILRIQLELTQVKSEIdrkiaeKDEEIEQLKRNYQrtvetmqgaldaevrsrnEAIRLKKK 1618
Cdd:PRK03918 355 EELE--------ERHELYEEAKAKKEELERLKKRL------TGLTPEKLEKELE------------------ELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1619 MEGDLNEIEIQLSHANRQAAE---TIKHLRSVQGQLKDTQLHLDDALRGQ--EDLKEQLAIVERRANLLQAEVEELRATL 1693
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKElkkAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1694 EQTERarklaeqeLLDSNERVQLLHTQNTSLIHTKKKLETDLTQlqsEVEDASRDARNAEEKAKKAITDAAMMAEELKKE 1773
Cdd:PRK03918 483 RELEK--------VLKKESELIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1774 QDtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEfELEGEQKRNTESVKGLRKYERRVKELTY 1853
Cdd:PRK03918 552 EE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1854 QSEEDRKNVLRLQDLVDKLQVKVKSYKRQ--AEEADEQANVHLTKFRK---AQHELEEAEERADIAESQVNKLRA 1923
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLELSRElagLRAELEELEKRREEIKKTLEKLKE 701
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1571-1936 |
4.29e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1571 SEIDRKIAEKDEEIEQLKRNYQR---TVETMQGALDAEVRSRNEAIR---LKKKME--------GDLNEIEIQLSHANRQ 1636
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqaLLKEKReyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1637 AAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQL-AIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQ 1715
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1716 LLHTQNTSLIHTKKKLETDLTQLQSEvedasRDARNAEEKAKKAITDAamMAEELKKEQDTSAHLERMKKNLEQTVKDLQ 1795
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKR-----RDKLTEEYAELKEELED--LRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1796 HRLDEAeQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESvkglrkyERRVKELTYQSEEDRKNVLRLQDLVDKLQVK 1875
Cdd:TIGR02169 399 REINEL-KRELDRLQEELQRLSEELADLNAAIAGIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1876 VksYKRQAEEADEQanvhlTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVH 1936
Cdd:TIGR02169 471 L--YDLKEEYDRVE-----KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
6.82e-12 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 61.68 E-value: 6.82e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 6981234 33 DAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDV 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1201-1743 |
1.39e-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: 69.77 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1201 AAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSR 1280
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1281 LQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQR 1360
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1361 ALSKAnsevaqwrtkyeTDAIQRTEELEeakKKLAQRLQDSEEqVEAVNAKCAS---LEKTKQRLQGEVEDLMVDVERAN 1437
Cdd:pfam05557 161 QQSSL------------AEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHLNENIENKL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1438 SLAAALDKKQRNFDKVlaewktkcEESQAELEAALKESRSLSTELFKLKNAYEEALDQL---ETVKRENKNLEQEIADLT 1514
Cdd:pfam05557 225 LLKEEVEDLKRKLERE--------EKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1515 EQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRkiaekdeeIEQLKRNYQRT 1594
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDG--------YRAILESYDKE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1595 VeTMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKdtqlhlddALRGQEDLKEQLAI 1674
Cdd:pfam05557 369 L-TMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--------ALRQQESLADPSYS 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 1675 VERRANLLQaEVEELRATLEQTERARKLAEQEL--------LDSNERVQLLHTQNTSLIHTKKKLEtDLTQLQSEVE 1743
Cdd:pfam05557 440 KEEVDSLRR-KLETLELERQRLREQKNELEMELerrclqgdYDPKKTKVLHLSMNPAAEAYQQRKN-QLEKLQAEIE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1258-1920 |
1.83e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1258 SEARGKNEETQRSLSELTTQKSRLQ--TEAGELSRQLEE--KESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNAL--- 1330
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEeaKKKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARkae 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1331 -AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE----TDAIQRTEEL----EEAKKklAQRLQDS 1401
Cdd:PTZ00121 1174 dAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEdakkAEAVKKAEEAkkdaEEAKK--AEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1402 EEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQaELEAALKESRSLSTE 1481
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKK 1330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1482 LFKLKNAYEEALDQLETVKRENKNLEQEiadlteqiAENGKSIHELEKSRKQMELEKADiqmalEEAEAALEHEEAKILR 1561
Cdd:PTZ00121 1331 ADAAKKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKAEAAEKKKEEAKKKAD-----AAKKKAEEKKKADEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1562 IQLELTQVKSEIDRKIAEKDEEIEQLKRNYQrtvetmqgaldaEVRSRNEAirlKKKMEGDLNEIEIQLSHANRQAAETI 1641
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAE------------EKKKADEA---KKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1642 KHlrsvqgqlKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQElldsnervqllhtqn 1721
Cdd:PTZ00121 1463 KK--------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE--------------- 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1722 tslihTKKKLEtdltqlqsevedasrDARNAEEKAKkaiTDAAMMAEELKKEQDTSAhLERMKKNLEQTVKDLQHRLDEA 1801
Cdd:PTZ00121 1520 -----EAKKAD---------------EAKKAEEAKK---ADEAKKAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1802 EQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKglRKYERRVK-ELTYQSEEDRKNVLRLQDLVDKLQVKVKSYK 1880
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 6981234 1881 RQAEE----ADEQANVHLTKFRKAQhELEEAEERADIAESQVNK 1920
Cdd:PTZ00121 1654 KAEEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKK 1696
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1246-1519 |
1.88e-11 |
|
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: 69.11 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1246 LEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENK 1325
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1326 AKNALAHALQSSRhdcdllreQYEEEQEGKAELQRALSKANSevaqwrtKYETDAI-QRTEELEEAKKKLAQRLQDSEEQ 1404
Cdd:pfam09726 480 ARASAEKQLAEEK--------KRKKEEEATAARAVALAAASR-------GECTESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1405 VEAVNAKCASLEKTKQRlQGEVEDLMvdveraNSLAAALDKKQrnfdkvlaewktkceesqaELEAALKESRSLSTELFk 1484
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ-------------------HLENSLSAETRIKLDLF- 597
|
250 260 270
....*....|....*....|....*....|....*
gi 6981234 1485 lkNAYEEALDQLETVKRENKNLEQEIADLTEQIAE 1519
Cdd:pfam09726 598 --SALGDAKRQLEIAQGQIYQKDQEIKDLKQKIAE 630
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1255-1709 |
2.30e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1255 DQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFT--QQIEELKRQLEEENKAKNALAH 1332
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1333 ALQSSRHdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKC 1412
Cdd:COG4717 154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1413 ASLEKTKQRLQgEVEDLMVDVERANSLAAALDkkqrnfdkVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEA 1492
Cdd:COG4717 230 EQLENELEAAA-LEERLKEARLLLLIAAALLA--------LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1493 LDQLETVKRENKNLEQEIADLTEQIAENGksiheLEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSE 1572
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALG-----LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1573 IDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKME-GDLNEIEIQLSHANRQAAETIKHLRSVQGQL 1651
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaLDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1652 KDTQLHLDDALRGQE--DLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLD 1709
Cdd:COG4717 456 AELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1415 |
5.11e-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: 68.28 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQaESENLLDAEERCDQLIKAKF-QLEAK 919
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ-DTQELLQEETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 920 IKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKA 999
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1000 LQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQ------------------------------------------------- 1030
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlaeekaisaryaeerdraeaeareketralslaraleealeakeeler 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1031 -------QVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQL-DERLK--------KKDFEySQLQSK 1094
Cdd:pfam01576 658 tnkqlraEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATeDAKLRlevnmqalKAQFE-RDLQAR 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1095 VEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAggvtstqIELNKKREAEFLK 1174
Cdd:pfam01576 737 DEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEA-------VKQLKKLQAQMKD 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1175 LRRDLEEATLQHEATVATLR---KKHADSAAE---LAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEK 1248
Cdd:pfam01576 810 LQRELEEARASRDEILAQSKeseKKLKNLEAEllqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEA 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1249 ICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAG---------------------ELSRQLEEKESIV-SQLSRSK 1306
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAaerstsqksesarqqlerqnkELKAKLQEMEGTVkSKFKSSI 969
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1307 QAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYEtDAIQRTEE 1386
Cdd:pfam01576 970 AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASR 1048
|
650 660
....*....|....*....|....*....
gi 6981234 1387 LEEAKKKLAQRLQDSEEQVEAVNAKCASL 1415
Cdd:pfam01576 1049 ANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1566-1932 |
6.93e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1566 LTQVKSEIDRK---------------IAEKDEEIEQLKRNYQRTVETMQGALD--AEVRSRNEAIrlkKKMEGDLNEIEI 1628
Cdd:PRK02224 189 LDQLKAQIEEKeekdlherlngleseLAELDEEIERYEEQREQARETRDEADEvlEEHEERREEL---ETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1629 QLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQE-DLKEQLAIVERRANLlQAEVEELRATLEQTERARKLAEQEL 1707
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARREEL-EDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1708 LDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDAS----------RDARNAEEKAKKAITDAAMMAEELKKEQDts 1777
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRReeieeleeeiEELRERFGDAPVDLGNAEDFLEELREERD-- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1778 aHLERMKKNLEQTVKDLQHRLDEAEQLaLKGGK---------------------KQIQKLETRIRELEFELEGEQKRnTE 1836
Cdd:PRK02224 423 -ELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEER-LE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1837 SVKGLRKYERRVKELtyqsEEDRKNVlrlQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAES 1916
Cdd:PRK02224 500 RAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
410
....*....|....*.
gi 6981234 1917 QVNKLRAKTRDFTSSR 1932
Cdd:PRK02224 573 EVAELNSKLAELKERI 588
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1171-1924 |
1.02e-10 |
|
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: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1171 EFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEK-SEFKLEIDDLSSSVESVSKSKANLEKI 1249
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlQELKLKEQAKKALEYYQLKEKLELEEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1250 CRTLEDQLSEARGKNEETQRslsELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNA 1329
Cdd:pfam02463 225 YLLYLDYLKLNEERIDLLQE---LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1330 LAHALQSSRHDcdllREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDS--EEQVEA 1407
Cdd:pfam02463 302 LLKLERRKVDD----EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEqlEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1408 VNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKN 1487
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1488 AYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELT 1567
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1568 QVKSEIDRKIAEKDE------EIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETI 1641
Cdd:pfam02463 538 VENYKVAISTAVIVEvsatadEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1642 KHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQN 1721
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1722 TSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEA 1801
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELA 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1802 EQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNvLRLQDLVDKLQVKVKSYKR 1881
Cdd:pfam02463 778 EEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE-LALELKEEQKLEKLAEEEL 856
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 6981234 1882 QAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAK 1924
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK 899
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
836-1393 |
1.38e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEErcdqlIKAKFQ 915
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-----AKKKAE 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 916 LEAKIKEVTERAEDEEEinAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEELAGLDETIAKLTR 995
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 996 EKKALQEAHQQTLDDLQAEEDKvnslsklKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEgDLKLAQEsiLDLENDKQ 1075
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--LKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1076 QLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAg 1155
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA- 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1156 gvtstqielNKKREAEflKLRRDLEEATLQheatvatlrkkhadsAAELAEQIDNLQRVKQKLEKEKSEfkleiddlsss 1235
Cdd:PTZ00121 1644 ---------EEKKKAE--ELKKAEEENKIK---------------AAEEAKKAEEDKKKAEEAKKAEED----------- 1686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1236 vesvskskanlekicrtlEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEE 1315
Cdd:PTZ00121 1687 ------------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1316 LKRQLEEENK----AKNALAHALQSSRHDCDLLREQYEEEQEG-KAELQRAL--SKANSEVAQWRTKYETDAIQRTEELE 1388
Cdd:PTZ00121 1749 AKKDEEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdIFDNFANIIEGGKEGNLVINDSKEME 1828
|
....*
gi 6981234 1389 EAKKK 1393
Cdd:PTZ00121 1829 DSAIK 1833
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1067-1627 |
1.51e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1067 ILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQtlslQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEE 1146
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1147 LSErleeaggvTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKhadsAAELAEQIDNLQRVKQK------LEK 1220
Cdd:PRK03918 233 LEE--------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKEKaeeyikLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1221 EKSEFKLEIDDLSSSVESVSKSKANLEKICRTLED---QLSEARGKNEETQRSLSELTT-------------QKSRLQTE 1284
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErhelyeeakakkeELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1285 AGELSrqLEEKESIVSQLSRSKQAFTQQIEEL---KRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEG--KAELQ 1359
Cdd:PRK03918 381 LTGLT--PEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1360 RALSKANSEVAQWRTKyETDAIQRTEELEEA---------KKKLAQRLQDSEEQVEAVN-----AKCASLEKTKQR---L 1422
Cdd:PRK03918 459 AELKRIEKELKEIEEK-ERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNleeleKKAEEYEKLKEKlikL 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1423 QGEVEDLMVDVERANSL---AAALDKKQRNFDKVLAEWKTKCEE----SQAELEAALKESRSLSTELFKLKNAYEEaldq 1495
Cdd:PRK03918 538 KGEIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEYLELKDAEKE---- 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1496 LETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLE-LTQVKSEID 1574
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEeLEKRREEIK 693
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1575 RKIAEKDEEIEQLKRnYQRTVETMQGALDAEVRSRNEAIRLKKKM-EGDLNEIE 1627
Cdd:PRK03918 694 KTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLkERALSKVG 746
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
840-1107 |
2.43e-10 |
|
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: 65.61 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 840 LLKSAETEKEMATMK-----EEFQKTKDELAKSEAKRKE-----LEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQL 909
Cdd:pfam10174 264 LLHTEDREEEIKQMEvykshSKFMKNKIDQLKQELSKKEsellaLQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 910 ikakfqlEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDET 989
Cdd:pfam10174 344 -------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 990 IAKLTREKKALQEAHQQ------TLDDLQAEEDKV-NSLSKLKSKLEQQVDDLESSLEQEKKlrvDLERNKRKLEGDLKL 1062
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNtdtaltTLEEALSEKERIiERLKEQREREDRERLEELESLKKENK---DLKEKVSALQPELTE 493
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6981234 1063 AQESILDLENDKQQLDERLKKKDFEYSQL----QSKVEDEQTLSLQLQK 1107
Cdd:pfam10174 494 KESSLIDLKEHASSLASSGLKKDSKLKSLeiavEQKKEECSKLENQLKK 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1344-1923 |
3.03e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1344 LREQYEEEQEgkAELQRALSKANSEVAqwrtkyETDAIqrTEELEEAKKKLAQRLQDSEEqveavnakcaSLEKTKQRLQ 1423
Cdd:PRK02224 192 LKAQIEEKEE--KDLHERLNGLESELA------ELDEE--IERYEEQREQARETRDEADE----------VLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1424 gEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESrslstelfKLKNAYEEAL-DQLETVKRE 1502
Cdd:PRK02224 252 -ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--------GLDDADAEAVeARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1503 NKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQmaleeaeaaleheeAKILRIQLELTQVKSEIDR---KIAE 1579
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR--------------EEAAELESELEEAREAVEDrreEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1580 KDEEIEQLKRNYQRTVETMQGALD--AEVRSRNEAIRlkkkmeGDLNEIEIQLshanRQAAETIKHLRSVQ--------G 1649
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDflEELREERDELR------EREAELEATL----RTARERVEEAEALLeagkcpecG 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1650 QLKDTQLHLDDAlrgqEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQ--ELLDSNERV-QLLHTQNTSLIH 1726
Cdd:PRK02224 459 QPVEGSPHVETI----EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLeELIAERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1727 TKKKLETdltqLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEqTVKDLQHRLDEAEQlal 1806
Cdd:PRK02224 535 KRERAEE----LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAED--- 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1807 kggkkqiqkletRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQ-DLVDKLQVKVKSYKRQAEE 1885
Cdd:PRK02224 607 ------------EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDkERAEEYLEQVEEKLDELRE 674
|
570 580 590
....*....|....*....|....*....|....*...
gi 6981234 1886 ADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRA 1923
Cdd:PRK02224 675 ERDDLQAEIGAVENELEELEELRERREALENRVEALEA 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
847-1393 |
3.15e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER 926
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 927 AEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK---EKHATENKVKNLTEELAGLDETIAKLTREKKALQEA 1003
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1004 HQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDlklaqesILDLENDKQQ-----LD 1078
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-------ISDLNNQKEQdwnkeLK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1079 ERLKKKDFEYSQLQSKV-EDEQTLS------LQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERL 1151
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQIsQNNKIISqlneqiSQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1152 EEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVATlRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDD 1231
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1232 LSSSvesvskskanLEKICRTLEDQLSEARGKNEEtqrsLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQ 1311
Cdd:TIGR04523 473 LSRS----------INKIKQNLEQKQKELKSKEKE----LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1312 QIEELKRQLEE--ENKAKNALAHALQSSRHDCDLLREQYEE---EQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEE 1386
Cdd:TIGR04523 539 KISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSlkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
....*..
gi 6981234 1387 LEEAKKK 1393
Cdd:TIGR04523 619 LEKAKKE 625
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1433-1925 |
3.65e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1433 VERANSLAAALDKKQRNFDKvLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIAD 1512
Cdd:PRK02224 205 HERLNGLESELAELDEEIER-YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1513 LTEQIAENGKSIHELeksRKQMELEKADIQmaleeaeaaleheeakilriqlELTQVKSEIDRKIAEKDEEIEQLKRNYQ 1592
Cdd:PRK02224 284 LRERLEELEEERDDL---LAEAGLDDADAE----------------------AVEARREELEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1593 RTVETMQGALD--AEVRSRNEAIRLK-KKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLK 1669
Cdd:PRK02224 339 AHNEEAESLREdaDDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1670 EQLAIVERRANLLQAEVEELRATLEQTER---ARKLAE--QELLDSnERVQLLHTQNTSlihtKKKLETDLTQLQSEVED 1744
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEAlleAGKCPEcgQPVEGS-PHVETIEEDRER----VEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1745 asRDARNAEekakkaitdaammAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLETRIRELE 1824
Cdd:PRK02224 494 --VEERLER-------------AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE--------RAEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1825 FELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDkLQVKVKSYKRQAE----------EADEQANVHL 1894
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT-LLAAIADAEDEIErlrekrealaELNDERRERL 629
|
490 500 510
....*....|....*....|....*....|.
gi 6981234 1895 TKFRKAQHELEEAEERADIAESQVNKLRAKT 1925
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
941-1526 |
5.62e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 941 KRKLEDECSELKKDIDDLELTLAKVEKEKHATE--NKVKNLTEELAGLDETIAKLTREKKALQ-EAHQQTLDDLQAEEDK 1017
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1018 vnsLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDlklaqeSILDLENDKQQLDERLKKKDFEYSQLQSKVed 1097
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALL-- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1098 eQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAggvtSTQIELNKKR----EAEFL 1173
Cdd:COG4913 369 -AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL----EAEIASLERRksniPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1174 KLRRDLEEATLQHEATVA------TLRKKHAD--SAAELA----------EQiDNLQRVKQKLEKEKSEFKLEIDDLSSS 1235
Cdd:COG4913 444 ALRDALAEALGLDEAELPfvgeliEVRPEEERwrGAIERVlggfaltllvPP-EHYAAALRWVNRLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1236 VESVSKSKANLEKICRTLEDQLSEARG--KNEETQR-------SLSELTTQKSRLqTEAGELS----------------- 1289
Cdd:COG4913 523 LPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRfdyvcvdSPEELRRHPRAI-TRAGQVKgngtrhekddrrrirsr 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1290 --------RQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLlrEQYEEEQEGKAELQRA 1361
Cdd:COG4913 602 yvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1362 LSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLA- 1440
Cdd:COG4913 680 LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAr 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1441 -----------------AALDKKQRNFDKVLAEWKTKCEESQAELEAALKE--------SRSLSTELFKLkNAYEEALDQ 1495
Cdd:COG4913 745 lelralleerfaaalgdAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESL-PEYLALLDR 823
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 6981234 1496 LETV----------KRENKNLEQEIADLTEQIAENGKSIHE 1526
Cdd:COG4913 824 LEEDglpeyeerfkELLNENSIEFVADLLSKLRRAIREIKE 864
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1304 |
9.75e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDE-----------LAKS----------EAKRKELEEKLVTLVQEKNDLQLQVQA-------E 895
Cdd:PRK02224 268 AETEREREELAEEVRDLRERleeleeerddlLAEAglddadaeavEARREELEDRDEELRDRLEECRVAAQAhneeaesL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 896 SENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 975
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 976 VKNLTEELAGLDETIakltREKKALQEA--------------HQQTLDDlqaEEDKVNSLSKLKSKLEQQVDDLESSLEQ 1041
Cdd:PRK02224 428 EAELEATLRTARERV----EEAEALLEAgkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLER 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1042 EKKLrVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEE 1121
Cdd:PRK02224 501 AEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1122 EIEAERATRAKTEKQRSDYARELEELSERLeeaggvtstqiELNKKREaeflklrrDLEEATLQHEATVATLRKKHADSA 1201
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIADAEDEIE-----------RLREKRE--------ALAELNDERRERLAEKRERKRELE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1202 AEL-AEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDqLSEARGKNEETQRSLSELTTQKSR 1280
Cdd:PRK02224 641 AEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE-LRERREALENRVEALEALYDEAEE 719
|
490 500
....*....|....*....|....
gi 6981234 1281 LQTEAGELSRQLEEKEsiVSQLSR 1304
Cdd:PRK02224 720 LESMYGDLRAELRQRN--VETLER 741
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
915-1352 |
1.14e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 915 QLEAKIKEVTErAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK--HATENKVKNLTEELAGLDETIAK 992
Cdd:COG4717 72 ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 993 LTREKKALQEAHQQtLDDLQAEedkvnsLSKLKSKLEQQVDDLesSLEQEKKLRvDLERNKRKLEGDLKLAQESILDLEN 1072
Cdd:COG4717 151 LEERLEELRELEEE-LEELEAE------LAELQEELEELLEQL--SLATEEELQ-DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1073 DKQQLDERLK--KKDFEYSQLQSKVEDEQTL--------------------------------------SLQLQKKIKEL 1112
Cdd:COG4717 221 ELEELEEELEqlENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1113 QARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQheatvAT 1192
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-----AL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1193 LRKKHADSAAELAEQIDNLQRvKQKLEKEKSEFKLEIDDLSSSVESVSKSKanlekicrtledQLSEARGKNEETQRSLS 1272
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAL------------DEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1273 ELTTQKSRLQTEAGELSRQLEEKESivsqlSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHdcdlLREQYEEEQ 1352
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKLALELLEE----AREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
902-1113 |
2.14e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 902 AEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE 981
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 982 ELAGLDETIAKLTRekkALQEAHQQTL-------DDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKR 1054
Cdd:COG4942 98 ELEAQKEELAELLR---ALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1055 KLEGDLKLAQESILDLE---NDKQQLDERLKKKDFEY-SQLQSKVEDEQTLSLQLQKKIKELQ 1113
Cdd:COG4942 175 ELEALLAELEEERAALEalkAERQKLLARLEKELAELaAELAELQQEAEELEALIARLEAEAA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
832-1505 |
2.86e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.37 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 832 KLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSE--AKRKELEEKLVTLVQEKNDLQLQVQAESENL------LDAE 903
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 904 ERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 976
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 977 KNLTEELAGLDETI----------AKLTREKKALQEAHQQtlddLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLR 1046
Cdd:TIGR00606 615 ESKEEQLSSYEDKLfdvcgsqdeeSDLERLKEEIEKSSKQ----RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1047 VDLERNKRKLEGDLKLAQESILDLENDkqqlderLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAE 1126
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESE-------LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1127 RATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELnKKREAEFLKLRRDLEEATLqhEATVATLRKKHADSAAEL-- 1204
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELdt 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1205 -AEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKicrtLEDQLSEargKNEETQRSLSELTTQKSRLQT 1283
Cdd:TIGR00606 841 vVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ----FEEQLVE---LSTEVQSLIREIKDAKEQDSP 913
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1284 EAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSrhdCDLLREQYEEEQEGKA----ELQ 1359
Cdd:TIGR00606 914 LETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG---KDDYLKQKETELNTVNaqleECE 990
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1360 RALSKANSEVAQWRTKYETDAIQ------------RTEELEEAKKKLAQRLQDSEEQveavnaKCASLEKTKQRLQGEVE 1427
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQM------QVLQMKQEHQKLEENID 1064
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981234 1428 DLMVDVERANSLAAALDKKQRNFDKVLAEWKTK-CEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKN 1505
Cdd:TIGR00606 1065 LIKRNHVLALGRQKGYEKEIKHFKKELREPQFRdAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1251-1471 |
3.24e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1251 RTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNAL 1330
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1331 AHALQssrhdcDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQ 1399
Cdd:COG4942 103 KEELA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1400 DSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAA 1471
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1215-1442 |
4.15e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1215 KQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEE 1294
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1295 KESIVSQLSRSKQAfTQQIEELKRQLEEENkaKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRT 1374
Cdd:COG4942 102 QKEELAELLRALYR-LGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1375 KYETDAIQRtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAA 1442
Cdd:COG4942 179 LLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
848-1113 |
4.85e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKakfQLEAKIKEVTERA 927
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK---QIENLEEKEMNLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 928 EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQT 1007
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1008 LDDLQAEEDKVN----SLSKLKSKLEQQVDDLESSLE----QEKKLRVDLERNKRKLEGDLKLAQ-----------ESIL 1068
Cdd:pfam05483 628 NKQLNAYEIKVNklelELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKeidkrcqhkiaEMVA 707
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6981234 1069 DLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQ 1113
Cdd:pfam05483 708 LMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIK 752
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
853-1519 |
5.10e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.28 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 853 MKEEFQKTKDELAKSEAKRKELEEKLVTLvqeKNDLQLQVQAESENLLDAEercdqliKAKFQLEAKIKEVTERAED-EE 931
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 932 EINAELTAKKRK---LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTL 1008
Cdd:pfam05483 230 EYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1009 DDLQAEEDKVN----SLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESildLENDKQQLderlkkk 1084
Cdd:pfam05483 310 STQKALEEDLQiatkTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR---LEKNEDQL------- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1085 dfeysqlqskvedeQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGgvtstqiel 1164
Cdd:pfam05483 380 --------------KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG--------- 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1165 nKKREAEFLKLRRDLEEATLQHEATVATLRKKHadsaaelaeQIDNLQRVKQKLEKEK---SEFKLEIDDLSSSVESVSK 1241
Cdd:pfam05483 437 -KEQELIFLLQAREKEIHDLEIQLTAIKTSEEH---------YLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQ 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1242 SKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEK-ESIVSQLSRSkqaftqqiEELKRQL 1320
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKgDEVKCKLDKS--------EENARSI 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1321 EEENKAKNALAHALQSSrhdCDLLREQYEEEQEGKAELQ---RALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQR 1397
Cdd:pfam05483 579 EYEVLKKEKQMKILENK---CNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1398 LQDSEEQVEAVNAkcaslekTKQRLQGEVEDLMVDVERANSLAAALDKK---------------QRNFDKVLAEWKTKCE 1462
Cdd:pfam05483 656 IDNYQKEIEDKKI-------SEEKLLEEVEKAKAIADEAVKLQKEIDKRcqhkiaemvalmekhKHQYDKIIEERDSELG 728
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 1463 ESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE 1519
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
841-1076 |
6.50e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKI 920
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 921 KEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKAL 1000
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1001 QEAHQQTLDDLQAEEDkVNSLSKLKSKLEQQVDDLES-------SLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEND 1073
Cdd:TIGR02169 937 EDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
...
gi 6981234 1074 KQQ 1076
Cdd:TIGR02169 1016 KRE 1018
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
915-1300 |
7.30e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.29 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 915 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLT 994
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 995 REKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDK 1074
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1075 QQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYAreleelserlEEA 1154
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1155 GGVTSTQIELNKKR-EAEFLKLRrdLEEATLQheatvatLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLS 1233
Cdd:pfam07888 265 AQRDRTQAELHQARlQAAQLTLQ--LADASLA-------LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQ 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1234 SSVESVSKSKANL--EKICRTLedQLSEARGKNEETQRSLSELTTQKSRLQTEAGEL---SRQLEEKESIVS 1300
Cdd:pfam07888 336 EERMEREKLEVELgrEKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVA 405
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
847-1640 |
9.55e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 60.83 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLL--DAEERCDQL----------IKAKF 914
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRarDSLIQSLATrleldgfergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 915 QLEAKIKEVTERAEDE--------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGL 986
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEaktaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 987 DETIAKLTREKKALQEAhqqtldDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQes 1066
Cdd:TIGR00606 471 DRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK-- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1067 ildlenDKQQLDERLKKKDFEYS-QLQSKVED---EQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYAR 1142
Cdd:TIGR00606 543 ------DKMDKDEQIRKIKSRHSdELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELES 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1143 ELEELSERLEEAGGVTSTQIElnkkrEAEFLKLRRDLEEATLQhEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEK 1222
Cdd:TIGR00606 617 KEEQLSSYEDKLFDVCGSQDE-----ESDLERLKEEIEKSSKQ-RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1223 SEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQ-------RSLSELTTQKSRLQTEAGELSRQLEEK 1295
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQsiidlkeKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1296 ESIVS------QLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSrhDCDLLREQYEEEQEGKAELQRALSKA---N 1366
Cdd:TIGR00606 771 ETLLGtimpeeESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKielN 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1367 SEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQdseeQVEAVNAKCASLEKTKQRLQGEVEDLMvdvERANSLAAALDKK 1446
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ----RRQQFEEQLVELSTEVQSLIREIKDAK---EQDSPLETFLEKD 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1447 QRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDqletvkRENKNLEQEIADLTEQIAENGKsihE 1526
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD------DYLKQKETELNTVNAQLEECEK---H 992
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1527 LEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQL-ELTQVKSEIDRKIAEkdEEIEQLKRNYQRtvetMQGALDAE 1605
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELkEVEEELKQHLKEMGQ--MQVLQMKQEHQK----LEENIDLI 1066
|
810 820 830
....*....|....*....|....*....|....*
gi 6981234 1606 VRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAET 1640
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1490-1936 |
1.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1490 EEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKAdiqmaleeaeaaleheeakilriQLELTQV 1569
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----------------------LLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1570 KSEIDRKIAEKDEEIEQLKRNYQRTVEtmqgaLDAEVRSRNEAIRlkkKMEGDLNEIEIQLSHANRQaaetikhlrsvqg 1649
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRE-----LEEELEELEAELA---ELQEELEELLEQLSLATEE------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1650 QLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKK 1729
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1730 KLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalK 1807
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRIEEL--Q 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1808 GGKKQIQKLETRIRELEFELEGEQ---KRNTESVKGLR----------KYERRVKELTYQSEEDRKNVLRLQDLVDK--L 1872
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAllaEAGVEDEEELRaaleqaeeyqELKEELEELEEQLEELLGELEELLEALDEeeL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1873 QVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIA------ESQVNKLRAKTRDFTSSRMVVH 1936
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAellqelEELKAELRELAEEWAALKLALE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1200-1414 |
1.39e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1200 SAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKS 1279
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1280 RLQTEAGELSRQLEE------------------KESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDC 1341
Cdd:COG4942 94 ELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1342 DLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCAS 1414
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
967-1425 |
1.54e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 967 KEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQtLDDLQAEEDKVNSLSKLKSKLEQQVDDLESsLEQEKKLR 1046
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPERLEE-LEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1047 VDLERNKRKLEGDLKLAQESILDLENDK-QQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEeleeeiea 1125
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1126 eratRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELnkkreAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELA 1205
Cdd:COG4717 231 ----QLENELEAAALEERLKEARLLLLIAAALLALLGLG-----GSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1206 EQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEetQRSLSELTTQKSRLQTEA 1285
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1286 GelSRQLEEKESIVSQLSRsKQAFTQQIEELKRQLEEENKAKNALAHAlqssrHDCDLLREQYEEEQEGKAELQRALSKA 1365
Cdd:COG4717 380 G--VEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1366 NSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCAS---LEKTKQRLQGE 1425
Cdd:COG4717 452 REELA--ELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAlelLEEAREEYREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1278-1843 |
1.79e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.74 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1278 KSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLRE----------Q 1347
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarsaektkK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1348 YEEEQEGK----AELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQ 1423
Cdd:pfam05483 174 YEYEREETrqvyMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1424 GEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELE-AALKESRSLSTElfklKNAYEEALDQLETVKRE 1502
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdIKMSLQRSMSTQ----KALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1503 NKNLEQEIADLTEQIAENGKSIHELEKS---------RKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEI 1573
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATtcsleellrTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1574 DRKIAEKDEEIEQLKRNYQRTVETMQGaldaevrSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKd 1653
Cdd:pfam05483 410 LKKILAEDEKLLDEKKQFEKIAEELKG-------KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE- 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1654 tqlhlddalrgqedlKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQElldsnERVQLLHTQNTSLIHTKKKLET 1733
Cdd:pfam05483 482 ---------------KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ-----EDIINCKKQEERMLKQIENLEE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1734 DLTQLQSEVEDASRDARNAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQ----LA 1805
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQenkaLK 621
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 6981234 1806 LKGG--KKQIQKLETRIRELEFELEGEQKRNTESVKGLRK 1843
Cdd:pfam05483 622 KKGSaeNKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
990-1910 |
2.98e-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: 59.29 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 990 IAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQ------QVDDLESSLEQEKKLRVDLERNKRKLEGDLKLA 1063
Cdd:TIGR00606 178 IFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKaceirdQITSKEAQLESSREIVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1064 QE---SILDLENDKQQLDERLKKKDFEYSQLQSKVEDE-QTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSD 1139
Cdd:TIGR00606 258 EHnlsKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1140 YARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEA--------TVATLRKKHADSA-------AEL 1204
Cdd:TIGR00606 338 LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqiknFHTLVIERQEDEAktaaqlcADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1205 AEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTE 1284
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1285 AgelsrqleeKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALS- 1363
Cdd:TIGR00606 498 T---------LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGy 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1364 -KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEE---QVEAVNAKCASLEK------TKQRLQGEVEDLMVDV 1433
Cdd:TIGR00606 569 fPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHinnELESKEEQLSSYEDklfdvcGSQDEESDLERLKEEI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1434 ERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADL 1513
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1514 TEQIAENGKSIHELEKSRKQM--ELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNY 1591
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELrnKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1592 QRTVETMQGA-LDAEVRSRNEAIRLKK-KMEGDLNEIEiQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLK 1669
Cdd:TIGR00606 809 AQQAAKLQGSdLDRTVQQVNQEKQEKQhELDTVVSKIE-LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1670 EQLaiverranllqaevEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKkkletdltqlqsevedasrda 1749
Cdd:TIGR00606 888 EQL--------------VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK--------------------- 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1750 rnaEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkgGKKQIQKlETRIR 1821
Cdd:TIGR00606 933 ---ETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLM 1003
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1822 ELEFELEGEQKRNTESVKGLRKYERRVKEL-----TYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTK 1896
Cdd:TIGR00606 1004 RQDIDTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
970
....*....|....
gi 6981234 1897 FRKAQHELEEAEER 1910
Cdd:TIGR00606 1084 IKHFKKELREPQFR 1097
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
847-1760 |
3.59e-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: 58.90 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLvqekndlqlqvqaesenlldaeercdqlikakFQLEAKIKEVTER 926
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKI--------------------------------MKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 927 AEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEELAGLDETIAKLTREKKALQEAH-- 1004
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKte 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1005 ---QQTLDDLQAEEDKVNSLSK----LKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQL 1077
Cdd:TIGR00606 345 llvEQGRLQLQADRHQEHIRARdsliQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1078 DERLKKKDFEYSQLQSKVEDEqtlSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSerleeaggv 1157
Cdd:TIGR00606 425 QEQADEIRDEKKGLGRTIELK---KEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK--------- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1158 tSTQIELNKKREAEFLKLRRDLEEAtlqheatvatlRKKHADSAAELAEQIDNLQRVkQKLEKEKSEFKLEIDDLSSSVE 1237
Cdd:TIGR00606 493 -NSLTETLKKEVKSLQNEKADLDRK-----------LRKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHS 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1238 SVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSR------SKQAFTQ 1311
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcGSQDEES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1312 QIEELKRQLEEENKAKNALAHALQssrhdcdlLREQYEEEQEGKaelqralSKANSEVAQwrtkyetDAIQRTEELEEAK 1391
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEFI 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1392 KKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELE-- 1469
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGti 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1470 -AALKESRSLSTELFKLKNAYEEaldqletVKRENKNLEQEIADLteQIAENGKSIHELEKSRKQMELEKADIQMALEEA 1548
Cdd:TIGR00606 778 mPEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1549 EAALEHEEAKILRIQLELTQVKSEiDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEI 1628
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1629 QLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKE-QLAIVERRANLLQAEVEELRATLEQTERARKLAEQEL 1707
Cdd:TIGR00606 928 LISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDdYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 1708 LDSNERVQLLHTQNTSLIHTK--KKLETDLTQLQSEV-EDASRDARNAEEKAKKAI 1760
Cdd:TIGR00606 1008 DTQKIQERWLQDNLTLRKRENelKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1385-1919 |
3.84e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1385 EELEEAKkklaQRLQDSEEQVEA---VNAKCASLEKTKQRLQG-EVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTK 1460
Cdd:COG4913 235 DDLERAH----EALEDAREQIELlepIRELAERYAAARERLAElEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1461 CEESQAELEAALKESRSLstelfklKNAYEEA-LDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKA 1539
Cdd:COG4913 311 LERLEARLDALREELDEL-------EAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1540 DIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKR---NYQRTVETMQGALDAEVRSRNEAIRLK 1616
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksNIPARLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1617 kkmeGDLneIEIQLSHAN-RQAAETikhlrsvqgqlkdtqlhlddALRGQ--------EDLKEQLAIVERRanllqaeve 1687
Cdd:COG4913 464 ----GEL--IEVRPEEERwRGAIER--------------------VLGGFaltllvppEHYAAALRWVNRL--------- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1688 ELRATLeQTERARKLAEQELLDSNERVQLLHtqntslihtkkKLETDLTQLQSEVED--ASRDA----RNAEE--KAKKA 1759
Cdd:COG4913 509 HLRGRL-VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAelGRRFDyvcvDSPEElrRHPRA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1760 ITDAAMmaeelkkeqdtsahlerMKKNLEQTVKDLQHRLDE--------AEQLALKggKKQIQKLETRIRELEFELEG-- 1829
Cdd:COG4913 577 ITRAGQ-----------------VKGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLEAle 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1830 -------EQKRNTESVKGLRKYERRVKELTY---QSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRK 1899
Cdd:COG4913 638 aeldalqERREALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580
....*....|....*....|
gi 6981234 1900 AQHELEEAEERADIAESQVN 1919
Cdd:COG4913 718 LEKELEQAEEELDELQDRLE 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
855-1404 |
8.86e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 855 EEFQKTKDELAKSEAKRKELEekLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER-----AED 929
Cdd:COG4913 262 ERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 930 EEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQ 1006
Cdd:COG4913 340 LEQLEREIERLERELEErerRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1007 TLDDLQAEedkVNSLSKLKSKLEQQVDDLESSLEQEKKLRVD---------------------LER-------------- 1051
Cdd:COG4913 420 ELRELEAE---IASLERRKSNIPARLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaIERvlggfaltllvppe 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1052 ---------NKRKLEGDL-----KLAQESILDLENDKQQLDERLKKKDFEYS-----QLQS-----KVEDEQTLSlQLQK 1107
Cdd:COG4913 497 hyaaalrwvNRLHLRGRLvyervRTGLPDPERPRLDPDSLAGKLDFKPHPFRawleaELGRrfdyvCVDSPEELR-RHPR 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1108 KIkelqarieeleeeieaeraTRAKTEKQRSD-YARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQH 1186
Cdd:COG4913 576 AI-------------------TRAGQVKGNGTrHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1187 EATVATLRKKHA------------DSAAELAEQIDNLQRVKQKLEKEKSEFkleiddlsssvesvskskanlekicRTLE 1254
Cdd:COG4913 637 EAELDALQERREalqrlaeyswdeIDVASAEREIAELEAELERLDASSDDL-------------------------AALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1255 DQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAF-TQQIEELKRQLEEENKAKnALAHA 1333
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAALGDAVER-ELREN 770
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1334 LQSSRHDCDLLREQYEEEQEGKaeLQRALSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQDSEEQ 1404
Cdd:COG4913 771 LEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSIE 846
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1508 |
9.24e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 845 ETEKEMATMKEEfQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLdaEERCDQLIKAKFQLEAKIKEVT 924
Cdd:COG4913 239 RAHEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL--EAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 925 ERAEDEEEINAELTAKKRKLE-DECSELKKDIDDLELTLAKVEkekhateNKVKNLTEELAGLDETIAKLTREKKALQEA 1003
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERE-------RRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1004 HQQTLDDLQAEEDKV-NSLSKLKSKLEQQVDDLEsSLEQEKKlrvDLERNKRKLEGDLKLAQESIldlendKQQLDERLK 1082
Cdd:COG4913 389 AAALLEALEEELEALeEALAEAEAALRDLRRELR-ELEAEIA---SLERRKSNIPARLLALRDAL------AEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1083 KKDF--EYsqLQSKVEDE------------QTLSL--------QLQKKIKELQarieeleeeieaeRATRAKTEKQRSDY 1140
Cdd:COG4913 459 ELPFvgEL--IEVRPEEErwrgaiervlggFALTLlvppehyaAALRWVNRLH-------------LRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1141 ARELEELSERLEEAGGVTstqIELNKKRE--AEFLKLRRDLE----EATLQHEA---TVATLRKK------HADSAAELA 1205
Cdd:COG4913 524 PDPERPRLDPDSLAGKLD---FKPHPFRAwlEAELGRRFDYVcvdsPEELRRHPraiTRAGQVKGngtrheKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1206 EQI---DNLQRVKQkLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLE--DQLSEARGKNEETQRSLSELTTQKSR 1280
Cdd:COG4913 601 RYVlgfDNRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1281 LQTEAGELsRQLEEkesivsQLSRSKqaftQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQR 1360
Cdd:COG4913 680 LDASSDDL-AALEE------QLEELE----AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1361 AlskansEVAQWRTKYETDAIQRT--EELEEAKKKLAQRLQDSEEQVEAVnakcasLEKTKQRLQGEVEDLMVDVERANS 1438
Cdd:COG4913 749 A------LLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESLPE 816
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1439 LAAALDKKQRNfdkVLAEWktkceesQAELEAALKES--RSLSTELFKLKNAYEEALDQLETVkreNKNLEQ 1508
Cdd:COG4913 817 YLALLDRLEED---GLPEY-------EERFKELLNENsiEFVADLLSKLRRAIREIKERIDPL---NDSLKR 875
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1384-1940 |
1.03e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1384 TEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKvLAEWKTKCEE 1463
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR-KAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1464 SQAELEAALKESRSLSTELFKlknayEEALDQLETVKRENKNLEQEIADLTEQI--AENGKSIHELEKS----RKQMELE 1537
Cdd:PTZ00121 1169 ARKAEDAKKAEAARKAEEVRK-----AEELRKAEDARKAEAARKAEEERKAEEArkAEDAKKAEAVKKAeeakKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1538 KADIQMALEEAEAALEHEEAKILRIQlelTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRS--RNEAIRL 1615
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQ---AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAeeAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1616 KKKMEgdlnEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRatleQ 1695
Cdd:PTZ00121 1321 KKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK----K 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1696 TERARKLAEQELLDSNErVQLLHTQNTSLIHTKKKLETdlTQLQSEVEDASRDARNAEEKAKKAitDAAMMAEELKKEQD 1775
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE--KKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1776 TSAHLERMKKNLEQTVKdlqhrldeAEQLALKGGKKQIQKLETRIRElefelegEQKRNTESVKglRKYERRVKELTYQS 1855
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADEAKKAA-------EAKKKADEAK--KAEEAKKADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1856 EEDRKnvlrlqdlvdKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVV 1935
Cdd:PTZ00121 1531 EEAKK----------ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
....*
gi 6981234 1936 HESEE 1940
Cdd:PTZ00121 1601 YEEEK 1605
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1256-1851 |
1.06e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 57.07 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1256 QLSEARgKNEETQRSLSELT-TQKSRLQTEAGELS-----------------------------------RQLEEKESI- 1298
Cdd:pfam07111 71 QLQELR-RLEEEVRLLRETSlQQKMRLEAQAMELDalavaekagqaeaeglraalagaemvrknleegsqRELEEIQRLh 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1299 VSQLSRSKQAFTQQIEELKRQLEEENKAKNAL-------AHALQSSRHDCDLLREQY---EEEQEGKAELQRALSKANSE 1368
Cdd:pfam07111 150 QEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLRKQLsktQEELEAQVTLVESLRKYVGE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1369 VAQWRTKYETDAIQRtEELEEAKKKLAQRLQDSEEQVEAVNAKCASLektKQRLQGEVEDLMVDVERANSLAAALDKKQR 1448
Cdd:pfam07111 230 QVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATVELLQVRVQSL---THMLALQEEELTRKIQPSDSLEPEFPKKCR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1449 NfdkVLAEWKTKCEESQAELEAALKESRSlstelfklknayeealdqletvkrENKNLEQEIADLTEQIAENGKsihele 1528
Cdd:pfam07111 306 S---LLNRWREKVFALMVQLKAQDLEHRD------------------------SVKQLRGQVAELQEQVTSQSQ------ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1529 ksrkqmelEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRnYQRTVETMQGALDAEVRS 1608
Cdd:pfam07111 353 --------EQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTR 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1609 RNEAIrlkkkmeGDLNEIEIQLSHANRQaAETIKHLRSVQGQLKDTQLHL----DDALRGQEDLKEQLAIVERRANLLQA 1684
Cdd:pfam07111 424 VEQAV-------ARIPSLSNRLSYAVRK-VHTIKGLMARKVALAQLRQEScpppPPAPPVDADLSLELEQLREERNRLDA 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1685 EVeELRATLEQTE--RARKLAEQELLDSNERVQllhtqntslihtkkKLETDLTQLQSEVEDASRDARNAEEKAKKAITD 1762
Cdd:pfam07111 496 EL-QLSAHLIQQEvgRAREQGEAERQQLSEVAQ--------------QLEQELQRAQESLASVGQQLEVARQGQQESTEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1763 AAMMAEELKKEQDTSAH-----LERMKKNLEQTVKDLQHRLDEA--EQLALKGGKKQIQKLETRIRELEFELE--GEQKR 1833
Cdd:pfam07111 561 AASLRQELTQQQEIYGQalqekVAEVETRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHRATQEKERNQELRrlQDEAR 640
|
650
....*....|....*...
gi 6981234 1834 NTESvkglRKYERRVKEL 1851
Cdd:pfam07111 641 KEEG----QRLARRVQEL 654
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
863-1018 |
1.12e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.93 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 863 ELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER-AEDEEEINAELTAKK 941
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARiKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 942 RK-LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKV 1018
Cdd:COG1579 91 YEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1386-1828 |
1.16e-07 |
|
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: 56.62 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1386 ELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDL-------MVDVERANSLAAALDKKQRNFDKVLA--- 1455
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLesgddsgTPGGKKYLLLQKQLEQLQEENFRLETard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1456 EWKTKCEE----------SQAELEAALKESRSLSTELFKLKNA-------------YEEALDQLETVKRENKNLEQEIAD 1512
Cdd:pfam05622 84 DYRIKCEElekevlelqhRNEELTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1513 LTEQIAENGKSIHELEKSRKQMELEKADIQmaleEAEAALEHEEAKILRIQLELTQ-------VKSEIDRKIAEKD---E 1582
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKleekleaLQKEKERLIIERDtlrE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1583 EIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANrqaaetiKHLRSVQG-----QLKDTQLH 1657
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHEN-------KMLRLGQEgsyreRLTELQQL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1658 LDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLeqterarklaeqelldsnervQLLHTQNTSLIHTKKKLETDLTQ 1737
Cdd:pfam05622 313 LEDANRRKNELETQNRLANQRILELQQQVEELQKAL---------------------QEQGSKAEDSSLLKQKLEEHLEK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1738 LQSEVEDASRDARNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLEQ---TVKDLQHRLDEAEQLALKGG 1809
Cdd:pfam05622 372 LHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQAL 451
|
490
....*....|....*....
gi 6981234 1810 KKQIQKLETRIRELEFELE 1828
Cdd:pfam05622 452 KNQLLEKDKKIEHLERDFE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1661-1891 |
1.30e-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: 55.93 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1661 ALRGQEDLKEQLaivERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQS 1740
Cdd:COG4942 14 AAAAQADAAAEA---EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1741 EVEDASRDARNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNLEQTVKDLQHRLDE--AEQLALKGGKKQIQ 1814
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1815 KLETRIRELEFELEGEQKR----NTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQA 1890
Cdd:COG4942 171 AERAELEALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
.
gi 6981234 1891 N 1891
Cdd:COG4942 251 L 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1311-1927 |
1.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1311 QQIEELKRQLEEENKAKNALAHALQssrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQwrTKYETdAIQRTEELEEA 1390
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1391 KKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE-VEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELE 1469
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1470 AALKESR----SLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLteqiAENGKSI-HELEKSRKQM--ELEKADIQ 1542
Cdd:COG4913 384 ALRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNIpARLLALRDALaeALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1543 maleeaeaaleheeakiLRIQLELTQVKseidrkiaEKDEE----IEQLKRNYQRT--VETmqgALDAEVRSRNEAIRLK 1616
Cdd:COG4913 460 -----------------LPFVGELIEVR--------PEEERwrgaIERVLGGFALTllVPP---EHYAAALRWVNRLHLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1617 KKMegDLNEIEIQLSHANRQAAETikhlRSVQGQLkDTQLHlddALRGQedLKEQLAiveRRANLLQAE-VEELRA---- 1691
Cdd:COG4913 512 GRL--VYERVRTGLPDPERPRLDP----DSLAGKL-DFKPH---PFRAW--LEAELG---RRFDYVCVDsPEELRRhpra 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1692 -TLE-QTERARKLAEQELLDSNERVQLLHTQNTSLIhtkKKLETDLTQLQSEVEDASRDArnaeekakkaitdaammaEE 1769
Cdd:COG4913 577 iTRAgQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKL---AALEAELAELEEELAEAEERL------------------EA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1770 LKKEQDTsahLERmKKNLEQTVKDLQHRLDEAEQLAlkggkKQIQKLETRIRELEfelegeqkrntESVKGLRKYERRVK 1849
Cdd:COG4913 636 LEAELDA---LQE-RREALQRLAEYSWDEIDVASAE-----REIAELEAELERLD-----------ASSDDLAALEEQLE 695
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1850 ELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRD 1927
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
970-1224 |
1.96e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 970 HATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSL----EQEKKL 1045
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1046 RVDLERNKRKLEGDLKLAQESildleNDKQQLDERLKKKDFeySQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEA 1125
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1126 ERATRAKTEKQRsdyareleelserleeaggvtstqielnkkreAEFLKLRRDLEEATLQHEATVATLRKK---HADSAA 1202
Cdd:COG4942 169 LEAERAELEALL--------------------------------AELEEERAALEALKAERQKLLARLEKElaeLAAELA 216
|
250 260
....*....|....*....|..
gi 6981234 1203 ELAEQIDNLQRVKQKLEKEKSE 1224
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1244-1492 |
2.05e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1244 ANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEE 1323
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1324 nkaKNALAhalqssrhdcDLLREQYEEEQEGKAELqrALSKANSEVAQWRTKYetdaiqrteeleeakkkLAQRLQDSEE 1403
Cdd:COG4942 103 ---KEELA----------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQY-----------------LKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1404 QVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELF 1483
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
....*....
gi 6981234 1484 KLKNAYEEA 1492
Cdd:COG4942 231 RLEAEAAAA 239
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1039-1322 |
2.62e-07 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 55.63 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1039 LEQE-KKLRVDLERNkRKLEGDLKLAQESILDLE-------NDKQQLDERLKKKdfEYSQLQSKVEDEQTLSlQLQKKIK 1110
Cdd:pfam09726 400 LEQDiKKLKAELQAS-RQTEQELRSQISSLTSLErslkselGQLRQENDLLQTK--LHNAVSAKQKDKQTVQ-QLEKRLK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1111 ELQArieeleeeieaeraTRAKTEKQrsdyareleelserleeaggvtstqieLNKKREaeflklRRDLEEATLQHEATV 1190
Cdd:pfam09726 476 AEQE--------------ARASAEKQ---------------------------LAEEKK------RKKEEEATAARAVAL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1191 AtlrkkhadsAAELAEQIDNLQRVKQKLEKE----KSEFKL---EIDDLSSSVESVSKSKANlEKICRTLEDQLSEARGK 1263
Cdd:pfam09726 509 A---------AASRGECTESLKQRKRELESEikklTHDIKLkeeQIRELEIKVQELRKYKES-EKDTEVLMSALSAMQDK 578
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981234 1264 NEETQRSLSELTTQKSRLQTEAGELSRQLEekesIVSQLSRSKQaftQQIEELKRQLEE 1322
Cdd:pfam09726 579 NQHLENSLSAETRIKLDLFSALGDAKRQLE----IAQGQIYQKD---QEIKDLKQKIAE 630
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1069-1610 |
3.10e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1069 DLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARieelEEEIEAERATRAKTEKQRSDYARELEELS 1148
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1149 ERLEEAG----------GVTSTQIELNKKREAEFLKLRRDLEEaTLQHEATVATLRKKHADSaaeLAEQIDNLQRVKQKL 1218
Cdd:PRK02224 286 ERLEELEeerddllaeaGLDDADAEAVEARREELEDRDEELRD-RLEECRVAAQAHNEEAES---LREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1219 EKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKEsi 1298
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1299 vsqlsrskqaftQQIEElKRQLEEENKAKNAlAHALQSSRHDCDLlreqyEEEQEGKAELQRALSKANSEVAQWRTKYET 1378
Cdd:PRK02224 440 ------------ERVEE-AEALLEAGKCPEC-GQPVEGSPHVETI-----EEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1379 -----DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDlmvdveransLAAALDKKQRNFDKV 1453
Cdd:PRK02224 501 aedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE----------KREAAAEAEEEAEEA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1454 LAEWKTkCEESQAELEAALKESRSLSTELFKLKNAYE------EALDQLETVKRENKNLEQEIADLTEQIAE--NGKSIH 1525
Cdd:PRK02224 571 REEVAE-LNSKLAELKERIESLERIRTLLAAIADAEDeierlrEKREALAELNDERRERLAEKRERKRELEAefDEARIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1526 ELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRK--IAEKDEEIEQLKRNyQRTVETMQGALD 1603
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERReaLENRVEALEALYDE-AEELESMYGDLR 728
|
....*..
gi 6981234 1604 AEVRSRN 1610
Cdd:PRK02224 729 AELRQRN 735
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1011-1269 |
3.62e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1011 LQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQ 1090
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1091 LQSKVEDEQTlslQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYAreleelserleeaggvtstqiELNKKREA 1170
Cdd:COG4942 95 LRAELEAQKE---ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK---------------------YLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1171 EFLKLRRDLEEatlqheatVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKIC 1250
Cdd:COG4942 151 QAEELRADLAE--------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250
....*....|....*....
gi 6981234 1251 RTLEDQLSEARGKNEETQR 1269
Cdd:COG4942 223 EELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
935-1139 |
3.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 935 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAE 1014
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1015 EDKVNSLSKLKS------------KLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLK 1082
Cdd:COG3883 99 GGSVSYLDVLLGsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 1083 KKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSD 1139
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
866-1446 |
4.31e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 866 KSEAKRKELEEKLVTLVQEKNDLQLQVQAEsenLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLE 945
Cdd:pfam05483 205 QAENARLEMHFKLKEDHEKIQHLEEEYKKE---INDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQD 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 946 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEA--HQQTLDDLQAEEDKVNSLSk 1023
Cdd:pfam05483 282 ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnKAKAAHSFVVTEFEATTCS- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1024 LKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDfEYSQLQSKVED----EQ 1099
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD-EKKQFEKIAEElkgkEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1100 TLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIEL--------------- 1164
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELtqeasdmtlelkkhq 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1165 -----NKKREAEFLKLRRDLEEATLQheatvatLRkkhadsaaelaeqiDNLQRVKQKLEKEKSEFKLEIDDLSSSVESV 1239
Cdd:pfam05483 520 ediinCKKQEERMLKQIENLEEKEMN-------LR--------------DELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1240 SKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVS----QLSRSKQAFTQQIEE 1315
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNklelELASAKQKFEEIIDN 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1316 LKRQLEEENKAKNALAHALQSSRHDCDllrEQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAK-KKL 1394
Cdd:pfam05483 659 YQKEIEDKKISEEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKnKEQ 735
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1395 AQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKK 1446
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1470-1717 |
5.00e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1470 AALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKAdiqmaleeae 1549
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1550 aaleheeakilriqlELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLkkkmegdlneiEIQ 1629
Cdd:COG4942 87 ---------------ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR-----------LQY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1630 LSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLD 1709
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
....*...
gi 6981234 1710 SNERVQLL 1717
Cdd:COG4942 221 EAEELEAL 228
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1665-1913 |
5.68e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1665 QEDLKEQLAIVERRANLLQAEVEELRATLEQTERARK--LAEQELLDSNERVQLLHTQNTSlihtkkkLETDLTQLQSEV 1742
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSE-------LESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1743 EDASRDARNAEEKAKKAITDAAMMAEelkkeqdtSAHLERMKKNLEQTVKDLQhrldeaeQLALKGGKK--QIQKLETRI 1820
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQ--------SPVIQQLRAQLAELEAELA-------ELSARYTPNhpDVIALRAQI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1821 RELEFELEGEQKRNTESVKG-LRKYERRVKELTYQSEEDRKNVLRLQdlvdKLQVKVKSYKRQAEEADEQANVHLTKFRK 1899
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEE 376
|
250
....*....|....
gi 6981234 1900 AQheLEEAEERADI 1913
Cdd:COG3206 377 AR--LAEALTVGNV 388
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1675-1919 |
6.13e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1675 VERRANLLQAEVEELRATLEQTERARKlaEQELLdsnERVQLLHTQNTSLIHTKKKLETDLTQLQseVEDASRDARNAEE 1754
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDARE--QIELL---EPIRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1755 KakkaitdaammAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEgEQKRN 1834
Cdd:COG4913 296 E-----------LEELRAELAR---LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE-ERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1835 tesvkgLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEeaEERADIA 1914
Cdd:COG4913 361 ------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE--AEIASLE 432
|
....*
gi 6981234 1915 ESQVN 1919
Cdd:COG4913 433 RRKSN 437
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1350-1905 |
6.32e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.73 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1350 EEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK---------------------KLAQRLQDSEEQVEAV 1408
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieaqrkaiqelqfenekvslKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1409 NAK---CASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKES----RSLSTE 1481
Cdd:pfam05483 151 NATrhlCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDhekiQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1482 LFKLKNAYEEALDQL--ETVKRENKN-----LEQEIADLTEQIAENGK----SIHELEKSRKQMELEKADIQMALEEAEA 1550
Cdd:pfam05483 231 YKKEINDKEKQVSLLliQITEKENKMkdltfLLEESRDKANQLEEKTKlqdeNLKELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1551 ALEHEEAKILRIQLELTQVKSEIDRKIAEKDE-----------------EIEQLKRNYQRTVETMQGALD---AEVRSRN 1610
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQMEELNKakaahsfvvtefeattcSLEELLRTEQQRLEKNEDQLKiitMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1611 ----EAIRLKKKMEGDLNEIEIQLSHANRQAAETiKHLRSVQGQLKDTQLHLDDALRGQE----DLKEQLAIVERRANLL 1682
Cdd:pfam05483 391 seleEMTKFKNNKEVELEELKKILAEDEKLLDEK-KQFEKIAEELKGKEQELIFLLQAREkeihDLEIQLTAIKTSEEHY 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1683 QAEVEELRATLEQteraRKLAEQELLDSNERVQL----LHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKK 1758
Cdd:pfam05483 470 LKEVEDLKTELEK----EKLKNIELTAHCDKLLLenkeLTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1759 AITDAAMMAEELKKEQD-TSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGG--KKQIQKLETRIRELEFELEGEQKRNT 1835
Cdd:pfam05483 546 LRDELESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQENKALKKKGS 625
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1836 ESVKGLRKYERRVKELTYQSEEDRKnvlRLQDLVDKLQVKVKSYKRQAE---EADEQANVHLTKFRKAQHELE 1905
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISEEkllEEVEKAKAIADEAVKLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1346-1583 |
6.50e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1346 EQYEEEQEGKAELQRALSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE 1425
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1426 VEDLMVDVerANSLAAALDKKQRNFDKVLAEwktkcEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKREnkn 1505
Cdd:COG4942 99 LEAQKEEL--AELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE--- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1506 LEQEIADLTEQIAENGKSIHELEKSRKqmelEKADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEE 1583
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1742-1918 |
7.44e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.09 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1742 VEDASRDARNAEEKAKKAITDAAmmAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKLETRIR 1821
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHE--ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE--------RIERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1822 ELEFELEGEQKRNTEsvkgLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLqvkvKSYKRQAEEADEQANVHLTKFRKaq 1901
Cdd:COG2433 452 EARSEERREIRKDRE----ISRLDREIERLERELEEERERIEELKRKLERL----KELWKLEHSGELVPVKVVEKFTK-- 521
|
170
....*....|....*..
gi 6981234 1902 HELEEAEERADIAESQV 1918
Cdd:COG2433 522 EAIRRLEEEYGLKEGDV 538
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
838-1112 |
7.46e-07 |
|
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: 54.36 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 838 KPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKlVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKA---KF 914
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEA-EKARQAEMDRQAAIYAEQERMAMERERELERIRQeerKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 915 QLE-----------AKIKEV----TERAEDEEEINAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKhATENKVKN 978
Cdd:pfam17380 361 ELErirqeeiameiSRMRELerlqMERQQKNERVRQELeAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-ARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 979 LTEELAGLDETIAKLTREKKALQEAHQQtlddlQAEEDKVNSLSKLKSKLEQQVDD------LESSLEQEKKLRVDLERN 1052
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQVERLRQ-----QEEERKRKKLELEKEKRDRKRAEeqrrkiLEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1053 KRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYS---QLQSKVEDEQTLSLQLQKKIKEL 1112
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMEREREM 577
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1278-1535 |
7.82e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.13 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1278 KSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE 1357
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1358 L---QRALSKANSEvaqwrtkyetdAIQRTEELEEAKKKLAQRLQDSEeqveavnakcASLEKTKQRlqgevedlmvdVE 1434
Cdd:pfam07888 113 LseeKDALLAQRAA-----------HEARIRELEEDIKTLTQRVLERE----------TELERMKER-----------AK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1435 RANSLaaaldkkqrnfdkvLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLT 1514
Cdd:pfam07888 161 KAGAQ--------------RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
250 260
....*....|....*....|.
gi 6981234 1515 EQIAENGKSIHELEKSRKQME 1535
Cdd:pfam07888 227 RKEAENEALLEELRSLQERLN 247
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
652-676 |
8.87e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 50.81 E-value: 8.87e-07
10 20
....*....|....*....|....*
gi 6981234 652 FRENLNKLMSNLRTTHPHFVRCIIP 676
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
968-1642 |
9.83e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 968 EKHATENKVKNLTEELAGLDET---IAKLTREKKALQEAhQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKk 1044
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAheaLEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1045 lRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLkkkdfeysqLQSKVEDEQtlslQLQKKIKELQarieeleeeie 1124
Cdd:COG4913 297 -LEELRAELARLEAELERLEARLDALREELDELEAQI---------RGNGGDRLE----QLEREIERLE----------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1125 aeratRAKTEKQRsdyareleelserleeaggvtstqielnkkREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAEL 1204
Cdd:COG4913 352 -----RELEERER------------------------------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1205 AEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELttqksrLQTE 1284
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL------IEVR 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1285 AGELS--------------------RQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDC-DL 1343
Cdd:COG4913 471 PEEERwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAW 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1344 LREQYEEEQ-----EGKAELQRA--------LSKANSEVAQ------WRTKYET--DAIQRTEELEEAKKKLAQRLQDSE 1402
Cdd:COG4913 551 LEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSRYVLgfDNRAKLAALEAELAELEEELAEAE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1403 EQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERAnSLAAALdkkqrnfdkvlaewktkceesqAELEAALKESRSLSTEL 1482
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREI----------------------AELEAELERLDASSDDL 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1483 FKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRI 1562
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1563 QLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGD------------LNEIEIQ- 1629
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeerfkelLNENSIEf 847
|
730
....*....|....*.
gi 6981234 1630 ---LSHANRQAAETIK 1642
Cdd:COG4913 848 vadLLSKLRRAIREIK 863
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
840-1113 |
1.01e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 840 LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLqlqVQAESENLL---DAEERCDQLikakfql 916
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRavkDIKQERDQL------- 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 917 eakIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlteeLAGLDETIAKLTRE 996
Cdd:pfam15921 659 ---LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMG 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 997 KKALQEAHQQTLDDLQAE----EDKVNSLSKLKSKLEQQVDDLESSLEQekklrVDLERNkrKLEGDLKLAQESILDLEN 1072
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKiqflEEAMTNANKEKHFLKEEKNKLSQELST-----VATEKN--KMAGELEVLRSQERRLKE 804
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6981234 1073 DKQQLDERLKKKDFEYSQLQSKV--EDEQTLSLQLQKK--IKELQ 1113
Cdd:pfam15921 805 KVANMEVALDKASLQFAECQDIIqrQEQESVRLKLQHTldVKELQ 849
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1018-1701 |
1.13e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1018 VNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLK-LAQE--SILDLENDKQQLDERLKKKDFEYSQLQSK 1094
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKqIADDekSHSITLKEIERLSIEYNNAMDDYNNLKSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1095 VEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSdyareleelserleeaggVTSTQIELNKKREAEFLK 1174
Cdd:PRK01156 241 LNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMK------------------IINDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1175 LRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKleKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLE 1254
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1255 DQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEeenkaknalahaL 1334
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------------M 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1335 QSSRHDCDLLReqyeeeqegkaelqralskansevaqwrTKYETDAIQR-TEELEEAKKKLAQRLQDSEEQVEAVNAKCA 1413
Cdd:PRK01156 449 LNGQSVCPVCG----------------------------TTLGEEKSNHiINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1414 SLEKTKQRLQG-EVEDLMVDVERANSLAAALdKKQRNFDKVLAEWKTKCEEsqaeleaALKESRSLSTELFKLKN-AYEE 1491
Cdd:PRK01156 501 DLKKRKEYLESeEINKSINEYNKIESARADL-EDIKIKINELKDKHDKYEE-------IKNRYKSLKLEDLDSKRtSWLN 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1492 ALDQLETVkrenknleqEIADLTEQIAENGKSIHELEKSRKQMELEKADIqmaleeaeaaleheeakilriqleltqvKS 1571
Cdd:PRK01156 573 ALAVISLI---------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD----------------------------KS 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1572 EIDRKIAEKDEEIEQLKRNY------QRTVETMQGALDaevrSRNEAIRLKKKMEGDLNEIEIQLSHANrqaaetikhlr 1645
Cdd:PRK01156 616 YIDKSIREIENEANNLNNKYneiqenKILIEKLRGKID----NYKKQIAEIDSIIPDLKEITSRINDIE----------- 680
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 1646 svqGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARK 1701
Cdd:PRK01156 681 ---DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1263-1873 |
1.29e-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: 53.49 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1263 KNEETQRSLSELTTQKSRL---QTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRH 1339
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1340 DCDLLREQYEEEQEGKAELQRALSKANsevaqwrtKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTK 1419
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENK--------KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1420 QRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWkTKCEESQAELEAALKEsrsLSTELFKLKNAYEEALDQLETV 1499
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI-SELKKQNNQLKDNIEK---KQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1500 KRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADiqMALEEAEAALEHEEAKILRIQLELTQVKSEID---RK 1576
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELKSELKNQEKKLEEIQNQISqnnKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1577 IAEKDEEIEQLKRNYQRtvetmqgaldaevrSRNEAIRLKKKMEGDLNEIEiQLSHANRQAAETIKHLRSvqgQLKDTQL 1656
Cdd:TIGR04523 337 ISQLNEQISQLKKELTN--------------SESENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLES---QINDLES 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1657 HLDDALRGQEDLKEQLAIVERRANLLQAEVEELRAT----------LEQTERARKLAEQELldsNERVQLLHTQNTSLIH 1726
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknnseikdLTNQDSVKELIIKNL---DNTRESLETQLKVLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1727 TKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQ-LA 1805
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFeLK 555
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1806 LKGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQ 1873
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1259-1629 |
1.80e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1259 EARGKNEETQRSLSELTTQKS-----RLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKnalaha 1333
Cdd:pfam17380 237 ERRKESFNLAEDVTTMTPEYTvryngQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR------ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1334 lqssrhDCDLLREQYEEEQEGKAELQRAlskansevAQWRTKYETDAIQRTEELEEAkkklaqRLQDSEEQVEAVNAKCA 1413
Cdd:pfam17380 311 ------EVERRRKLEEAEKARQAEMDRQ--------AAIYAEQERMAMERERELERI------RQEERKRELERIRQEEI 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1414 SLEKTKQRlqgEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTElfKLKNAYEEAL 1493
Cdd:pfam17380 371 AMEISRMR---ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR--EVRRLEEERA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1494 DQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKS-RKQMELEKA-----DIQMALEEAEAALEHEEAKILRIQLELT 1567
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEkRDRKRAEEQrrkilEKELEERKQAMIEEERKRKLLEKEMEER 525
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1568 Q--VKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGAldAEVRSRNEAIRLKKKMEGDLNEIEIQ 1629
Cdd:pfam17380 526 QkaIYEEERRREAEEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKA 587
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
853-1334 |
1.88e-06 |
|
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: 53.26 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 853 MKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESE---NLLDAEERCDQLIKAKFQLEAKIKEVTERAED 929
Cdd:pfam01576 550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQlvsNLEKKQKKFDQMLAEEKAISARYAEERDRAEA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 930 E------------------EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETI- 990
Cdd:pfam01576 630 EareketralslaraleeaLEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELq 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 991 ----AKLtREKKALQEAHQQTLDDLQAEEDKVNSLSKLkskLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQES 1066
Cdd:pfam01576 710 atedAKL-RLEVNMQALKAQFERDLQARDEQGEEKRRQ---LVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1067 ILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQ-------TLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSD 1139
Cdd:pfam01576 786 IDAANKGREEAVKQLKKLQAQMKDLQRELEEARasrdeilAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDE 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1140 YARELeelserleeAGGVTSTQIELNKKR--EAEFLKLRRDLEEATLQHEATVATLRKKHADS---AAELAEQIDNLQRV 1214
Cdd:pfam01576 866 LADEI---------ASGASGKSALQDEKRrlEARIAQLEEELEEEQSNTELLNDRLRKSTLQVeqlTTELAAERSTSQKS 936
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1215 ---KQKLEKEKSEFKLEIDDLSSSVESVSKSK-ANLEKICRTLEDQL-SEARGKN------EETQRSLSELTTQ------ 1277
Cdd:pfam01576 937 esaRQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQLeQESRERQaanklvRRTEKKLKEVLLQvederr 1016
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1278 ---KSRLQTEAG-----ELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHAL 1334
Cdd:pfam01576 1017 hadQYKDQAEKGnsrmkQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
842-1031 |
2.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ------ 915
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 916 -----LEAK-IKEVTERA-------EDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE 982
Cdd:COG3883 104 yldvlLGSEsFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981234 983 LAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQ 1031
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
861-1113 |
2.22e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 861 KDELAKSEAKRKELEEKL---VTLVQEKNDLQLQVQAESENLLDAEERCDQLIKA--KFQLEAKIKEVTERAED-EEEIn 934
Cdd:COG3206 106 DEDPLGEEASREAAIERLrknLTVEPVKGSNVIEISYTSPDPELAAAVANALAEAylEQNLELRREEARKALEFlEEQL- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 935 AELTAKKRKLEDECSELKKD----------------IDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTrEKK 998
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKnglvdlseeaklllqqLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL-QSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 999 ALQEAHQQtLDDLQAEEDKVNSLSKLKS----KLEQQVDDLESSLEQEkklrvdLERNKRKLEGDLKLAQESILDLENDK 1074
Cdd:COG3206 264 VIQQLRAQ-LAELEAELAELSARYTPNHpdviALRAQIAALRAQLQQE------AQRILASLEAELEALQAREASLQAQL 336
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6981234 1075 QQLDERLK---KKDFEYSQLQSKVEDEQTLSLQLQKKIKELQ 1113
Cdd:COG3206 337 AQLEARLAelpELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1735-1933 |
2.39e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1735 LTQLQSEVEDASRDARNAEE----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEqlalkggk 1810
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-------- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1811 KQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQA 1890
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6981234 1891 NVHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRM 1933
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1504-1927 |
2.46e-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: 52.52 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1504 KNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEH-EEAKILRIQLELTQVK-SEIDRKIAEKD 1581
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDpAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1582 EEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKME---GDLNEIEIQLshanrQAAETikHLRSVQGQLKDTQLHL 1658
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDqlkQELSKKESEL-----LALQT--KLETLTNQNSDCKQHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1659 ddalrgqEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERV-----QLLHTQNTSLIHTKK--KL 1731
Cdd:pfam10174 327 -------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKstlagEIRDLKDMLDVKERKinVL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1732 ETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EQTVKDLQHRLDEAEQL--ALKG 1808
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1809 GKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDlvdklqvkvKSYKRQAEEADE 1888
Cdd:pfam10174 480 LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN---------QLKKAHNAEEAV 550
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 6981234 1889 QANVHLT-KFRKAQHELEEAEERADIAESQVNKLRAKTRD 1927
Cdd:pfam10174 551 RTNPEINdRIRLLEQEVARYKEESGKAQAEVERLLGILRE 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1629-1812 |
2.62e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1629 QLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQT-----ERARKLA 1703
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1704 EQ-----------------ELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDaamM 1766
Cdd:COG3883 97 RSggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE---L 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6981234 1767 AEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQ 1812
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1349-1522 |
3.82e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1349 EEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqdsEEQVEavnAKCASLEKTKQRLQGEVED 1428
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----EENLD---RKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1429 lmvdveranslaaaLDKKQRNFDKvlaeWKTKCEESQAELEAALKESRSLSTElfklkNAYEEALDQLEtvkrenKNLEQ 1508
Cdd:PRK12704 119 --------------LEQKQQELEK----KEEELEELIEEQLQELERISGLTAE-----EAKEILLEKVE------EEARH 169
|
170
....*....|....
gi 6981234 1509 EIADLTEQIAENGK 1522
Cdd:PRK12704 170 EAAVLIKEIEEEAK 183
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1304-1910 |
4.13e-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: 52.06 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1304 RSKQAFTQQIEELKRQLEEenkaknalahaLQSSRHDCDLLREQyEEEQEGKAELQralskansevaqwrtKYETDAIQR 1383
Cdd:pfam07111 56 EGSQALSQQAELISRQLQE-----------LRRLEEEVRLLRET-SLQQKMRLEAQ---------------AMELDALAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1384 TEELEEAKkklAQRLQDSEEQVEAVNakcASLEKTKQRLQGEVEDL----MVDVERANSLA-AALDKKQRNFDKVLAEWK 1458
Cdd:pfam07111 109 AEKAGQAE---AEGLRAALAGAEMVR---KNLEEGSQRELEEIQRLhqeqLSSLTQAHEEAlSSLTSKAEGLEKSLNSLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1459 TKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKnlEQEIADLTEQIAENGKsiHELEKSRKQMELEK 1538
Cdd:pfam07111 183 TKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVG--EQVPPEVHSQTWELER--QELLDTMQHLQEDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1539 ADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIrlkKK 1618
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSV---KQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1619 MEGDLNEIEIQLSHANRQAAETIKHLRSVQGQL-------KDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRA 1691
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVevermsaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1692 TLEQTERARKLAEQELLDSNERVqllhTQNTSLIHTKKKL---ETDLTQLQSEVEDASrdarnaeEKAKKAITDAAMMAE 1768
Cdd:pfam07111 416 WLETTMTRVEQAVARIPSLSNRL----SYAVRKVHTIKGLmarKVALAQLRQESCPPP-------PPAPPVDADLSLELE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1769 ELKKEQDT-SAHLERMKKNLEQTVKDLQHRlDEAEQLALKGGKKQIQKLETRIRE--------LEFELEGEQKrNTESVK 1839
Cdd:pfam07111 485 QLREERNRlDAELQLSAHLIQQEVGRAREQ-GEAERQQLSEVAQQLEQELQRAQEslasvgqqLEVARQGQQE-STEEAA 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1840 GLRKYERRVKELTYQSEEDrknvlRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEER 1910
Cdd:pfam07111 563 SLRQELTQQQEIYGQALQE-----KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
855-1086 |
4.26e-06 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 52.08 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 855 EEFQKTKDELAKSEAKR----KELEEKLVTLVQEKNDLQLQVQAESEnlldaeercdqlikaKFQLEAKIKEVTERAEDE 930
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKRehleKEVEKKLESKSGNKNKMEAKAQANSQ---------------KDEIFALINKEANRDARA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 931 EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGL-------DETIAKLTREKKALQEA 1003
Cdd:pfam18971 675 IAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSvkdlginPEWISKVENLNAALNEF 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1004 HQQTLDDL----QAEEDKVNSLSK--LKSKLEQQVDDLESSLEQEKKLrvdlernkrkleGDLKLAQESILDLEN-DKQQ 1076
Cdd:pfam18971 755 KNGKNKDFskvtQAKSDLENSVKDviINQKVTDKVDNLNQAVSVAKAM------------GDFSRVEQVLADLKNfSKEQ 822
|
250
....*....|.
gi 6981234 1077 LDERLKK-KDF 1086
Cdd:pfam18971 823 LAQQAQKnEDF 833
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1190-1922 |
4.57e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1190 VATLRKKHADSAAELAEQIDNLQRVKQKL-EKEKSEFKLEIDDLSSSVESVSKSKA--NLEKICRTLEDqLSEARGKNEE 1266
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELeELSARESDLEQDYQAASDHLNLVQTAlrQQEKIERYQED-LEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1267 TQRSLSELTTQKSRLQTEAGELSrqlEEKESIVSQLSRSKQAF-TQQIEELKRQleeenKAKNALAHAlqssRHDCDL-- 1343
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLADYQQALdVQQTRAIQYQ-----QAVQALEKA----RALCGLpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1344 ------------LREQYEEEQEGKAELQRALSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKKLAQ--RLQDSEEQ 1404
Cdd:COG3096 434 ltpenaedylaaFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1405 VEAVNAKCASLEKTKQRLQgevedlmvdveRANSLAAALDKKQ-RNFDKVLAewktkCEESQAELEAALKEsrsLSTELf 1483
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQ-----------NAERLLEEFCQRIgQQLDAAEE-----LEELLAELEAQLEE---LEEQA- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1484 klknayEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEaaleheeaKILRIQ 1563
Cdd:COG3096 574 ------AEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQ--------QLLERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1564 LELTQVKSEIDRKIAEKDEEIEQLKRNyqrtvetmQGALDAEVrsrneaIRLKKKMEGDL-NEI--EIQLSHA------- 1633
Cdd:COG3096 640 REATVERDELAARKQALESQIERLSQP--------GGAEDPRL------LALAERLGGVLlSEIydDVTLEDApyfsaly 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1634 --NRQAAeTIKHLRSVQGQLKdtqlhlddalrGQEDLKEQLAIVERRANLLQA---EVEEL------------------- 1689
Cdd:COG3096 706 gpARHAI-VVPDLSAVKEQLA-----------GLEDCPEDLYLIEGDPDSFDDsvfDAEELedavvvklsdrqwrysrfp 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1690 ------RATLEQteRARKL-AEQELLDSN--------ERVQLLHTQNTSLI--HTKKKLETD-------LTQLQSEVEDA 1745
Cdd:COG3096 774 evplfgRAAREK--RLEELrAERDELAEQyakasfdvQKLQRLHQAFSQFVggHLAVAFAPDpeaelaaLRQRRSELERE 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1746 SRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNLEQTVKDLQHRLDEAEQ----LALKGgkKQIQKLETRIR 1821
Cdd:COG3096 852 LAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQHG--KALAQLEPLVA 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1822 ELE-------------FELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNvlRLQDLVDKLQVKVKSYKRQAEEADE 1888
Cdd:COG3096 928 VLQsdpeqfeqlqadyLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLG--ENSDLNEKLRARLEQAEEARREARE 1005
|
810 820 830
....*....|....*....|....*....|....
gi 6981234 1889 QANVHLTKFRKAQHELEEAEERADIAESQVNKLR 1922
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELE 1039
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1252-1721 |
4.64e-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: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1252 TLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQ-------LSRSKQAFTQQIEELKRQLEEEN 1324
Cdd:pfam10174 314 TLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKktkqlqdLTEEKSTLAGEIRDLKDMLDVKE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1325 KAKNALA---HALQSSRHDCDL----LREQYEEEQEGK-------AELQRALSKANSEVAQWRTKYETDAIQRTEELEEA 1390
Cdd:pfam10174 394 RKINVLQkkiENLQEQLRDKDKqlagLKERVKSLQTDSsntdtalTTLEEALSEKERIIERLKEQREREDRERLEELESL 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1391 KKKlaqrLQDSEEQVEAVNAKCASLEKTKQRLQgevedlmvdvERANSLAAALDKKQRNFDKVLAEWKTKCEESQAelea 1470
Cdd:pfam10174 474 KKE----NKDLKEKVSALQPELTEKESSLIDLK----------EHASSLASSGLKKDSKLKSLEIAVEQKKEECSK---- 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1471 alkesrsLSTELFKLKNAYEEALDQLETVKREnKNLEQEIADLTEqiaengksihelEKSRKQMELEkadiqmaleeaea 1550
Cdd:pfam10174 536 -------LENQLKKAHNAEEAVRTNPEINDRI-RLLEQEVARYKE------------ESGKAQAEVE------------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1551 aleheeaKILRIQLELTQVKSEIDRKIAE---------KDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEG 1621
Cdd:pfam10174 583 -------RLLGILREVENEKNDKDKKIAElesltlrqmKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1622 DLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLdDALRgQEDLKEQLAIVERRANLLQAEVEELRATLEQTE---- 1697
Cdd:pfam10174 656 QLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHL-TNLR-AERRKQLEEILEMKQEALLAAISEKDANIALLElsss 733
|
490 500
....*....|....*....|....*....
gi 6981234 1698 RARKLAEQELLDSNERVQLLH-----TQN 1721
Cdd:pfam10174 734 KKKKTQEEVMALKREKDRLVHqlkqqTQN 762
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
854-1091 |
4.72e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.69 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 854 KEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEER--------CDQLIKAKFQLEAKIKEVTE 925
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKeiedlrrqLDTLTVERARLQLELDNLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 926 RAEDEEEINAELTAKKRKLEDECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEELAGL----DETIAKLT------- 994
Cdd:pfam00038 83 AAEDFRQKYEDELNLRTSAENDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLkknhEEEVRELQaqvsdtq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 995 -----------------------------REKKALQEAHQQTLDDLQAEEDK----VNSLSKLKSKLEQQVDDLESSLEQ 1041
Cdd:pfam00038 156 vnvemdaarkldltsalaeiraqyeeiaaKNREEAEEWYQSKLEELQQAAARngdaLRSAKEEITELRRTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1042 EKKLRVDLERNKRKLE----GDLKLAQESILDLENDKQQLDERLKKKDFEYSQL 1091
Cdd:pfam00038 236 LKKQKASLERQLAETEeryeLQLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1465-1696 |
4.84e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1465 QAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENK--NLEQEIADLTEQIAENGKSIHELeksrkQMELEKADIQ 1542
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA-----RAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1543 MALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVetmqgALDAEVRSRNEaiRLKKKMEGD 1622
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-----ALRAQIAALRA--QLQQEAQRI 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1623 LNEIEIQLSHANRQAAEtikhLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQT 1696
Cdd:COG3206 315 LASLEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1254-1448 |
5.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1254 EDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHA 1333
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1334 LQSSRHDCDLLrEQYEEEQE-----GKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAV 1408
Cdd:COG3883 95 LYRSGGSVSYL-DVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6981234 1409 NAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQR 1448
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1357-1776 |
5.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1357 ELQRALSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKC------ASLEKTKQRLQGEVED 1428
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLLPLYQelealeAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1429 LMVDVERANSLAAALDKkqrnfdkvLAEWKTKCEESQAELEAALKEsrslstELFKLKNAYEEALDQLETVKRENKNLEQ 1508
Cdd:COG4717 155 LEELRELEEELEELEAE--------LAELQEELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1509 EIADLTEQIAENGKSIHELEKSRKQMELE--------------KADIQMALEEAEAALEHEEAKILRIQLELTQVKSEID 1574
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1575 RKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQaAETIKHLRSVQGQLKDT 1654
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1655 QLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELR---------ATLEQTERARKLAEQELLDSNERVQLLHTQNTSLI 1725
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLgeleelleaLDEEELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1726 HTKKKLETD--LTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDT 1776
Cdd:COG4717 460 AELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1154-1383 |
5.27e-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: 50.92 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1154 AGGVTSTQIELNKKREAEFLKLRRDLEEAtlqhEATVATLRKKHADSAAELAE---QIDNLQRVKQKLEKEKSEFKLEID 1230
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAAlerRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1231 DLSSSVESVSkskANLEKICRTLEDQLSEA--RGKN------------EETQRSLSELTTQKSRLQTEAGELSRQLEEKE 1296
Cdd:COG4942 87 ELEKEIAELR---AELEAQKEELAELLRALyrLGRQpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1297 SIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKY 1376
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
....*..
gi 6981234 1377 ETDAIQR 1383
Cdd:COG4942 244 PAAGFAA 250
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
844-1113 |
8.88e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 924 TERAE-------DEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAkltrE 996
Cdd:pfam07888 156 KERAKkagaqrkEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----E 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 997 KKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQE------------------KKLRVDLERNKRKLEG 1058
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQArlqaaqltlqladaslalREGRARWAQERETLQQ 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 1059 DLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSL-QLQKKIKELQ 1113
Cdd:pfam07888 312 SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRvQLSESRRELQ 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1754-1927 |
1.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1754 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLalkggkKQIQKLETRIRELEFELEGEQKR 1833
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1834 ntesVKGLRKYERRVKELTYQSEEDRKNVLRLQ-DLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERAD 1912
Cdd:COG4717 148 ----LEELEERLEELRELEEELEELEAELAELQeELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*
gi 6981234 1913 IAESQVNKLRAKTRD 1927
Cdd:COG4717 224 ELEEELEQLENELEA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1382-1586 |
1.64e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1382 QRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANslaAALDKKQRNFDKVLAEWKTkc 1461
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERARALYR-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1462 EESQAELEAALKESRSLS---TELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEK 1538
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6981234 1539 ADIQMALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQ 1586
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
853-1331 |
1.65e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 853 MKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEE---RCDQLIKAKFQLEAKIKEVTERAED 929
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 930 EEEINAELTA--------------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIakltr 995
Cdd:PRK01156 268 ELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI----- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 996 EKKALQEAHQQTLDDLQAEEDK----VNSLSKLKSKLE--------------------------------------QQVD 1033
Cdd:PRK01156 343 KKKSRYDDLNNQILELEGYEMDynsyLKSIESLKKKIEeyskniermsafiseilkiqeidpdaikkelneinvklQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1034 DLESSLEQEKKL----RVDLERNKRKLEGDLK-------LAQESILDL----ENDKQQLDERLKKKDFEYSQLQSKVEDE 1098
Cdd:PRK01156 423 SKVSSLNQRIRAlrenLDELSRNMEMLNGQSVcpvcgttLGEEKSNHIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1099 QTLSLQLQ-KKIKELQARIEELEEEieaeratRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKL-- 1175
Cdd:PRK01156 503 KKRKEYLEsEEINKSINEYNKIESA-------RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNAla 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1176 -RRDLEEATLQHEATvaTLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLE 1254
Cdd:PRK01156 576 vISLIDIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1255 DQLSEARGKnEETQRSLSELTTQKSRLQTEAGELSRQLE-------EKESIVSQLSRSKQAFTQQIEELKRQLEEENKAK 1327
Cdd:PRK01156 654 NYKKQIAEI-DSIIPDLKEITSRINDIEDNLKKSRKALDdakanraRLESTIEILRTRINELSDRINDINETLESMKKIK 732
|
....
gi 6981234 1328 NALA 1331
Cdd:PRK01156 733 KAIG 736
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1219-1376 |
1.85e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1219 EKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESI 1298
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1299 VSQLSRSKQAFTQQIEELKRQLeeenkakNALAHALQSSrhdcdllrEQYEEEQEGKAE-----LQRALSKANSEVAQWR 1373
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQL-------AALEAALDAS--------EKRDRESQAKIAdlgrrLNVALAQRVQELNRYR 196
|
...
gi 6981234 1374 TKY 1376
Cdd:PRK09039 197 SEF 199
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1084 |
1.93e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 862 DELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTER----AEDEEEINAEL 937
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 938 TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTlddlqaeEDK 1017
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL-------EAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 1018 VNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKK 1084
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1398-1639 |
2.52e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1398 LQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELE---AALKE 1474
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraRALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1475 SRSLSTELFKLKNA--YEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKAdiqmaleeaeaal 1552
Cdd:COG3883 98 SGGSVSYLDVLLGSesFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1553 eheeakilriqlELTQVKSEIDRKIAEKDEEIEQLKRNyQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSH 1632
Cdd:COG3883 165 ------------ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*..
gi 6981234 1633 ANRQAAE 1639
Cdd:COG3883 232 AAAAAAA 238
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
884-1532 |
2.62e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 884 EKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELtakkRKLEDECSELKKDIDDLELTLA 963
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 964 KVEKEKHATENKVKNLTEELAGLDEtiakltrekkalqeahqqTLDDLQAEEDKVNslsKLKSKLEQQVDDLESSLEQEK 1043
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKS------------------ALNELSSLEDMKN---RYESEIKTAESDLSMELEKNN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1044 KLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDerlkkkdfEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEeei 1123
Cdd:PRK01156 274 YYKELEERHMKIINDPVYKNRNYINDYFKYKNDIE--------NKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI--- 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1124 eaeratraKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATlqheatvATLRKKHADsAAE 1203
Cdd:PRK01156 343 --------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS-------EILKIQEID-PDA 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1204 LAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLE--KICRTLEDQLSEargknEETQRSLSELTTQKSRL 1281
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqSVCPVCGTTLGE-----EKSNHIINHYNEKKSRL 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1282 QTEAGELSRQLEEKESIVSQLSRSKQAFTQqiEELKRQLEEENKAKNAlAHALQSSRHDCDLLREQYEEEQEGKAELQRA 1361
Cdd:PRK01156 482 EEKIREIEIEVKDIDEKIVDLKKRKEYLES--EEINKSINEYNKIESA-RADLEDIKIKINELKDKHDKYEEIKNRYKSL 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1362 -LSKANSEVAQW------RTKYETDAIQ-RTEELEEAKKKLAQRLQDSEEQVEAVNakcASLEKTKQRLQGEVEDLMVDV 1433
Cdd:PRK01156 559 kLEDLDSKRTSWlnalavISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKY 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1434 ERANSLAAALDK---KQRNFDKVLAEWKTKcEESQAELEAALKESrslSTELFKLKNAYEEALDQLETVKRENKNLEQEI 1510
Cdd:PRK01156 636 NEIQENKILIEKlrgKIDNYKKQIAEIDSI-IPDLKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
650 660
....*....|....*....|..
gi 6981234 1511 ADLTEQIAENGKSIHELEKSRK 1532
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKK 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1610-1940 |
2.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1610 NEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDA---LRGQEDLKEQLAIVERRANLLQAEV 1686
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1687 EELRATLEQTERARKLAEQELLDSNERVQLLH------TQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAI 1760
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1761 TDAAMMAEELKKEQDTSAHLERMKKNLEqTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEfelegeqKRNTESVKG 1840
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE-------KAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1841 LRKYERRVKELTYQSEEDRKNVLRLQdlvdKLQVKVKSYKRQAEEAD-----EQANVHLTKFRKAQHELEEAEERADIAE 1915
Cdd:PRK03918 407 ISKITARIGELKKEIKELKKAIEELK----KAKGKCPVCGRELTEEHrkellEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340
....*....|....*....|....*
gi 6981234 1916 SQVNKLRAKTRDFTSSRMVVHESEE 1940
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKE 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1565-1809 |
3.06e-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: 48.61 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1565 ELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQgALDAEVRSRNEAIRlkkKMEGDLNEIEIQLSHANRQAAETIKHL 1644
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1645 RSVQGQLKDtQLHLDDALRGQEDLK-----EQLAIVERRANLLQAEVEELRATLEQTERARklaeqelldsnervQLLHT 1719
Cdd:COG4942 100 EAQKEELAE-LLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADL--------------AELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1720 QNTSLIHTKKKLETDLTQLQSEvedasRDARNAEEKAKKAItdAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLD 1799
Cdd:COG4942 165 LRAELEAERAELEALLAELEEE-----RAALEALKAERQKL--LARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
250
....*....|
gi 6981234 1800 EAEQLALKGG 1809
Cdd:COG4942 238 AAAERTPAAG 247
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
890-1513 |
3.08e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.07 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 890 LQVQAESENLLDAEERCDQLIKAkfqleakIKEVTERAEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEK 969
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFG-------YKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 970 HATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKL----KSKLEQQVDDLESSLEQEkkL 1045
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKAltgkHQDVTAKYNRRRSKIKEQ--N 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1046 RVDLERNKRKL----EGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDE-QTLSLQLQKKI--KELQARIEE 1118
Cdd:pfam12128 389 NRDIAGIKDKLakirEARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRlGELKLRLNQATatPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1119 LEEEIEAERATRAKTEKQRSDYAreleelsERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVAT----LR 1194
Cdd:pfam12128 469 FDERIERAREEQEAANAEVERLQ-------SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTllhfLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1195 KKHADSAAELAEQIDNLQRVKQKLEKEKSEF----------------KLEIDDLSSSVESVSKSKANLEKICRT------ 1252
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRIDVPEWAASEEELRERLDKAEEALQSarekqa 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1253 -LEDQLSEARGKNEETQRslsELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKA-KNAL 1330
Cdd:pfam12128 622 aAEEQLVQANGELEKASR---EETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQlDKKH 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1331 AHALQSSRHDCDLLR---EQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQ---------------RTEELEEAKK 1392
Cdd:pfam12128 699 QAWLEEQKEQKREARtekQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALEtwykrdlaslgvdpdVIAKLKREIR 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1393 KLAQRLQDSEEQVEAV------------------NAKCASLEKTKQRLQGEVEDLMVDVERANS--------------LA 1440
Cdd:pfam12128 779 TLERKIERIAVRRQEVlryfdwyqetwlqrrprlATQLSNIERAISELQQQLARLIADTKLRRAklemerkasekqqvRL 858
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1441 AALDKKQRNFDKVLAEWKTKCEESQAELEAAlkeSRSLSTELFKLKNAYEEaldqlETVKRENKNLEQEIADL 1513
Cdd:pfam12128 859 SENLRGLRCEMSKLATLKEDANSEQAQGSIG---ERLAQLEDLKLKRDYLS-----ESVKKYVEHFKNVIADH 923
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1728-1927 |
3.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1728 KKKLETDLTQLQSEVEDASRdARNAEEKAKKAI---TDAAMMAEELKKEQDTSAHLERMKKNL-----EQTVKDLQHRLD 1799
Cdd:COG4913 220 EPDTFEAADALVEHFDDLER-AHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1800 EAEQlALKGGKKQIQKLETRIRELEFELEG-EQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKS 1878
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6981234 1879 YKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRD 1927
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
862-1067 |
3.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 862 DELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIkevteraedeEEINAELTAKK 941
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI----------AEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 942 RKLEDECSELKK---DIDDLELTLAkvekekhatenkVKNLTEELAGLD--ETIAKLTREKKALQEAHQQTLDDLQAE-E 1015
Cdd:COG3883 86 EELGERARALYRsggSVSYLDVLLG------------SESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAElE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1016 DKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESI 1067
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1438-1652 |
4.15e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1438 SLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQI 1517
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1518 AENGKSIHELEKSRKQM--ELEKADIQ-MALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRT 1594
Cdd:COG4942 93 AELRAELEAQKEELAELlrALYRLGRQpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 1595 VETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLK 1652
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1620-1940 |
4.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1620 EGDLNEIEIQLSHANR-QAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTER 1698
Cdd:PTZ00121 1044 EKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1699 ARKLAEQELLDSNERVQLLHtqntsliHTKKKLETDLTQLQSEVEDASR--DARNAE-----EKAKKAI----------- 1760
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAE-------EARKAEDAKRVEIARKAEDARKaeEARKAEdakkaEAARKAEevrkaeelrka 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1761 -----TDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLE----TRIRELEFELEGEQ 1831
Cdd:PTZ00121 1197 edarkAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEearmAHFARRQAAIKAEE 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1832 KRNTESVKG---------LRKYE--RRVKELTYQSEEDRKnVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKA 1900
Cdd:PTZ00121 1277 ARKADELKKaeekkkadeAKKAEekKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 6981234 1901 QHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE 1940
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
1415-1600 |
4.59e-05 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 48.02 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1415 LEKTKQRLQGEVEDLMVDVE-RANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTElfklknAYEEAL 1493
Cdd:COG4487 24 VKQRRAEFEKELAERLADAAkREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKKALAVAE------EKEKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1494 DQLETVKRENknlEQEIADLTEQIAENGKSIHELEKSRKQMELEKAdiQMALEEAEAALEHEEAKILRIQLELTQVK-SE 1572
Cdd:COG4487 98 AALQEALAEK---DAKLAELQAKELELLKKERELEDAKREAELTVE--KERDEELDELKEKLKKEEEEKQLAEKSLKvAE 172
|
170 180
....*....|....*....|....*...
gi 6981234 1573 IDRKIAEKDEEIEQLKRNYQRTVETMQG 1600
Cdd:COG4487 173 YEKQLKDMQEQIEELKRKKEQGSTQLQG 200
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1003 |
5.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 845 ETEKEMATMKEEFQKTKDELAKSEAK----RKELEEKLVTLVQEKNDLQLQVQAESENLLDA--------------EERC 906
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkylaparREQA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 907 DQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEdecselkKDIDDLELTLAKVEKEKHATENKVKNLTEELAGL 986
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
170
....*....|....*..
gi 6981234 987 DETIAKLTREKKALQEA 1003
Cdd:COG4942 226 EALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1161-1425 |
6.88e-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: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1161 QIELNKKREAEFLKLRRDLEEATLQHEATV---ATLRKKHADSAAELAEQIDNLQRVKQKLEKEK---SEFKLEIDDLSS 1234
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMdrqAAIYAEQERMAMERERELERIRQEERKRELERirqEEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1235 SVESVSKSKANLEKICRTLEdQLSEARGKNEETQRSLSELTTQKSRLQTEAG-----ELSRQLEEKESIVSQLSRSKQAF 1309
Cdd:pfam17380 380 LERLQMERQQKNERVRQELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQEearqrEVRRLEEERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1310 TQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE-----------LQRALSKANSEVAQWRTKYET 1378
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREA 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 6981234 1379 DAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGE 1425
Cdd:pfam17380 539 EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1265-1511 |
7.93e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1265 EETQRSLSELTTQKSrLQTEAGELSRQLEEKESIVSQLSRSKQ---AFTQQIEELKRQLEEENKAKNALAHALQSSRHD- 1340
Cdd:PRK11281 39 ADVQAQLDALNKQKL-LEAEDKLVQQDLEQTLALLDKIDRQKEeteQLKQQLAQAPAKLRQAQAELEALKDDNDEETREt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1341 -----CDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKL-AQRLQDSEEQVEAV 1408
Cdd:PRK11281 118 lstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKGGkVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1409 NAKCASLE-KTKQR---LQGevedlmvdveraNSLAAALDKKQRNFdkvLAEWKTKCEESQAELEAALKESRSLSTElfk 1484
Cdd:PRK11281 198 QAEQALLNaQNDLQrksLEG------------NTQLQDLLQKQRDY---LTARIQRLEHQLQLLQEAINSKRLTLSE--- 259
|
250 260
....*....|....*....|....*...
gi 6981234 1485 lkNAYEEALDQLETVK-RENKNLEQEIA 1511
Cdd:PRK11281 260 --KTVQEAQSQDEAARiQANPLVAQELE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1306-1523 |
7.99e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1306 KQAFTQQIEELKRQLEEENKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdaiqRTE 1385
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAE-----------AEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1386 ELEEAKKKLAQRLQDSEEQVEAVNA---------------KCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNF 1450
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1451 DKVLAEwktkCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKS 1523
Cdd:COG3883 160 EALKAE----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
890-1053 |
9.15e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 890 LQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEI---NAELTAKKRKLEDECSELKKDIDDLELTLAKVE 966
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 967 KEKHATENKVKNLTEELAGLDETIAKltrEKKALQEAHQqtlddLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLR 1046
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEE---QLQELERISG-----LTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEE 185
|
....*..
gi 6981234 1047 VDLERNK 1053
Cdd:PRK12704 186 ADKKAKE 192
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1220 |
1.09e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESE---NLLDAEERCDQLIKAkfQLEAKIKEV 923
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipNLQNITVRLQDLTEK--LSEAEDMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 924 TERAEDEEEINAELtakkrkledecselkkDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKL-TREKKALQE 1002
Cdd:TIGR00618 612 CEQHALLRKLQPEQ----------------DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsIRVLPKELL 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1003 AHQQTLddLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLER-------NKRKLEGDLKLAQESILDLEndkQ 1075
Cdd:TIGR00618 676 ASRQLA--LQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELM---H 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1076 QLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYareleelserleeaG 1155
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD--------------E 816
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1156 GVTSTQIELNKKREAEFLKLRRdlEEATLQHEatVATLRKKHADSAAELAEQIDNLQRVKQKLEK 1220
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLE--EKSATLGE--ITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1669-1930 |
1.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1669 KEQLAIVE--RRANLLQAEVEELRATLEQ-------TERaRKLAEQELLDSNE---RVQLLHtqntslihtkKKLETDLT 1736
Cdd:TIGR02168 135 KRSYSIIEqgKISEIIEAKPEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDIL----------NELERQLK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1737 QLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNLEQTVKDLQHRLDEAEQlalkggkkQIQKL 1816
Cdd:TIGR02168 204 SLERQAEKAERYKELKAELRELELALLVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1817 ETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTK 1896
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
250 260 270
....*....|....*....|....*....|....
gi 6981234 1897 FRKAQHELEEAEERADIAESQVNKLRAKTRDFTS 1930
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1263-1539 |
1.22e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1263 KNEETQRSLSELTTQKSRLQTEAGELSRQLEE--KESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSsrhd 1340
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1341 cdlLREQYEEEQEGKAELQralskANSEVAQWRTKYEtdaiqrteELEEAKKKLAQRLQDSEEQVEAVNAKcasLEKTKQ 1420
Cdd:COG3206 245 ---LRAQLGSGPDALPELL-----QSPVIQQLRAQLA--------ELEAELAELSARYTPNHPDVIALRAQ---IAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1421 RLQGEVEDLMVDVEranslaaaldkkqrnfdkvlaewktkceesqAELEAALKESRSLSTELfklkNAYEEALDQLetvk 1500
Cdd:COG3206 306 QLQQEAQRILASLE-------------------------------AELEALQAREASLQAQL----AQLEARLAEL---- 346
|
250 260 270
....*....|....*....|....*....|....*....
gi 6981234 1501 renKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKA 1539
Cdd:COG3206 347 ---PELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
844-976 |
1.37e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQ--EKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIK 921
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAriKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6981234 922 EVTERAEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 976
Cdd:COG1579 114 ELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
868-1210 |
1.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 868 EAKRKELEEKLVTLVQEKNDLQLQVQAeSENLLDAEERCDQL----IKAKfQLEAKIKEVTERAEDEEEINAELtakkRK 943
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYswdeIDVA-SAEREIAELEAELERLDASSDDL----AA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 944 LEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHqqtLDDLQAEEDKVNSLSK 1023
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVERE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1024 LKSKLEQQVDDLESSLEQ-EKKLRVDLERNKRKLEGDLKLAQESILDLEnDKQQLDERLK-------KKDFEYSQLQSKV 1095
Cdd:COG4913 767 LRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-EYLALLDRLEedglpeyEERFKELLNENSI 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1096 EDEQTLSLQLQKKIKELQARIEeleeeieaeratRAKTEKQRSDYareleelserleeaGGVTSTQIELNKKREAEFLKL 1175
Cdd:COG4913 846 EFVADLLSKLRRAIREIKERID------------PLNDSLKRIPF--------------GPGRYLRLEARPRPDPEVREF 899
|
330 340 350
....*....|....*....|....*....|....*
gi 6981234 1176 RRDLEEATLQHEATVATLRKKHADSAAELAEQIDN 1210
Cdd:COG4913 900 RQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
766-1111 |
1.67e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.86 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 766 FKAGLLGTLEEMR---------DERLAKLITRTQavcrgflmRVEFQKMMQRRESIFCIQYNIRAFMNVKHWPWMKLFF- 835
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 836 ---KIKPLLKSAETEKEMATMKE---EFQKTKDELAKseaKRKELEEKLvtlvqeknDLQLQVQAESENLLDAEERCDQL 909
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEGLKEtlkALQVSKYSLQK---KVSEMEQKL--------QLHLLAKEDHHKQLNEIEKYYAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 910 IKAKFQLEAKIKEVTERAEDEE-EINAELTAKKRKLEDECSELKKDIDDL--ELTLAKVEKEKHATENKVkNLTEELAGL 986
Cdd:pfam15818 146 ITGQFGLVKENHGKLEQNVQEAiQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTCQYKMGEENI-NLTIKEQKF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 987 DETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVD---DLESSLEQEKKLRVDLERNKRKLEGDLKLA 1063
Cdd:pfam15818 225 QELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQantEMEAELKALKENNQTLERDNELQREKVKEN 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6981234 1064 QESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKE 1111
Cdd:pfam15818 305 EEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1187-1429 |
1.73e-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: 46.87 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1187 EATVATLRKKHADSAAELAEQIDNLQRVKQKLEkeksEFKLEIDDLSSSVESVSKSKANlekicrTLEDQLSEARGKNEE 1266
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKLLPQANLLADE------TLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1267 TQRSLSELTTQKSRLqteagelsRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRH------- 1339
Cdd:COG3096 905 AQEAQAFIQQHGKAL--------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedav 976
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1340 -----DCDL---LREQYEEEQEGKAELQRALSKANSEVAQW-----------RTKYET--DAIQRTEELE-----EAKKK 1393
Cdd:COG3096 977 gllgeNSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEELGvqadaEAEER 1056
|
250 260 270
....*....|....*....|....*....|....*.
gi 6981234 1394 LAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDL 1429
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1161-1367 |
1.88e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1161 QIELNKKREAEFLKLRRDLEEATLQHEATVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVS 1240
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1241 KS----KANLEKICRTLE--DQLSEARGKN-EETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQI 1313
Cdd:COG4942 122 LAlllsPEDFLDAVRRLQylKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1314 EELKRQLeeenKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANS 1367
Cdd:COG4942 202 ARLEKEL----AELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
848-1112 |
1.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENL------LDAEERCDQLIKAKFQLEAKIK 921
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvqtaLRQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 922 EVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKEKH 970
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 971 ATENKVKNLTEELAGLDETI----AKLTREKKALQ------------EAHQQTLDDL-QAEEDKVnsLSKLKSKLEQQVD 1033
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKLsvaqAAHSQFEQAYQlvrkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMRLS 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6981234 1034 DLESSLEQEKklrvDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKEL 1112
Cdd:PRK04863 524 ELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1063-1297 |
1.96e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1063 AQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRsdyAR 1142
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1143 ELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEAtlqheatvATLRKKHADSAAELAEQIDNLQRVKQKLEKEK 1222
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA--------VRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1223 SEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKES 1297
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1187-1429 |
2.29e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1187 EATVATLRKKHADSAAELAEQIDNLQRVKQKLEKekseFKLEIDDLSSSVESVSKSKAN-LEKICRTLEDQLSEArgknE 1265
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQ----AKEGLSALNRLLPRLNLLADEtLADRVEEIREQLDEA----E 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1266 ETQRS-------LSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQ---AFTQQI--------EELKRQLEEENKAK 1327
Cdd:PRK04863 908 EAKRFvqqhgnaLAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVqrrahfsyEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1328 NALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEvaqWRTKYET--DAIQRTEEL-----EEAKKKLAQRLQD 1400
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDE 1064
|
250 260
....*....|....*....|....*....
gi 6981234 1401 SEEQVEAVNAKCASLEKTKQRLQGEVEDL 1429
Cdd:PRK04863 1065 LHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1274-1528 |
2.63e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.30 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1274 LTTQKSRLQTEAgelsRQLEEKESivSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQE 1353
Cdd:pfam00038 23 LEQQNKLLETKI----SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1354 GKAELQ---RALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQ 1423
Cdd:pfam00038 97 LRTSAEndlVGLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1424 GEVEDLMvdveranslaaaldkkQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKREN 1503
Cdd:pfam00038 177 AQYEEIA----------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260
....*....|....*....|....*....
gi 6981234 1504 KNLEQEIADLTE----QIAENGKSIHELE 1528
Cdd:pfam00038 241 ASLERQLAETEEryelQLADYQELISELE 269
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1644-1933 |
3.01e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1644 LRSVQGQLKDTQ---LHLDDA-LRGQEDLKEQLAivERRAnlLQAEVEELRATLEQTERARKLAEQElldsNERVQLLHT 1719
Cdd:PLN02939 130 LEDLVGMIQNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQE----KIHVEILEE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1720 QntsLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNLEQTVKDLQH 1796
Cdd:PLN02939 202 Q---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELES 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1797 RLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKGLRKY---ERRVKELTYQSEEdrKNVLRLQ-DLVDKL 1872
Cdd:PLN02939 279 KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELL 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1873 QVKVKSYKRQAEEADEQANVHLTKFrkaQHELEEAEeraDIAESQVNKLRAKTRDFTSSRM 1933
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHSYIQLY---QESIKEFQ---DTLSKLKEESKKRSLEHPADDM 411
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1456-1709 |
3.25e-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: 45.88 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1456 EWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALD--QLETVKRENKNLEQEiadlteQIAENGKSIHELEksRKQ 1533
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELEriRQEERKRELERIRQE------EIAMEISRMRELE--RLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1534 MELEkadiQMALEEAEAALEHEEAKILriqleltqvKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAI 1613
Cdd:pfam17380 385 MERQ----QKNERVRQELEAARKVKIL---------EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1614 RLKkkmegdlnEIEIQlshanrqaaETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQlaiverRANLLQAEVEELRATL 1693
Cdd:pfam17380 452 RLE--------EQERQ---------QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAM 508
|
250
....*....|....*.
gi 6981234 1694 EQTERARKLAEQELLD 1709
Cdd:pfam17380 509 IEEERKRKLLEKEMEE 524
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1246-1885 |
3.98e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1246 LEKicrtLEDQLSEARGKNEETQRSLSE----LTTQKSRLQTEAGELSRQLE---EKESIVSQLSRSKQAFTQQIEELkr 1318
Cdd:PRK10246 200 LEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSLNwltRLDELQQEASRRQQALQQALAAE-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1319 qlEEENKAKNALAHALQSSRhdcdlLREQYEEEQEGKAELQRALSKANS------EVAQWRTKYETDAIQRTEELEEAKK 1392
Cdd:PRK10246 274 --EKAQPQLAALSLAQPARQ-----LRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAELQAQQQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1393 KLAQRLQDSE------EQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALdkkqrnfdkvlaewKTKCEESQA 1466
Cdd:PRK10246 347 SLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAIT--------------LTLTADEVA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1467 ELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE-------------NGKSIHELEKSRKQ 1533
Cdd:PRK10246 413 AALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqlaDVKTICEQEARIKD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1534 MELEKADIQ--------------MALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRN---YQRTVE 1596
Cdd:PRK10246 493 LEAQRAQLQagqpcplcgstshpAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDeseAQSLRQ 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1597 TMQgALDAEVRSRNEAIRLKKKMEGDLN-------EIEIQLSHANR------QAAETIKHLRSVQGQLKDTQLHLDDALR 1663
Cdd:PRK10246 573 EEQ-ALTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLLSQrhelqgQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1664 G-------QEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKL-----AEQELLDSNERVQL-----LHTQNTSLIH 1726
Cdd:PRK10246 652 GyaltlpqEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLletlpQSDDLPHSEETVALdnwrqVHEQCLSLHS 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1727 TKKKLETDLTQLQSEVEDASRD---ARNAEEKAKKAITDAAMMAEElkkeqdTSAHLERMKKNLEQtvkdlqhRLDEAEQ 1803
Cdd:PRK10246 732 QLQTLQQQDVLEAQRLQKAQAQfdtALQASVFDDQQAFLAALLDEE------TLTQLEQLKQNLEN-------QRQQAQT 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1804 LALKGGKKQIQKLETRIRELEFELEGE--QKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDklqvKVKSYKR 1881
Cdd:PRK10246 799 LVTQTAQALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQ----QIAQATQ 874
|
....
gi 6981234 1882 QAEE 1885
Cdd:PRK10246 875 QVED 878
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1174-1369 |
4.05e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1174 KLRRDLEEAtlqhEATVATLRKKH-----ADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEK 1248
Cdd:COG3206 186 ELRKELEEA----EAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1249 --ICRTLEDQLSEARGKNEETQRSLSE-------LTTQKSRLQTE-AGELSRQLEEKESIVSQLSRSKQAFTQQIEELKR 1318
Cdd:COG3206 262 spVIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1319 QLEEENKAKNALAhALQssrHDCDLLREQYEE--EQEGKAELQRALSKANSEV 1369
Cdd:COG3206 342 RLAELPELEAELR-RLE---REVEVARELYESllQRLEEARLAEALTVGNVRV 390
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1177-1926 |
4.09e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1177 RDLEEATLQHEATVATLRKKHADSAAElAEQIdnlqrVKQKLEKEKSefkleiddlsssvESVSKSKANLEKICRTLEDQ 1256
Cdd:NF041483 316 RLVGEATKEAEALKAEAEQALADARAE-AEKL-----VAEAAEKART-------------VAAEDTAAQLAKAARTAEEV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1257 LSEA--------RGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKqafTQQIEELKRQLEEENKAKN 1328
Cdd:NF041483 377 LTKAsedakattRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAK---TVELQEEARRLRGEAEQLR 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1329 ALAHAlQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQ-RTEELEEA---KKKLAQRLQDSEEQ 1404
Cdd:NF041483 454 AEAVA-EGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERvRTEAIERAttlRRQAEETLERTRAE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1405 VEAVNAKCASL-EKTKQRLQGEVEDLMVDVERanslaaALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELF 1483
Cdd:NF041483 533 AERLRAEAEEQaEEVRAAAERAARELREETER------AIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIR 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1484 KlknayeEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAAL---EHEEAKIL 1560
Cdd:NF041483 607 R------EAAEETERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRLRSEAAAEAErlkSEAQESAD 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1561 RIQLELT----QVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAE-VRSRNEAIRL----KKKMEGDLNEIEIQLS 1631
Cdd:NF041483 681 RVRAEAAaaaeRVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQErERAREQSEELlasaRKRVEEAQAEAQRLVE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1632 HANRQAAETI----KHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAivERRANLLQAEVEELRA---------------- 1691
Cdd:NF041483 761 EADRRATELVsaaeQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAA--ERTRTEAQEEADRVRSdayaererasedanrl 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1692 ---TLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLtqLQSEVEDASRDARNAEEKAKKAITDAAMMAE 1768
Cdd:NF041483 839 rreAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDT--LASAEQDAARTRADAREDANRIRSDAAAQAD 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1769 ELKKEQDTSAHLERmkknlEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESVKG-------L 1841
Cdd:NF041483 917 RLIGEATSEAERLT-----AEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSaqqhaerI 991
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1842 RKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEAdEQANVHLTKFRKAQHEL-----EEAEERADIAES 1916
Cdd:NF041483 992 RTEAERVKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAA-EQADTLITEAAAEADQLtakaqEEALRTTTEAEA 1070
|
810
....*....|
gi 6981234 1917 QVNKLRAKTR 1926
Cdd:NF041483 1071 QADTMVGAAR 1080
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
847-1051 |
4.25e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDEL-AKSEAKRKELEE----KLVTLVQEKNDLQLQVQAESENLldaEERCDQLIKAK-------F 914
Cdd:pfam12128 695 DKKHQAWLEEQKEQKREArTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKAL---ETWYKRDLASLgvdpdviA 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 915 QLEAKIKEVTERAEDEEEINAE------------------LTAKKRKLEDECSELKKD----IDDLELTLAKVEKEKHAT 972
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQQQlarlIADTKLRRAKLEMERKAS 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 973 ENKVKNLTEELAGLDETIAKLTREKKAlqeahqQTLDDLQAEEDKVNS-LSKLKSKLEQQVDDLESSLEQEKKLRVDLER 1051
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKLATLKED------ANSEQAQGSIGERLAqLEDLKLKRDYLSESVKKYVEHFKNVIADHSG 925
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1197-1417 |
4.48e-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: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1197 HADS-AAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESvskskanlekicrtLEDQLSEARGKNEETQRSLSELT 1275
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE--------------LQAELEALQAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1276 TQKSRLQTEAGELSRQLEEKESIVSQL-----SRSKQAFTQQIEELKR-------QLEEENKAKNALAHALQSSRHDCDL 1343
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLdvllgSESFSDFLDRLSALSKiadadadLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1344 LREQYEEEQEGKAELQRALSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEK 1417
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1565-1778 |
4.56e-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: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1565 ELTQVKSEIDRKIAEKDEEIEQLKRNYQRtvetmqgaLDAEVRSRNEAIrlkKKMEGDLNEIEIQLSHANRQAAETIKHL 1644
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNE--------LQAELEALQAEI---DKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1645 rsvqgQLKDTQLHLDDALRGQEDLKEQLaiveRRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSL 1724
Cdd:COG3883 96 -----YRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1725 IHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSA 1778
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1414-1932 |
4.90e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1414 SLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQ---RNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYE 1490
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNlelENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1491 EALDQLETVKRENKNLEQEIADLTEQIAENGKsIHELEKSRKQMELEKA---------------DIQMALE--EAEAALE 1553
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNY-YKELEERHMKIINDPVyknrnyindyfkyknDIENKKQilSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1554 HEEAKILRIQLELTQVKSEIDRKIAEKDE------EIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIE 1627
Cdd:PRK01156 322 NKYHAIIKKLSVLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1628 IQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRAnllQAEVEELRATLEQTERARKLAEQEL 1707
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQS---VCPVCGTTLGEEKSNHIINHYNEKK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1708 LDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELK---------KEQDTSA 1778
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdkhdkyeeiKNRYKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1779 HLERMKKNLEQTVKDLQHRLD---EAEQLALKGGKKQIQKLETRIRELEFELEGEQKRNTESvkgLRKYERRVKELTYQS 1855
Cdd:PRK01156 559 KLEDLDSKRTSWLNALAVISLidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS---IREIENEANNLNNKY 635
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6981234 1856 EEDRKNvlrlQDLVDKLQVKVKSYKRQAEEADEQanvhltkfrkaQHELEEAEERADIAESQVNKLRAKTRDFTSSR 1932
Cdd:PRK01156 636 NEIQEN----KILIEKLRGKIDNYKKQIAEIDSI-----------IPDLKEITSRINDIEDNLKKSRKALDDAKANR 697
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1175-1921 |
4.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1175 LRRDLEEATlqheatvaTLRKKHADSAAELAEQIDNLQRVKQKLEK-EKSEFKLEID--DLSSSVESVSKSKANLEKICR 1251
Cdd:PRK04863 281 RRVHLEEAL--------ELRRELYTSRRQLAAEQYRLVEMARELAElNEAESDLEQDyqAASDHLNLVQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1252 TLEDqLSEARGKNEETQRSLSELTTQKSRLQTEAGELSrqlEEKESIVSQLSRSKQAFtqqiEELKRQLEEENKAKNALA 1331
Cdd:PRK04863 353 YQAD-LEELEERLEEQNEVVEEADEQQEENEARAEAAE---EEVDELKSQLADYQQAL----DVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1332 HAlqssRHDCDL--------------LREQYEEEQEGKAELQRALSKANSEVAQWRTKYE-----TDAIQRTEELEEAKK 1392
Cdd:PRK04863 425 RA----KQLCGLpdltadnaedwleeFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiAGEVSRSEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1393 KLA----QRLQDseEQVEAVNAKCASLEktkQRLQgevedlmvdveranslaaaldkKQRNFDKVLAEWKTKC---EESQ 1465
Cdd:PRK04863 501 LLRrlreQRHLA--EQLQQLRMRLSELE---QRLR----------------------QQQRAERLLAEFCKRLgknLDDE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1466 AELEAALKEsrsLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMAL 1545
Cdd:PRK04863 554 DELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVT 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1546 EEAEAAleheeakiLRIQLELTQVKSEIDRKIAEKDEEIEQLKR-------NYQRTVETMQGALDAE------------- 1605
Cdd:PRK04863 631 EYMQQL--------LERERELTVERDELAARKQALDEEIERLSQpggsedpRLNALAERFGGVLLSEiyddvsledapyf 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1606 ------------VRSRNEAIRLKKKME---GDLNEIE--IQLSHANRQAAETIKHLRSVQgqLKDTQLH---------LD 1659
Cdd:PRK04863 703 salygparhaivVPDLSDAAEQLAGLEdcpEDLYLIEgdPDSFDDSVFSVEELEKAVVVK--IADRQWRysrfpevplFG 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1660 DALRGQ--EDLKEQLAIVERRANLLQAEVEELRATLEQTER--ARKLA-------EQELLDSNERVQllhtqntslihtk 1728
Cdd:PRK04863 781 RAAREKriEQLRAEREELAERYATLSFDVQKLQRLHQAFSRfiGSHLAvafeadpEAELRQLNRRRV------------- 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1729 kKLETDLTQLQSEVedasRDARNAEEKAKKAITDAAMMAEELKKEQDTSahlermkknLEQTVKDLQHRLDEAEQLA--L 1806
Cdd:PRK04863 848 -ELERALADHESQE----QQQRSQLEQAKEGLSALNRLLPRLNLLADET---------LADRVEEIREQLDEAEEAKrfV 913
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1807 KGGKKQIQKLETR---IRELEFELEGEQKRNTESVKGLRKYERRVKELTYQ-------SEEDRKNVL-RLQDLVDKLQVK 1875
Cdd:PRK04863 914 QQHGNALAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVvqrrahfSYEDAAEMLaKNSDLNEKLRQR 993
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 6981234 1876 VKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKL 1921
Cdd:PRK04863 994 LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
926-1051 |
5.17e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 926 RAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETI-AKLTREKKALQEAH 1004
Cdd:cd22656 101 DDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIARKE 180
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1005 qqtLDDLQAEEDKVNS--LSKLKSKLE---QQVDDLESSLEQEKKLRVDLER 1051
Cdd:cd22656 181 ---IKDLQKELEKLNEeyAAKLKAKIDelkALIADDEAKLAAALRLIADLTA 229
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1395-1748 |
5.34e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1395 AQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdkvLAEWKTKCEESQAELEAALKE 1474
Cdd:PLN02939 63 SKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ------QTNSKDGEQLSDFQLEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1475 SRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEH 1554
Cdd:PLN02939 137 IQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGAT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1555 EEAKILRIQLELTQVKSEidrKIAEKDeEIEQLKRNYQRTVETmqgaldaevrsRNEAIRLKKK---MEGDLNEIEIQLS 1631
Cdd:PLN02939 217 EGLCVHSLSKELDVLKEE---NMLLKD-DIQFLKAELIEVAET-----------EERVFKLEKErslLDASLRELESKFI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1632 hanrQAAETIKHLRSVQGQ-LKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERAR------KLAE 1704
Cdd:PLN02939 282 ----VAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKfssykvELLQ 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 6981234 1705 QELLDSNERVQLLHTQNTSLI----HTKKKLETDLTQLQSEVEDASRD 1748
Cdd:PLN02939 358 QKLKLLEERLQASDHEIHSYIqlyqESIKEFQDTLSKLKEESKKRSLE 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1307-1474 |
6.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1307 QAFTQQIEELKRQLEEENKAKNALAHALQSsrhdcdlLREQYEEEQEGKAELQRALSKANSEVAQWRTKyetdaiqrtee 1386
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEAR----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1387 LEEAKKKLAQrlQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQA 1466
Cdd:COG1579 75 IKKYEEQLGN--VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
....*...
gi 6981234 1467 ELEAALKE 1474
Cdd:COG1579 153 ELEAELEE 160
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1644-1932 |
6.24e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1644 LRSVQGQLKDtqlhLDDALRGQE--DLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTqn 1721
Cdd:PRK02224 182 LSDQRGSLDQ----LKAQIEEKEekDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1722 tslihtkkkLETDLTQLQSEVEDASRDarnaEEKAKKAITDAAMMAEELKKEqdtsahlermkknLEQTVKDLQhrLDEA 1801
Cdd:PRK02224 256 ---------LEAEIEDLRETIAETERE----REELAEEVRDLRERLEELEEE-------------RDDLLAEAG--LDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1802 EQLALKggkKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKR 1881
Cdd:PRK02224 308 DAEAVE---ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1882 QAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSR 1932
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1713-1886 |
6.72e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1713 RVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNLEQ--T 1790
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNvrN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1791 VKDLQHRLDEAEQLalkggKKQIQKLETRIRELEFELEGEQKRntesvkgLRKYERRVKELTYQSEEDRKnvlRLQDLVD 1870
Cdd:COG1579 88 NKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEE-------LAELEAELAELEAELEEKKA---ELDEELA 152
|
170
....*....|....*.
gi 6981234 1871 KLQVKVKSYKRQAEEA 1886
Cdd:COG1579 153 ELEAELEELEAEREEL 168
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
842-1113 |
7.12e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 842 KSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIK 921
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 922 EVTERAedeEEINAELTAKKRKLeDECSELKKDIDDLELTLAKVEKEKhatENKVKNLTEELAgLDETIAKLTREKKALQ 1001
Cdd:COG1340 82 ELNEKL---NELREELDELRKEL-AELNKAGGSIDKLRKEIERLEWRQ---QTEVLSPEEEKE-LVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1002 EAHQQTlDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERL 1081
Cdd:COG1340 154 KALEKN-EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEI 232
|
250 260 270
....*....|....*....|....*....|....
gi 6981234 1082 KKKDFEYSQLQSKVED--EQTLSLQLQKKIKELQ 1113
Cdd:COG1340 233 IELQKELRELRKELKKlrKKQRALKREKEKEELE 266
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
844-1113 |
7.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEV 923
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 924 TERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEA 1003
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1004 HQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKK 1083
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270
....*....|....*....|....*....|
gi 6981234 1084 KDFEYSQLQSKVEDEQTLSLQLQKKIKELQ 1113
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELK 296
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1682-1765 |
7.80e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1682 LQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARnaeEKAKKAIT 1761
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK---QKRKEITD 223
|
....
gi 6981234 1762 DAAM 1765
Cdd:PRK11448 224 QAAK 227
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
857-1113 |
8.46e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 857 FQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIK-----------AKFQLEAKIKEVTE 925
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKtllanrfsygpAIDELEKQLAEIEE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 926 RAEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEkhatenkvknLTEELAGLDETIAKLTREK--- 997
Cdd:pfam06160 161 EFSQFEELTESgdyLEAREvlEKLEEETDALEELMEDIPPLYEELKTE----------LPDQLEELKEGYREMEEEGyal 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 998 ---------KALQEAHQQTLDDLqaEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQES-- 1066
Cdd:pfam06160 231 ehlnvdkeiQQLEEQLEENLALL--ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnk 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 1067 -----------------------------ILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKELQ 1113
Cdd:pfam06160 309 elkeelervqqsytlnenelervrglekqLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFK 384
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
872-1112 |
9.32e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 872 KELEEKLVTLVQEKNDLQ---LQVQAESENLLDAEERcdqLIKAKFQLEaKIKEVteraedeeeINAELTAKKRKLEDEC 948
Cdd:PRK05771 15 KSYKDEVLEALHELGVVHiedLKEELSNERLRKLRSL---LTKLSEALD-KLRSY---------LPKLNPLREEKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 949 SELKKDIDDLELTLAKVEKEkhatenkVKNLTEELAGLDETIAKLTREKKALQ--EAHQQTLDDLQAEED---KVNSLSK 1023
Cdd:PRK05771 82 KSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1024 -LKSKLEQQVDDLESSLEQEKKLR-----VDLERNKRKLEGDLKLAQESILDLENDKqQLDERLKKKDFEYSQLQSKVED 1097
Cdd:PRK05771 155 dKLEELKLESDVENVEYISTDKGYvyvvvVVLKELSDEVEEELKKLGFERLELEEEG-TPSELIREIKEELEEIEKERES 233
|
250
....*....|....*
gi 6981234 1098 eqtlslqLQKKIKEL 1112
Cdd:PRK05771 234 -------LLEELKEL 241
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1923 |
9.67e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1254 EDQLSEARGKNEETQRSLSELTtqkSRLQTEAGELSRQLEekesivsqlsrskqaftQQIEELKRQLEEENKAKNALAHA 1333
Cdd:NF041483 592 EEALADARAEAERIRREAAEET---ERLRTEAAERIRTLQ-----------------AQAEQEAERLRTEAAADASAARA 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1334 lQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAiqrTEELEEAKKKLAQRLQDSEEQVEAVNAKcA 1413
Cdd:NF041483 652 -EGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEA---AEALAAAQEEAARRRREAEETLGSARAE-A 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1414 SLEKTKQRLQGEvedlmvdveranslaaaldkkqrnfdKVLAEWKTKCEESQAELEAALKESRSLSTELfkLKNAYEEAL 1493
Cdd:NF041483 727 DQERERAREQSE--------------------------ELLASARKRVEEAQAEAQRLVEEADRRATEL--VSAAEQTAQ 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1494 DQLETVKRENKNLEQEIADLtEQIAEngksiHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLELTQV-KSE 1572
Cdd:NF041483 779 QVRDSVAGLQEQAEEEIAGL-RSAAE-----HAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAaKAL 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1573 IDRKIAEKDEEIEQLKRNYQRTVETMQG-ALDAEVRSRNEAIRLKKKMEGDLNEIEiqlSHANRQAAETIKHLRSVQGQL 1651
Cdd:NF041483 853 AERTVSEAIAEAERLRSDASEYAQRVRTeASDTLASAEQDAARTRADAREDANRIR---SDAAAQADRLIGEATSEAERL 929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1652 K-----DTQLHLDDALRGQEDLK-EQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLI 1725
Cdd:NF041483 930 TaearaEAERLRDEARAEAERVRaDAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERL 1009
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1726 HTKKKLETDLTqLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAH---------LERM----KKNLEQTVK 1792
Cdd:NF041483 1010 RTEAREEADRT-LDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALrttteaeaqADTMvgaaRKEAERIVA 1088
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1793 DL---------QHRLDEAEQLAlkGGKKQIQKLETRIRELEFELEGE-----QKRNTESVKGLRKYERRVKELTYQSEED 1858
Cdd:NF041483 1089 EAtvegnslveKARTDADELLV--GARRDATAIRERAEELRDRITGEieelhERARRESAEQMKSAGERCDALVKAAEEQ 1166
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1859 RKnvlrlqdlvdklQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERADIAESQVNKLRA 1923
Cdd:NF041483 1167 LA------------EAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKA 1219
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
903-1044 |
1.06e-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: 43.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 903 EERCDQLIKAKFQLEAKIKEVTEraeDEEEINAELTakkrkledECSELKKDIDDLELTL-AKVEKEKHATENKVKNLTE 981
Cdd:smart00787 136 EWRMKLLEGLKEGLDENLEGLKE---DYKLLMKELE--------LLNSIKPKLRDRKDALeEELRQLKQLEDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 982 ELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKK 1044
Cdd:smart00787 205 ELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1003 |
1.09e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 839 PLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEA 918
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 919 KIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLE---LT----LAKVEKEKHATENKVKNLTEELAGLDETIA 991
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaieeYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 6981234 992 KLTREKK-ALQEA 1003
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1293-1541 |
1.13e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1293 EEKESIVSQLSRSkQAFtqQIEELKRQLEeenkaknalahalqssrhdcdllREQYEEEQEGKAELQRALSKANSEVAQW 1372
Cdd:PRK05771 16 SYKDEVLEALHEL-GVV--HIEDLKEELS-----------------------NERLRKLRSLLTKLSEALDKLRSYLPKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1373 RTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLM------VDVERANSL------A 1440
Cdd:PRK05771 70 NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLGFkyvsvfV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1441 AALDKkqRNFDKVLAEWKTKCEESQAELE-------AALKESRSLSTELFK--------------LKNAYEEALDQLETV 1499
Cdd:PRK05771 150 GTVPE--DKLEELKLESDVENVEYISTDKgyvyvvvVVLKELSDEVEEELKklgferleleeegtPSELIREIKEELEEI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6981234 1500 KRENKNLEQEIADLTEQIAENGKSIHELeksrKQMELEKADI 1541
Cdd:PRK05771 228 EKERESLLEELKELAKKYLEELLALYEY----LEIELERAEA 265
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1674-1824 |
1.17e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1674 IVERRANLLQAEVEELratLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDAsrdarnaE 1753
Cdd:COG1842 2 IFKRLSDIIRANINAL---LDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW-------E 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1754 EKAKKAitdaammaeeLKKEQDTSAH--LERmKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLETRIRELE 1824
Cdd:COG1842 72 EKARLA----------LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEKL-KEALRQLESKLEELK 132
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
930-1037 |
1.20e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 930 EEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQT 1007
Cdd:PRK11281 38 EADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110
....*....|....*....|....*....|
gi 6981234 1008 LDDLqaeedkvnSLSKLKSKLEQQVDDLES 1037
Cdd:PRK11281 118 LSTL--------SLRQLESRLAQTLDQLQN 139
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
912-1084 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 912 AKFQLEAKIKEVTERAE---DEEEINAELTAKKRKLEdecseLKKDIDDLEltlAKVEKEKHATENKVKNLteelaglde 988
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-----AKEEIHKLR---NEFEKELRERRNELQKL--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 989 tiakltrEKKALQeaHQQTLDDlqaeedKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEgdLKLAQESIL 1068
Cdd:PRK12704 88 -------EKRLLQ--KEENLDR------KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL--QELERISGL 150
|
170
....*....|....*.
gi 6981234 1069 DLENDKQQLDERLKKK 1084
Cdd:PRK12704 151 TAEEAKEILLEKVEEE 166
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1459-1618 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1459 TKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAE------NGKSIHELEKSRK 1532
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgNVRNNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1533 QMELEKADIQM---ALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTV---ETMQGALDAEV 1606
Cdd:COG1579 97 EIESLKRRISDledEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaerEELAAKIPPEL 176
|
170
....*....|..
gi 6981234 1607 RSRNEAIRLKKK 1618
Cdd:COG1579 177 LALYERIRKRKN 188
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1307-1703 |
1.42e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1307 QAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLL----------------------REQYEEEQEGKAELQR---A 1361
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLnkllpqanlladetladrleelREELDAAQEAQAFIQQhgkA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1362 LSKANSEVaqwrtkyetDAIQRTEELEEAkkkLAQRLQDSEEQVEAVNAKCASLEKTKQRL-----QGEVEDLmvdvERA 1436
Cdd:COG3096 919 LAQLEPLV---------AVLQSDPEQFEQ---LQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLL----GEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1437 NSLAAALdkKQRnfdkvLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLetvkrenKNLEQEIADLTEQ 1516
Cdd:COG3096 983 SDLNEKL--RAR-----LEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTL-------QELEQELEELGVQ 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1517 IAENGKSIHELEKSRKQMELekadiqmalEEAEAALEHEEAKILRIQLELTQVK---SEIDRKIAEKDEEIEQLKRNYQR 1593
Cdd:COG3096 1049 ADAEAEERARIRRDELHEEL---------SQNRSRRSQLEKQLTRCEAEMDSLQkrlRKAERDYKQEREQVVQAKAGWCA 1119
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1594 tVETMqgaldaeVRSRNeairlkkkMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQlHLDDALRGQEDLKEQLA 1673
Cdd:COG3096 1120 -VLRL-------ARDND--------VERRLHRRELAYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPRRPER 1182
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1674 IV-----------ER-----------RANLLQAEVEELRATLEQTERARKLA 1703
Cdd:COG3096 1183 KVqfyiavyqhlrERirqdiirtddpVEAIEQMEIELARLTEELTSREQKLA 1234
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1338-1593 |
1.46e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1338 RHDCDLLREQYEEEQEgKAELQRALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQ---RLQDSEEQVEA 1407
Cdd:pfam03528 1 QPDEDLQQRVAELEKE-NAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLkrqnavlQEAQVELDAlqnQLALARAEMEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1408 VNAKCASLEKTKQRLQGEVEDLMVdvERANSLAAALDKKQRNF--------DKVLAEWKTKCEESQAELeAALKESRSLS 1479
Cdd:pfam03528 80 IKAVATVSENTKQEAIDEVKSQWQ--EEVASLQAIMKETVREYevqfhrrlEQERAQWNQYRESAEREI-ADLRRRLSEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1480 TELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQ-----MELEKA---DIQMALEEAEAA 1551
Cdd:pfam03528 157 QEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKelnhyLEAEKScrtDLEMYVAVLNTQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6981234 1552 LEHEEAKILRIQLELtqvkSEIDRKIAEKDEEIEQLKRNYQR 1593
Cdd:pfam03528 237 KSVLQEDAEKLRKEL----HEVCHLLEQERQQHNQLKHTWQK 274
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1373-1506 |
1.55e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 43.46 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1373 RTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQrnfdK 1452
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1453 VLAEWKTKCEESQAELEAALKESRSLSTELFKlknayeeALDQLETVKRENKNL 1506
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQ-------VLDKVQEIHEDCSVL 131
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1471-1911 |
1.73e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1471 ALKESRSLSTELFKLKNAYE----EALDQLETVKRENKNLEQEIADLTEQIAENGKSiheLEKSRKQMELEKADIQMALE 1546
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHLREALQQTQQS---HAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1547 EAEAALEHEEAKILRIQLELTQVKSEIDRK---IAEKDEEIEQLKRNYQRTVETMQGALDAEVRSR-NEAIRLKKKMEGD 1622
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLmKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1623 LNEIEIQLSHA----NRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEV-----EELRATL 1693
Cdd:TIGR00618 342 EQRRLLQTLHSqeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQatidtRTSAFRD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1694 EQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLE-TDLTQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKK 1772
Cdd:TIGR00618 422 LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1773 EQdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKR-------NTESVKGLRKYE 1845
Cdd:TIGR00618 502 EP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslkeqMQEIQQSFSILT 576
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 1846 RRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANVHLTKFRKAQHELEEAEERA 1911
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1674-1828 |
1.74e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1674 IVERRANLLQAEVEELratLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETdltqlqsEVEDASRDARNAE 1753
Cdd:pfam04012 1 IFKRLGRLVRANIHEG---LDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLER-------RLEQQTEQAKKLE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6981234 1754 EKAKKAITDAAmmaEELKKEqdtsahLERMKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLETRIRELEFELE 1828
Cdd:pfam04012 71 EKAQAALTKGN---EELARE------ALAEKKSLEKQAEALETQLAQQRSAVEQL-RKQLAALETKIQQLKAKKN 135
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
915-1067 |
1.85e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 915 QLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTE---------ELAG 985
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 986 LDETIAKLTREKKALQEahqQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQE 1065
Cdd:COG1579 94 LQKEIESLKRRISDLED---EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
..
gi 6981234 1066 SI 1067
Cdd:COG1579 171 KI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
872-1875 |
1.86e-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: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 872 KELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLI----KAKFQLEAKIKEVTeraeDEEEINAELTAKKRKLEDE 947
Cdd:TIGR01612 557 KKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIiyinKLKLELKEKIKNIS----DKNEYIKKAIDLKKIIENN 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 948 CSElkkdIDDL-ELTLAKVEKEKHATENKVKNLTEELAGLDE-TIAKLTREKKALQEAhqqtlDDLQAEEDKVnSLSKLK 1025
Cdd:TIGR01612 633 NAY----IDELaKISPYQVPEHLKNKDKIYSTIKSELSKIYEdDIDALYNELSSIVKE-----NAIDNTEDKA-KLDDLK 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1026 SKLEQQVDDLESSLEQEKKLRV-DLERNKRKLEGDLKLAQESIL-DLENDKQQLDERLKKKDfeySQLQSKVEDEQTLSL 1103
Cdd:TIGR01612 703 SKIDKEYDKIQNMETATVELHLsNIENKKNELLDIIVEIKKHIHgEINKDLNKILEDFKNKE---KELSNKINDYAKEKD 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1104 QLQK---KIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERleeaggvTSTQIELNKKREAEFLKLRRDLE 1180
Cdd:TIGR01612 780 ELNKyksKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDE-------IFKIINEMKFMKDDFLNKVDKFI 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1181 EATLQHEATVATLRKKHADSAAELAEQIDNLQRvkQKLEKEKSEFKLEIDDLSSSVESVSKSKANLE------KICRTLE 1254
Cdd:TIGR01612 853 NFENNCKEKIDSEHEQFAELTNKIKAEISDDKL--NDYEKKFNDSKSLINEINKSIEEEYQNINTLKkvdeyiKICENTK 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1255 DQLSEARGKneetQRSLSELTTQKSRLQTEAGELSRQLEEK--ESIVSQLSRSKQAFTQ-QIEELKRQLEEENKAKNALA 1331
Cdd:TIGR01612 931 ESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLK 1006
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1332 HALQSSRHdcDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLqdSEEQVEAVNAK 1411
Cdd:TIGR01612 1007 ANLGKNKE--NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELL--NKEILEEAEIN 1082
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1412 CASLEKTKQRLqgevedlmvdveranslaaaldkKQRNFDKVLAEWKTKCEEsqaELEAALKESRSLSTELFKLKNAYEE 1491
Cdd:TIGR01612 1083 ITNFNEIKEKL-----------------------KHYNFDDFGKEENIKYAD---EINKIKDDIKNLDQKIDHHIKALEE 1136
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1492 ALDQLETVKRENKNLEQEIADLTEQIAENgKSIHELEKSRKQMeLEKADIQMALEEAEAALEHEEAKILRIQLELTQVKS 1571
Cdd:TIGR01612 1137 IKKKSENYIDEIKAQINDLEDVADKAISN-DDPEEIEKKIENI-VTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKG 1214
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1572 eIDRKIAEK-----DEEIEQLKRNYQRTVETMQGALD--AEVRSRNEAIRLKKKMEGDLN-EIEI-QLSHANRQAAETI- 1641
Cdd:TIGR01612 1215 -INLSYGKNlgklfLEKIDEEKKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEMDIKaEMETfNISHDDDKDHHIIs 1293
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1642 ------------KHLRSVQGQL---------KDTQLHLDDALRGQEDLKEQLAIVERRANLLQAE-----VEELRATLEQ 1695
Cdd:TIGR01612 1294 kkhdenisdireKSLKIIEDFSeesdindikKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKE 1373
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1696 TERARKLAEQELLDSNERVQLLhTQNTSLIHTKKKLETDL----------------TQLQSEVEDASRDARNAEE----- 1754
Cdd:TIGR01612 1374 IEENNKNIKDELDKSEKLIKKI-KDDINLEECKSKIESTLddkdidecikkikelkNHILSEESNIDTYFKNADEnnenv 1452
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1755 --------------------KAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNLEQTVKDLQHRLDEAEQ 1803
Cdd:TIGR01612 1453 lllfkniemadnksqhilkiKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFEQYKKDVTELLNKYSA 1532
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6981234 1804 LALKGG----KKQIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVK 1875
Cdd:TIGR01612 1533 LAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
861-1113 |
1.90e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 861 KDELAKSEAKRKELEEkLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKF-------QLEAKIKEVTERAEDEEEI 933
Cdd:PLN02939 142 KNILLLNQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhveileeQLEKLRNELLIRGATEGLC 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 934 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEELAGLDETIAKLTREKKALQEAHQQtLDDLQA 1013
Cdd:PLN02939 221 VHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDASLRELESKFIVAQEDVSK-LSPLQY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1014 EE--DKVNSLSKLKSKLEQQVDDLESSLEQEKklrvDLERNKRKLEGDLKLAQESILDLEndkqqlderlkkkdfeysql 1091
Cdd:PLN02939 296 DCwwEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLKEANVSKFSSY-------------------- 351
|
250 260
....*....|....*....|..
gi 6981234 1092 qsKVEdeqtlslQLQKKIKELQ 1113
Cdd:PLN02939 352 --KVE-------LLQQKLKLLE 364
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
841-971 |
1.93e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 841 LKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVqaesenlldaeERCDQLIKakfQLEAKI 920
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----------EEKDERIE---RLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 6981234 921 KEVTERAEDEEEINAELTAKKRK---LEDECSELKKDIDDLEltlAKVEKEKHA 971
Cdd:COG2433 451 SEARSEERREIRKDREISRLDREierLERELEEERERIEELK---RKLERLKEL 501
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1259-1537 |
1.96e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1259 EARGKNEETQRSLSELTTQKSRL---QTEAGELSRQLEEkesivsqLSRSKQAFTQQIEELKRQLeeeNKAKNALAHALQ 1335
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLaaeQYRLVEMARELAE-------LNEAESDLEQDYQAASDHL---NLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1336 SSRHDCDL------LREQ---YEEEQEGKAELQRALSKANSEVAQWRTKY----------ETDAIQ-------------- 1382
Cdd:PRK04863 350 IERYQADLeeleerLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldvqQTRAIQyqqavqalerakql 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1383 -------------RTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDlmVDVERANSLAAALDKKQRN 1449
Cdd:PRK04863 430 cglpdltadnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGE--VSRSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1450 fDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEK 1529
Cdd:PRK04863 508 -QRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
....*...
gi 6981234 1530 SRKQMELE 1537
Cdd:PRK04863 587 QLEQLQAR 594
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1462-1743 |
2.26e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1462 EESQAELEAALKESRS-LSTELFKLKNAYE----EALDQLETVKRENKNLEQEIaDLTEQIAENGKSIHElEKSRKQMEL 1536
Cdd:pfam00038 24 EQQNKLLETKISELRQkKGAEPSRLYSLYEkeieDLRRQLDTLTVERARLQLEL-DNLRLAAEDFRQKYE-DELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1537 EkADIQMaleeaeaaleheeakiLRIQL-ELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRL 1615
Cdd:pfam00038 102 E-NDLVG----------------LRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1616 KKKMEGDLNEIEIQL-SHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQedlKEQLAIVERRANLLQAEVEELRATLE 1694
Cdd:pfam00038 165 KLDLTSALAEIRAQYeEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA---KEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6981234 1695 QTERArkLAEQElldsnERVQLLHTQNTSLIHtkkKLETDLTQLQSEVE 1743
Cdd:pfam00038 242 SLERQ--LAETE-----ERYELQLADYQELIS---ELEAELQETRQEMA 280
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
973-1329 |
2.43e-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: 42.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 973 ENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLK---------------------SKLEQQ 1031
Cdd:COG5185 172 LNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKakeiinieealkgfqdpeselEDLAQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1032 VDDLESSLEQEKKLRVDLERNKRKLEGDLK-LAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQ-LQKKI 1109
Cdd:COG5185 252 SDKLEKLVEQNTDLRLEKLGENAESSKRLNeNANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1110 KELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREaEFLKLRRDLEEATLQHEAT 1189
Cdd:COG5185 332 RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKE-SLDEIPQNQRGYAQEILAT 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1190 VATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQlSEARGKNEETQR 1269
Cdd:COG5185 411 LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVR-SKKEDLNEELTQ 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1270 SLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQ-QIEELKRQLEEENKAKNA 1329
Cdd:COG5185 490 IESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRaRGYAHILALENLIPASEL 550
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1251-1520 |
2.47e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1251 RTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNAL 1330
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1331 AHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNA 1410
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1411 KcASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELFKLKNAYE 1490
Cdd:COG4372 208 L-IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270
....*....|....*....|....*....|
gi 6981234 1491 EALDQLETVKRENKNLEQEIADLTEQIAEN 1520
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDA 316
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
842-1395 |
2.67e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 842 KSAETEKEMATMKEEFQKTKDELAKSEA-KRKELEEKLVTLVQEKNDLQlQVQAESENL---LDAEERCDQLIKAKFQ-L 916
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDqHGAFLDADIETAAADQEQLP-SWQSELENLeerLKALTGKHQDVTAKYNrR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 917 EAKIKEvtERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLakvekeKHATENKVKNLTEELAGLDETIAKLtre 996
Cdd:pfam12128 381 RSKIKE--QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLKSRLGEL--- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 997 kKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQ 1076
Cdd:pfam12128 450 -KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQ 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1077 LD---------------------------ERLKKKDFEYSQLQSKVEDEQTL---SLQLQK--------KIKELQARIEE 1118
Cdd:pfam12128 529 LFpqagtllhflrkeapdweqsigkvispELLHRTDLDPEVWDGSVGGELNLygvKLDLKRidvpewaaSEEELRERLDK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1119 LEEEIEAERATRAKTEKQRSDYARELEELSERLEEAG----GVTSTQIELNKKREAEFLKLRRDLEEA---------TLQ 1185
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERkdsanerlnSLE 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1186 HEATVatLRKKHADSAAELAEQI-------------------DNLQRVKQKLEKEKSEFKLEIDDLSSSVESV------- 1239
Cdd:pfam12128 689 AQLKQ--LDKKHQAWLEEQKEQKreartekqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDlaslgvd 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1240 SKSKANLEKICRTLEDQLSEARGKNEEtqrslselTTQKSRLQTEAGELSRQ--LEEKESIVSQLSRSKQAFTQQIEELK 1317
Cdd:pfam12128 767 PDVIAKLKREIRTLERKIERIAVRRQE--------VLRYFDWYQETWLQRRPrlATQLSNIERAISELQQQLARLIADTK 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1318 R---QLEEENKAKNALAHALQSSRHDCDLLREQYEE--EQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1392
Cdd:pfam12128 839 LrraKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
...
gi 6981234 1393 KLA 1395
Cdd:pfam12128 919 VIA 921
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1623-1764 |
2.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1623 LNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQA---------EVEELRATL 1693
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1694 EQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASRDARNAEEKAKKAITDAA 1764
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
848-1044 |
2.71e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 848 KEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQ--------------AESENLLDAEERCDQLIKAK 913
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleeelerteerlaEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 914 FQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKL 993
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 994 -TREKKALQ------EAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKK 1044
Cdd:pfam00261 161 eASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
911-1073 |
2.90e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 911 KAKFQLEAKIKEVTERAEDEEEIN-AELTAKKRKLEDECSELKKDIDDLEltlakvekekhatenkvknltEELAGLDET 989
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELE---------------------AELEEKDER 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 990 IAKLTRE-KKALQEAHQQTLDD--LQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNK----RKLEgdlKL 1062
Cdd:COG2433 443 IERLERElSEARSEERREIRKDreISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGElvpvKVVE---KF 519
|
170
....*....|.
gi 6981234 1063 AQESILDLEND 1073
Cdd:COG2433 520 TKEAIRRLEEE 530
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
954-1056 |
2.95e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 954 DIDDLELTLAKVEKEKHATENkvknltEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVD 1033
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 6981234 1034 DLESSLEQEKKLRVDLERNKRKL 1056
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
872-1224 |
2.96e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 872 KELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSEL 951
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 952 KKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQ 1031
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1032 VDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKE 1111
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1112 LQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEATVA 1191
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 6981234 1192 TLRKKHADSAAELAEQIDNLQRVKQKLEKEKSE 1224
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1048-1852 |
2.98e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1048 DLERNKRKLEGDLKLAQESILDL-----ENDKQQLDERLKKKDFE--------YSQLQSKVEDEQTLSLQLQKKIKELQA 1114
Cdd:pfam05483 27 NLSKNGENIDSDPAFQKLNFLPMleqvaNSGDCHYQEGLKDSDFEnseglsrlYSKLYKEAEKIKKWKVSIEAELKQKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1115 RIEELEEEieaeratrakTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREA--EFLKLRRDL----EEATLQHEA 1188
Cdd:pfam05483 107 KLQENRKI----------IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNAtrHLCNLLKETcarsAEKTKKYEY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1189 TVATLRKKHADSAAELAEQIDNLQRVKQKLEKEKSEFKLEiddLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQ 1268
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK---LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1269 RSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQY 1348
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1349 EEEQEgkaELQRALSKANSEVAQWRTKyetdaiqrTEELEEAKKKLAQRLQDSEEQVEAvnakcaslektkqrlqgeved 1428
Cdd:pfam05483 334 EAQME---ELNKAKAAHSFVVTEFEAT--------TCSLEELLRTEQQRLEKNEDQLKI--------------------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1429 LMVDVERANSLAAALDKKQRNFDKVLAEWKTKCeesqAELEAALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQ 1508
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1509 EIADLTEQIAENGKSIHELeksrkQMELEKADIQMALEEAEAALEHEEAKilriqlELTQVKSEIDRKIAEKDEEIEQLK 1588
Cdd:pfam05483 458 QLTAIKTSEEHYLKEVEDL-----KTELEKEKLKNIELTAHCDKLLLENK------ELTQEASDMTLELKKHQEDIINCK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1589 RNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKdtqlhlddalrgqedl 1668
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK---------------- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1669 keqlaIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQ----NTSLIHTKKKLETDLTQLQSEVED 1744
Cdd:pfam05483 591 -----ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvnklELELASAKQKFEEIIDNYQKEIED 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1745 ASRDARN---AEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNLEQTVKDLQHRLDEaeqLALKGGKKQIQK---- 1815
Cdd:pfam05483 666 KKISEEKlleEVEKAKAIADEAVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSE---LGLYKNKEQEQSsaka 742
|
810 820 830
....*....|....*....|....*....|....*...
gi 6981234 1816 -LETRIRELEFELEGEQKRNTESVKGLRKYERRVKELT 1852
Cdd:pfam05483 743 aLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1572-1940 |
3.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1572 EIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETIKHLRSVQGQL 1651
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1652 KDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKL 1731
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1732 ETDLTQLQSEVEdaSRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKK 1811
Cdd:COG4372 163 QEELAALEQELQ--ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1812 QIQKLETRIRELEFELEGEQKRNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQAN 1891
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 6981234 1892 VHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE 1940
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1166-1330 |
3.11e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1166 KKREAEFLKLRRDLEEATLQheATVATLRKKHADSA-AELAEQIDNLqrvkqkleKEKSEFKLeiddlsssVESVSKSKA 1244
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGAlKECMQQLRNV--------KEEQEQKI--------HDVVLKKTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1245 NLEKICRTLEDQLSEargKNEETQRSLSELTTqksrlqteageLSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEEN 1324
Cdd:pfam05911 82 EWEKIKAELEAKLVE---TEQELLRAAAENDA-----------LSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCE 147
|
....*.
gi 6981234 1325 KAKNAL 1330
Cdd:pfam05911 148 KEINSL 153
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
949-1079 |
3.17e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 949 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKALQEAHQQTLDDL----------------- 1011
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAfrqgehtglqlilsgee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1012 ---------------QAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLEN---- 1072
Cdd:PRK11637 151 sqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqk 230
|
....*..
gi 6981234 1073 DKQQLDE 1079
Cdd:PRK11637 231 DQQQLSE 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
836-1057 |
3.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 836 KIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQ 915
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 916 LEAKIKEVTERAEDEEEInAELTAKKRKLEDECSELKKDIDDL------------ELTLAKVEKEKHATENKVKNLTEEL 983
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALaelnderrerlaEKRERKRELEAEFDEARIEEAREDK 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 984 AGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSK---LEQQVDDLESSLEQEKKL-------RVDL-ERN 1052
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERreaLENRVEALEALYDEAEELesmygdlRAELrQRN 735
|
....*
gi 6981234 1053 KRKLE 1057
Cdd:PRK02224 736 VETLE 740
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
862-1141 |
3.22e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 862 DELAKSeaKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKakfQLEAKIKEVTERAEDEEEINAELTakk 941
Cdd:PHA02562 169 DKLNKD--KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELVEEAKTIKAEIEELT--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 942 rkleDECSELKKDIDDLELTLAKvekekhatenkvknLTEELAGLDETIAKLTREKKALQEAHQ-----QTLDDlqaEED 1016
Cdd:PHA02562 241 ----DELLNLVMDIEDPSAALNK--------------LNTAAAKIKSKIEQFQKVIKMYEKGGVcptctQQISE---GPD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1017 KVnslsklkSKLEQQVDDLESSLEQEKKLRVDLErnkrKLEGDLKLAQESILDLENDKQQLDERLKKKDFEysqlqskve 1096
Cdd:PHA02562 300 RI-------TKIKDKLKELQHSLEKLDTAIDELE----EIMDEFNEQSKKLLELKNKISTNKQSLITLVDK--------- 359
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 6981234 1097 deqtlSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYA 1141
Cdd:PHA02562 360 -----AKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELV 399
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1465-1828 |
3.25e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1465 QAELEAALKESRSLSTELFKLKNAYEEALDQLETVK----RENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKAD 1540
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDReqweRQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1541 IQMALEEAEAALEHEEAKIlriqLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTvetmqGALDAEVRSRNEAIRLK-KKM 1619
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARI----RELEEDIKTLTQRVLERETELERMKERAKKA-----GAQRKEEEAERKQLQAKlQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1620 EGDLNEIEIQLSHANRQAAETIKHLRSVQGQLKDTQLHLDDALRGQ---EDLKEQLAIVERRANLLQAEVEELRATLEQT 1696
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1697 ERARKLAEQEL----LDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVE-------DASRDARNAEEKAKKAITDAAM 1765
Cdd:pfam07888 264 AAQRDRTQAELhqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEadkdrieKLSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6981234 1766 MAEELKKEQDTS-AHLERMKKNLEQTVKDLQHRLDEAEQLALkggkkQIQKLETRIRELEFELE 1828
Cdd:pfam07888 344 LEVELGREKDCNrVQLSESRRELQELKASLRVAQKEKEQLQA-----EKQELLEYIRQLEQRLE 402
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
863-999 |
3.41e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 42.05 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 863 ELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEE-RCDQLIkakfqLEAKIKEVTERAEdeeEINAELTAKK 941
Cdd:pfam10186 27 DLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRLlKSEVAI-----SNERLNEIKDKLD---QLRREIAEKK 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 942 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTREKKA 999
Cdd:pfam10186 99 KKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1322-1588 |
3.72e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1322 EENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAE--LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQ 1399
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1400 DSEEQVEAVNAKCASLEKTKQRLQGEVE-DLMVDVERANSLAAALDKKQRNFDkvLAEWKTKCEESQAELEAALKESRSL 1478
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNID--LEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1479 STELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGkSIHELEKSRKQMELEKADIQmaleeAEAALEHEEAK 1558
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG-ALQESTKQLKELPVEVAELQ-----SASKIISSEST 1040
|
250 260 270
....*....|....*....|....*....|
gi 6981234 1559 ILRIQLELTQVKSEIDRKIAEKDEEIEQLK 1588
Cdd:COG5022 1041 ELSILKPLQKLKGLLLLENNQLQARYKALK 1070
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1683-1873 |
3.84e-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: 42.04 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1683 QAEVEELRATLEQTERarKLAEQELLDSNERVQLLHTQNTSlihtKKKLETDLTQLQsEVEDASRDARNAEEKAKKAITD 1762
Cdd:pfam05557 1 RAELIESKARLSQLQN--EKKQMELEHKRARIELEKKASAL----KRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1763 AAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRL-DEAEQLalkggKKQIQKLETRIRELEFELEGEQKRNTESVKGL 1841
Cdd:pfam05557 74 QAELNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSEL-----RRQIQRAELELQSTNSELEELQERLDLLKAKA 148
|
170 180 190
....*....|....*....|....*....|..
gi 6981234 1842 RKYERRVKELTYQSEEDRKNVLRLQDLVDKLQ 1873
Cdd:pfam05557 149 SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ 180
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1328-1533 |
3.89e-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: 41.67 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1328 NALAHALQSSRHDCDLLREQyeeeqegkaelqraLSKANSEVAQWRTKYETDAIQRTEELEEAKkklaQRLQDSEEQVEA 1407
Cdd:pfam09787 43 TALTLELEELRQERDLLREE--------------IQKLRGQIQQLRTELQELEAQQQEEAESSR----EQLQELEEQLAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1408 VNAKCASLEKTKQRLQGEVEDLMVDVERA-NSLAAALDKKQRNFDKVLAEWKTKC--EESQAELEAALKE-SRSL---ST 1480
Cdd:pfam09787 105 ERSARREAEAELERLQEELRYLEEELRRSkATLQSRIKDREAEIEKLRNQLTSKSqsSSSQSELENRLHQlTETLiqkQT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1481 ELFKLKNAYEEALDQLETVKRENKNLEQEIADlteQIAENGKSIHELEKSRKQ 1533
Cdd:pfam09787 185 MLEALSTEKNSLVLQLERMEQQIKELQGEGSN---GTSINMEGISDGEGTRLR 234
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1312-1543 |
4.21e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 41.24 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1312 QIEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEgkaELQRALSKAnsevaQWRTKYETDAIQRTEELEEAK 1391
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAKA-----QQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1392 KKLAQRLQDSEEQVEAVNAKCASL-EKTKQRLQGEVEDLMVDVERANslaaaLDKKQRNFDKVLAEWKTKCEESQAELEA 1470
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1471 ALKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTeqiAENGKSIHELEKSRKQMELEKADIQM 1543
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEE 236
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1745-1912 |
4.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1745 ASRDARNAEEKAKKAITDAAMMAEELKKEqdtsahlermkKNLEqtVKDLQHRL-DEAEQlALKGGKKQIQKLETRIREL 1823
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKE-----------ALLE--AKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1824 EFELEgeqkrntesvKGLRKYERRVKELtyqsEEDRKNVLRLQDLVDKLQVKVKSYKRQAEE---------ADEQANVHL 1894
Cdd:PRK12704 95 EENLD----------RKLELLEKREEEL----EKKEKELEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKEILL 160
|
170 180
....*....|....*....|....*..
gi 6981234 1895 TKFR-KAQHEL--------EEAEERAD 1912
Cdd:PRK12704 161 EKVEeEARHEAavlikeieEEAKEEAD 187
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
982-1111 |
4.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 982 ELAGLDETIAKLTREKKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLE--QEKKLRVDLERNKRKLEGD 1059
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyEEQLGNVRNNKEYEALQKE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1060 LKLAQESILDLENDKQQLDERLKKKDFEYSQLQSKVEDEQTLSLQLQKKIKE 1111
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
831-1002 |
4.65e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 831 MKLFFKIKPLLKSAETEKEMATMKeeFQKTKDELAKSEAKRKELEEKLVTLVQEKNDlqlqVQAESENLLDAEERCDQLI 910
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMEGK--LQVTQKNLEHSKGKVAQLEEKLVSTEKEKIE----EKSETEKLLEYITELSCVS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 911 KakfQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDL--ELTLAKVEKEKHATENKVK--NLTEELAGL 986
Cdd:pfam15905 236 E---QVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLneKCKLLESEKEELLREYEEKeqTLNAELEEL 312
|
170
....*....|....*.
gi 6981234 987 DETIAKLTREKKALQE 1002
Cdd:pfam15905 313 KEKLTLEEQEHQKLQQ 328
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1627 |
4.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1247 EKICRTLEDQLSEARGKNEETQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKA 1326
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1327 KNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDSEEQVE 1406
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD--------LEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1407 AVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEAALKESRSLSTELfklk 1486
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1487 NAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKSIHELEKSRKQMELEKADIQMALEEAEAALEHEEAKILRIQLEL 1566
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6981234 1567 TQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQGALDAEVRSRNEAIRLKKKMEGDLNEIE 1627
Cdd:COG4372 310 IGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1002-1136 |
4.90e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1002 EAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRV-------DLERNKRKLEGDLKLAQESIldlENDK 1074
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEARI---KKYE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6981234 1075 QQLDERLKKKdfEYSQLQSKVEDEQTLSLQLQKKIKELQARIEELEEEIEAERATRAKTEKQ 1136
Cdd:COG1579 80 EQLGNVRNNK--EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1668-1836 |
5.00e-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: 40.78 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1668 LKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLTQLQSEVEDASR 1747
Cdd:pfam00261 48 LEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1748 DARNAEEKAKKAITDAAMMAEELKKEQDTSAHLE-------RMKKNLEQTVKDLQHRLDEAEQLALKGgKKQIQKLETRI 1820
Cdd:pfam00261 128 DLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekasEREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEV 206
|
170
....*....|....*.
gi 6981234 1821 RELEFELEGEQKRNTE 1836
Cdd:pfam00261 207 DRLEDELEAEKEKYKA 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-982 |
5.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDELAKSE---------AKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKF 914
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6981234 915 QLEAKIKEVTERAEDEEEinaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE 982
Cdd:COG4717 178 ELEELLEQLSLATEEELQ---DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
845-1084 |
5.69e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 845 ETEKEMATMKEE---FQKTKDELAKSEAKRKELEEKLVTlvQEKNDLQLQVQAESEnLLDAEERCDQLIKAKFQLeaKIK 921
Cdd:PRK01156 487 EIEIEVKDIDEKivdLKKRKEYLESEEINKSINEYNKIE--SARADLEDIKIKINE-LKDKHDKYEEIKNRYKSL--KLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 922 EVTERAEDEEEINAELTAKK-RKLEDECSELKKDIDDLELTLAKVEKE----KHATENKVKNLTEELAGLDETIaKLTRE 996
Cdd:PRK01156 562 DLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY-NEIQE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 997 KKALQEAHQQTLDDLQAEEDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQ 1076
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
....*...
gi 6981234 1077 LDERLKKK 1084
Cdd:PRK01156 721 INETLESM 728
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
981-1099 |
6.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 981 EELAGLDETIAKLTREKKAL----QEAHQQTLDDLQAEEDKvnslsklkskLEQQVDDLESSLEQEKKLRVDLERNKRKL 1056
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkkeqDEASFERLAELRDELAE----------LEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 6981234 1057 EGDlklaQESILDLENDKQQLDERLKKKDfeySQLQSKVEDEQ 1099
Cdd:COG0542 481 EQR----YGKIPELEKELAELEEELAELA---PLLREEVTEED 516
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
865-1048 |
6.17e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.39 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 865 AKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINA---ELTAKK 941
Cdd:PRK00106 24 IKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKYREEIEQEFKSerqELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 942 RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEElaglDETIAKLTREKkalqEAHQQTLDDLQAEEDKVNSL 1021
Cdd:PRK00106 104 SRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDER----EEQVEKLEEQK----KAELERVAALSQAEAREIIL 175
|
170 180
....*....|....*....|....*..
gi 6981234 1022 SKLKSKLEQQVDDLESSLEQEKKLRVD 1048
Cdd:PRK00106 176 AETENKLTHEIATRIREAEREVKDRSD 202
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1296-1408 |
6.48e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 40.76 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1296 ESIVSQLSRSKQAFTQQIEELKRQLEEENKAKnALAHALqSSRHDCDLLREQYEEEQEGKAELQRALSKANSEvaQWRTK 1375
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 6981234 1376 YEtDAIQRTEELEEAKKKLAQRLQDSEEQVEAV 1408
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1252-1427 |
6.70e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1252 TLEDQLSEARGKNEETQRSLSELTTQKsRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALA 1331
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDGTQK-KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1332 HALQSSRHDCDLLREQYEEEQEGKAELQ---RALSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAV 1408
Cdd:pfam15905 205 EKLVSTEKEKIEEKSETEKLLEYITELScvsEQVEKYKLDIAQ----LEELLKEKNDEIESLKQSLEEKEQELSKQIKDL 280
|
170
....*....|....*....
gi 6981234 1409 NAKCASLEKTKQRLQGEVE 1427
Cdd:pfam15905 281 NEKCKLLESEKEELLREYE 299
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
844-1007 |
8.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 844 AETEKEMATMKEEFQKTKDELAKSEAKRKELEEKL--------------------------VTLVQEKNDLQLQVQAESE 897
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralyrsggsvsyldvllgsesfSDFLDRLSALSKIADADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 898 NLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK 977
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
170 180 190
....*....|....*....|....*....|
gi 6981234 978 NLTEELAGLDETIAKLTREKKALQEAHQQT 1007
Cdd:COG3883 214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
992-1095 |
8.73e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.84 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 992 KLTREKKALQEAHQQTLDDLQAE-EDKVNSLSKLKSKLEQQVDDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDL 1070
Cdd:pfam11559 45 QQRDRDLEFRESLNETIRTLEAEiERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNAL 124
|
90 100
....*....|....*....|....*
gi 6981234 1071 ENDKQQLDERLKKKDFEYSQLQSKV 1095
Cdd:pfam11559 125 QQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1202-1338 |
9.45e-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: 39.91 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 1202 AELAEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSVESVSKSKANLEKICRTLEDQLSEARGKNEETQRSLSELTTQK--- 1278
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeye 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6981234 1279 -------------SRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQIEELKRQLEEENKAKNALAHALQSSR 1338
Cdd:COG1579 93 alqkeieslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
847-1001 |
9.98e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.81 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 847 EKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLvQEKNDL---QLQVQAESENLLDAEERcdqlikakfQLEAKIKEV 923
Cdd:pfam05911 701 EVELASCTENLESTKSQLQESEQLIAELRSELASL-KESNSLaetQLKCMAESYEDLETRLT---------ELEAELNEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6981234 924 TERAEDEEeinAELTAKKR---KLEDECSELKKDID-----DLELTLAKVEKEKHATENKVKNLTEELAGLDETIAKLTR 995
Cdd:pfam05911 771 RQKFEALE---VELEEEKNcheELEAKCLELQEQLErnekkESSNCDADQEDKKLQQEKEITAASEKLAECQETILNLGK 847
|
....*.
gi 6981234 996 EKKALQ 1001
Cdd:pfam05911 848 QLKALA 853
|
|
| |
