|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
1-544 |
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: 1177.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14927 133 MEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMN 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14927 213 PYDYHFCSQGVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAY 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14927 293 LMGVSSADLLKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14927 373 IFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDA 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14927 453 SFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYV 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14927 533 GSDSTEDPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGI 612
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14927 613 RICRKGFPNRILYADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
1-544 |
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: 1076.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd01377 128 LEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd01377 208 PSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAH 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd01377 288 LLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKP-MGILSILEEECMFPKASD 319
Cdd:cd01377 368 IFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATD 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 320 MSFKAKLYDNHIGKSPNFQKPrpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENY 399
Cdd:cd01377 448 KTFVEKLYSNHLGKSKNFKKP---KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 400 VSSSSdeppkaGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEG 479
Cdd:cd01377 525 EESGG------GGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEG 598
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 480 IRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01377 599 IRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
1-544 |
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: 954.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLISLN 80
Cdd:cd14929 124 LEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSAN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14929 203 PSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAF 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14929 283 LMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14929 363 ILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPDKKrKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14929 443 TFKTKLFDNHFGKSVHFQKPKPDKK-KFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPpkAGVKeKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14929 522 STDSAIQ--FGEK-KRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGI 598
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14929 599 RICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
1-544 |
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: 922.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14913 129 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14913 209 PYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14913 289 LMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14913 369 IFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDT 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPDKKRKyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14913 449 SFKNKLYDQHLGKSNNFQKPKVVKGRA-EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAGVKekrKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14913 528 TADADSGKKKVAK---KKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGI 604
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14913 605 RICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
1-544 |
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: 885.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14917 129 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14917 209 PYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14917 289 LMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14917 369 IFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDM 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRpDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYv 400
Cdd:cd14917 449 TFKAKLFDNHLGKSNNFQKPR-NIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY- 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 sSSSDEPPKAGvKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14917 527 -AGADAPIEKG-KGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGI 604
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14917 605 RICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
1-544 |
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: 856.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14916 130 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14916 210 PYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAY 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14916 290 LMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14916 370 IFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDM 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRpDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14916 450 TFKAKLYDNHLGKSNNFQKPR-NVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAgvKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14916 529 SADTGDSGKG--KGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGI 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14916 607 RICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
1-544 |
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: 841.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14923 130 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14923 210 PFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGY 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14923 290 LMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14923 370 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDT 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14923 450 SFKNKLYDQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEpPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14923 529 GAEAGD-SGGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGI 607
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14923 608 RICRKGFPSRILYADFKQRYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
1-544 |
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: 839.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14909 127 LEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14909 207 IYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14909 287 LFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14909 367 IFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQ 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14909 447 TFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDepPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14909 527 GQSGG--GEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGI 604
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKfvDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14909 605 RICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
1-544 |
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: 827.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14918 129 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14918 209 PYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14918 289 LQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14918 369 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDT 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14918 449 SFKNKLYDQHLGKSANFQKPKV-VKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAGVKekrKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14918 528 SAEADSGAKKGAK---KKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 604
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14918 605 RICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
1-544 |
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: 826.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14934 125 LEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14934 205 PKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAH 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14934 285 LMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14934 365 IFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSqNKLLGSLYEnyv 400
Cdd:cd14934 445 TFKAALYDNHLGKSSNFLKPKGGKGKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKS-SLGLLALLF--- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 ssssDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14934 521 ----KEEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGI 596
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14934 597 RICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
1-544 |
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: 819.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14910 131 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14910 211 PYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14910 291 LQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14910 371 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENyv 400
Cdd:cd14910 451 SFKNKLYEQHLGKSNNFQKPKP-AKGKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG-- 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14910 528 AAAAEAEEGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 607
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14910 608 RICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
1-544 |
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: 817.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14912 131 LEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14912 211 PYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14912 291 LQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14912 371 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYV 400
Cdd:cd14912 451 SFKNKLYEQHLGKSANFQKPKV-VKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQ 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14912 530 TAEGASAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGI 609
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14912 610 RICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
1-544 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 816.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:pfam00063 135 LEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-N 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQ-GVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:pfam00063 214 PKDYHYLSQsGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD-TRLARQFFIGVLDIAG 238
Cdd:pfam00063 294 SLLGIDSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPMGILSILEEECMFPKA 317
Cdd:pfam00063 374 FEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKA 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 318 SDMSFKAKLYDNHiGKSPNFQKPRPdkkrKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYE 397
Cdd:pfam00063 453 TDQTFLDKLYSTF-SKHPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFP 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 398 NYVSSSSDEPPKAGVK-EKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGV 476
Cdd:pfam00063 528 DYETAESAAANESGKStPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGV 607
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 477 LEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:pfam00063 608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
1-544 |
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: 815.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14915 131 LEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14915 211 PYDFAFVSQGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAY 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGFE 240
Cdd:cd14915 291 LTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKASDM 320
Cdd:cd14915 371 IFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGKSPNFQKPRPdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENyv 400
Cdd:cd14915 451 SFKNKLYEQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-- 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 401 SSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGI 480
Cdd:cd14915 528 GQTAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGI 607
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 481 RICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14915 608 RICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
1-556 |
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: 774.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:smart00242 140 LEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLK-S 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVT-TVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAE-NTESADKA 158
Cdd:smart00242 219 PEDYRYLNQGGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVkDKEELSNA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 159 CYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAG 238
Cdd:smart00242 299 AELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPMGILSILEEECMFPKA 317
Cdd:smart00242 379 FEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKG 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 318 SDMSFKAKLYDNHiGKSPNFQKPRpdkkRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYE 397
Cdd:smart00242 458 TDQTFLEKLNQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFP 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 398 NYvssssdeppkAGVKEKRKKaasFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVL 477
Cdd:smart00242 533 SG----------VSNAGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVL 599
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 478 EGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKFvDSRKATEKLLNSLELDHSQYKFGHTKVFFKAGLLGHLEEMRD 556
Cdd:smart00242 600 ENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1-843 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 677.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-N 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQG-VTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKqKQREEQAEAENTESADKAC 159
Cdd:COG5022 280 PKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKAC 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGF 239
Cdd:COG5022 359 YLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGF 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 240 EIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEK--PMGILSILEEECMFPKA 317
Cdd:COG5022 439 EIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 318 SDMSFKAKLYDN-HIGKSPNFQKPR-PDKKrkyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:COG5022 518 TDESFTSKLAQRlNKNSNPKFKKSRfRDNK------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YENYVSSSSdeppkagvkeKRKkaasFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNG 475
Cdd:COG5022 592 FDDEENIES----------KGR----FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCG 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 476 VLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKFV---DSRKATEKLLNSLELDHSQYKFGHTKVFFKAGLLGHLE 552
Cdd:COG5022 658 VLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 553 EMRDERLAKILTMLQARIRGRLMRIEYQKIISRREALYTIQWNIRAFNAVKNWSWMKLFFKIKPLLRSAQTEKEMATLKE 632
Cdd:COG5022 738 DMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLA 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 633 EFQKLKEALEKsEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLEDEEEMNA 712
Cdd:COG5022 818 CIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 713 dLTSKKRKLEDECAELKKDID-----DLELTLAKVEKEKHATEN-KVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALD 786
Cdd:COG5022 897 -LKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYED 975
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 787 DLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQES 843
Cdd:COG5022 976 LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSAS 1032
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
1-544 |
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: 655.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd00124 127 LEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHF----CSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREE--QAEAENTES 154
Cdd:cd00124 207 LSYYYLndylNSSGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDES 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 155 ADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQF--FIG 232
Cdd:cd00124 287 LKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 233 VLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPMGILSILEEE 311
Cdd:cd00124 367 ILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 312 CMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKrkyeaHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSqnkl 391
Cdd:cd00124 446 CLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL-----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG---- 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 392 lgslyenyvssssdeppkagvkekrkkaASFqtvsqvhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQL 471
Cdd:cd00124 517 ----------------------------SQF-------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQL 561
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 472 RCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAiPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd00124 562 RCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
1-544 |
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: 626.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElQDMLLISLN 80
Cdd:cd14911 136 LEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPE-QREKFILDD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14911 215 VKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAH 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDtRLARQ--FFIGVLDIAG 238
Cdd:cd14911 295 LLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQgaSFIGILDMAG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMFPKAS 318
Cdd:cd14911 374 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKAT 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 319 DMSFKAKLYDNHiGKSPNFQKprpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYEN 398
Cdd:cd14911 454 DKTFVDKLVSAH-SMHPKFMK----TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 399 YVSSSSDEPPKAGVK-EKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVL 477
Cdd:cd14911 529 AEIVGMAQQALTDTQfGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVL 608
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 478 EGIRICRKGFPNRLLYADFKQRYRILNPAAIPdDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14911 609 EGIRICRQGFPNRIPFQEFRQRYELLTPNVIP-KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-544 |
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: 608.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLISL 79
Cdd:cd14920 127 LESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NpyDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd14920 207 N--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLC 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDtRLARQ--FFIGVLDIA 237
Cdd:cd14920 285 HLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQgaSFIGILDIA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 238 GFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPM---GILSILEEECMF 314
Cdd:cd14920 364 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWF 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 315 PKASDMSFKAKLYDNHiGKSPNFQKPRpdkKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGS 394
Cdd:cd14920 444 PKATDKTFVEKLVQEQ-GSHSKFQKPR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAE 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 395 LYENY-----VSSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLH 469
Cdd:cd14920 520 LWKDVdrivgLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 599
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 470 QLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPdDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14920 600 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
1-544 |
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: 563.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLliSLN 80
Cdd:cd14932 131 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSEL--CLE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYD-YHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd14932 209 DYSkYRFLSNGNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVC 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD-TRLARQFFIGVLDIAG 238
Cdd:cd14932 289 HLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPM---GILSILEEECMFP 315
Cdd:cd14932 369 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFP 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNHiGKSPNFQKPrpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd14932 449 KATDKSFVEKVVQEQ-GNNPKFQKP---KKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YENyVSSSSDEPPKAGVKEK-----RKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQ 470
Cdd:cd14932 525 WKD-VDRIVGLDKVAGMGESlhgafKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQ 603
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 471 LRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14932 604 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
1-544 |
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: 559.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGK-KPELQDMLLISl 79
Cdd:cd01380 122 MEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGS- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd01380 201 AEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIAC 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQF--FIGVLDIA 237
Cdd:cd01380 281 ELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIY 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 238 GFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPMGILSILEEECMFPKA 317
Cdd:cd01380 361 GFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKG 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 318 SDMSFKAKLYDNHIGK-SPNFQKPRPDKKRkyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNkllgsly 396
Cdd:cd01380 440 SDENWAQKLYNQHLKKpNKHFKKPRFSNTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 397 enyvssssdeppkagvkekRKKaasfqTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGV 476
Cdd:cd01380 508 -------------------RKK-----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGV 563
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 477 LEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKfvDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01380 564 LETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRD--DKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
1-544 |
1.69e-175 |
|
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: 545.00 E-value: 1.69e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLISL 79
Cdd:cd14921 127 LEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NpyDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd14921 207 N--NYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVC 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD-TRLARQFFIGVLDIAG 238
Cdd:cd14921 285 HLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPM---GILSILEEECMFP 315
Cdd:cd14921 365 FEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFP 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNHiGKSPNFQKPrpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd14921 445 KATDKSFVEKLCTEQ-GNHPKFQKP---KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YEN---------YVSSSSDEPPKAgvkeKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFL 466
Cdd:cd14921 521 WKDvdrivgldqMAKMTESSLPSA----SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFL 596
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 467 VLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14921 597 VLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
1-544 |
3.73e-172 |
|
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: 536.19 E-value: 3.73e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd15896 131 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-N 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd15896 210 YNNYRFLSNGNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCH 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD-TRLARQFFIGVLDIAGF 239
Cdd:cd15896 290 LMGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGF 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 240 EIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPM---GILSILEEECMFPK 316
Cdd:cd15896 370 EIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 317 ASDMSFKAKLYDNHiGKSPNFQKPrpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLY 396
Cdd:cd15896 450 ATDKSFVEKVLQEQ-GTHPKFFKP---KKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELW 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 397 ENyVSSSSDEPPKAGVKEK----RKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLR 472
Cdd:cd15896 526 KD-VDRIVGLDKVSGMSEMpgafKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 604
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 473 CNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd15896 605 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-544 |
6.59e-171 |
|
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: 532.75 E-value: 6.59e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLisLN 80
Cdd:cd14919 124 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL--LE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYD-YHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd14919 202 PYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD-TRLARQFFIGVLDIAG 238
Cdd:cd14919 282 HLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPM---GILSILEEECMFP 315
Cdd:cd14919 362 FEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFP 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNHiGKSPNFQKPrpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd14919 442 KATDKSFVEKVVQEQ-GTHPKFQKP---KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YENyVSSSSDEPPKAGVKEK------RKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLH 469
Cdd:cd14919 518 WKD-VDRIIGLDQVAGMSETalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 596
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 470 QLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14919 597 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-544 |
5.38e-168 |
|
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: 525.04 E-value: 5.38e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd14930 127 LEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYdYHFCSQGVTTVDNlDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKACY 160
Cdd:cd14930 207 SH-YRFLTNGPSSSPG-QERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDtRLARQ--FFIGVLDIAG 238
Cdd:cd14930 285 LLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAG 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPM---GILSILEEECMFP 315
Cdd:cd14930 364 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFP 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNHiGKSPNFQKPRpdkKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd14930 444 KATDKSFVEKVAQEQ-GGHPKFQRPR---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEI 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YENY--------VSSSSDEPPKAgvkekRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLV 467
Cdd:cd14930 520 WKDVegivgleqVSSLGDGPPGG-----RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 594
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 468 LHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14930 595 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
1-544 |
7.33e-167 |
|
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: 521.04 E-value: 7.33e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd01381 118 LEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-D 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQG-VTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEAENTESADK 157
Cdd:cd01381 197 ASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLER 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 ACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFF---IGVL 234
Cdd:cd01381 277 AAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 235 DIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLI-EKPMGILSILEEECM 313
Cdd:cd01381 357 DIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 314 FPKASDMSFKAKLYDNHiGKSPNFQKPrpdkKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLG 393
Cdd:cd01381 436 FPKGTDQTMLEKLHSTH-GNNKNYLKP----KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLK 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 394 SLYENYVSSSSDeppkagvkeKRKKAasfQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRC 473
Cdd:cd01381 511 QLFNEDISMGSE---------TRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRY 578
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 474 NGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKfVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01381 579 SGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHK-TDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
1-544 |
5.32e-164 |
|
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: 513.63 E-value: 5.32e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd01378 122 LEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRP 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQrEEQAEAENTESADKACY 160
Cdd:cd01378 202 EQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDE-EGNAAISDTSVLDFVAY 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEY---MTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQ-FFIGVLDI 236
Cdd:cd01378 281 LLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHhmFVL--EQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPMGILSILEEECM 313
Cdd:cd01378 361 YGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 314 FP-KASDMSFKAKLydNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLL 392
Cdd:cd01378 438 TAgDATDQTFLQKL--NQLFSNHPHFECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 393 GSLYenyvssssDEPPKAGVKeKRKKAASFQTvsqvhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLR 472
Cdd:cd01378 516 RSLF--------PEGVDLDSK-KRPPTAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVK 581
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 473 CNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKFvDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01378 582 YLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
1-544 |
6.44e-160 |
|
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: 502.23 E-value: 6.44e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLn 80
Cdd:cd01383 116 LEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQ-GVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd01383 195 ASEYKYLNQsNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD---TRLARqfFIGVLDI 236
Cdd:cd01383 275 SLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEvgkRRTGR--SISILDI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPMGILSILEEECMFP 315
Cdd:cd01383 353 YGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLyDNHIGKSPNFQKPRpdkkrkyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd01383 432 KATDLTFANKL-KQHLKSNSCFKGER-------GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YENYVSSSSDEPP--KAGVKEKRKkaasfQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRC 473
Cdd:cd01383 504 ASKMLDASRKALPltKASGSDSQK-----QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRC 578
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 474 NGVLEGIRICRKGFPNRLLYADFKQRYRILNP--AAIPDDKFVDSRkATEKLLNSLEldhSQYKFGHTKVFFK 544
Cdd:cd01383 579 CGVLEVVRISRSGYPTRMTHQEFARRYGFLLPedVSASQDPLSTSV-AILQQFNILP---EMYQVGYTKLFFR 647
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
624-1701 |
4.34e-158 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 512.03 E-value: 4.34e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 624 EKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMER 703
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 704 LEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQ 783
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 784 ALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEF 863
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 864 ETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNK 943
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 944 KREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANA 1023
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1024 EKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKS 1103
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1104 KNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLAIRLQEAEEAVE 1183
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1184 AAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLK 1263
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1264 NAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLEL 1343
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1344 SQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQ 1423
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1424 LQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLIN 1503
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1504 HKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAL 1583
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1584 KGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEA 1663
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 2077626420 1664 EQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSR 1701
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
1-544 |
1.15e-156 |
|
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: 494.15 E-value: 1.15e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK--PELQDMLLIs 78
Cdd:cd14883 118 LEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 79 LNPYDYHFCSQ-GVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAE-AENTESAD 156
Cdd:cd14883 197 GEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 157 KACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDI 236
Cdd:cd14883 277 IVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEK-PMGILSILEEECMFP 315
Cdd:cd14883 357 FGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFP 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNHiGKSPNFQKPrpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd14883 436 KGTDLTYLEKLHAAH-EKHPYYEKP---DRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKEL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 --YENYVSSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRC 473
Cdd:cd14883 512 ftYPDLLALTGLSISLGGDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRY 591
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 474 NGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAI-PDDKfvDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14883 592 AGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARsADHK--ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
1-544 |
2.39e-144 |
|
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: 460.22 E-value: 2.39e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd01384 123 LEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-D 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVT-TVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTES---AD 156
Cdd:cd01384 202 PKQFHYLNQSKCfELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 157 KACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDI 236
Cdd:cd01384 282 AAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDI 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPMGILSILEEECMFP 315
Cdd:cd01384 362 YGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFP 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNhIGKSPNFQKPrpdkKRKYEAhFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd01384 441 RSTHETFAQKLYQT-LKDHKRFSKP----KLSRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YenyvssssdePPKAGvkEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNG 475
Cdd:cd01384 515 F----------PPLPR--EGTSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGG 582
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 476 VLEGIRICRKGFPNRLLYADFKQRYRILNPAAipDDKFVDSRKATEKLLNSLELDhsQYKFGHTKVFFK 544
Cdd:cd01384 583 VLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV--LKGSDDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
1-544 |
9.51e-136 |
|
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: 437.59 E-value: 9.51e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHF---------GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG----- 66
Cdd:cd14888 122 LEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareak 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 67 ------------------KKPELQDMLLI-SLNPYDYHFCSqGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIV 127
Cdd:cd14888 202 ntglsyeendeklakgadAKPISIDMSSFePHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 128 GAIMHFGNMKFKQKQREEQA---EAENTESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKA 204
Cdd:cd14888 281 AAILYLGNILFENNEACSEGavvSASCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 205 TYDRMFKWLVTRINKTLD-TRLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWV 283
Cdd:cd14888 361 LYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWN 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 284 FIDFGlDLQACIDLI-EKPMGILSILEEECMFPKASDMSFKAKLYDNHIGKSpnfqkpRPDKKRKYEAHFELVHYAGVVP 362
Cdd:cd14888 441 PLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 363 YNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYVSSSSDEPPkagvkEKRKkaasFQTVSQVHKENLNKLMTNLRA 442
Cdd:cd14888 514 YCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTDGNT-----KKKK----FVTVSSEFRNQLDVLMETIDK 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 443 TQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAaipddkfvdsrkatek 522
Cdd:cd14888 585 TEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNG---------------- 648
|
570 580
....*....|....*....|..
gi 2077626420 523 llnSLELDHSQYKFGHTKVFFK 544
Cdd:cd14888 649 ---EGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
1-544 |
1.83e-132 |
|
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: 427.82 E-value: 1.83e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLisln 80
Cdd:cd01382 120 LEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 pydyhfcsqgvtTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADK--- 157
Cdd:cd01382 196 ------------KDPLLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQsle 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 -ACYLMGISSADLIKGLLHpRVKVGNEYMTKGQ------NVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRlARQFF 230
Cdd:cd01382 264 yAAELLGLDQDELRVSLTT-RVMQTTRGGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYF 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 231 IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPMGILSILE 309
Cdd:cd01382 342 IGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 310 EECMFPKASDMSFKAKLYDNHiGKSPNFQKPRPDKKRKY-----EAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVF 384
Cdd:cd01382 421 EESKLPKPSDQHFTSAVHQKH-KNHFRLSIPRKSKLKIHrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 385 QKSQNKLLGSLYEnyvsssSDEPPKAGVKEKRKKaASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDA 464
Cdd:cd01382 500 CESKDKFIRSLFE------SSTNNNKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEG 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 465 FLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDdkfVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01382 573 AQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
1-542 |
1.03e-131 |
|
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: 426.13 E-value: 1.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKP-ELQDMLLISL 79
Cdd:cd14901 137 LEAFGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTES-ADKA 158
Cdd:cd14901 217 EEYKYLNSSQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 159 CYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL--DTRLARQFFIGVLDI 236
Cdd:cd14901 297 CDLLGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDI 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDlQACIDLIE-KPMGILSILEEECMFP 315
Cdd:cd14901 377 FGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLP 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNhIGKSPNFQKprpDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSl 395
Cdd:cd14901 456 RGNDEKLANKYYDL-LAKHASFSV---SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 yenyvssssdeppkagvkekrkkaasfqTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNG 475
Cdd:cd14901 531 ----------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSG 582
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 476 VLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLEL----DHSQYKFGHTKVF 542
Cdd:cd14901 583 VLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
1-544 |
1.90e-131 |
|
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: 424.96 E-value: 1.90e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISln 80
Cdd:cd14872 118 LEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 pYDYHFCSQ-GVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKAC 159
Cdd:cd14872 196 -AAYGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLK 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 Y---LMGISSADLIKGLLHPRVKVgneymtKGQNV-------EQVVYAVGALAKATYDRMFKWLVTRINKTLDTRL-ARQ 228
Cdd:cd14872 275 EvatLLGVDAATLEEALTSRLMEI------KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRPQKgAKT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 229 FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEK-PMGILSI 307
Cdd:cd14872 349 TFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 308 LEEECMFPKASDMSFKAKLYDNHIGKSpNFQkprPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKS 387
Cdd:cd14872 428 LDDQVKIPKGSDATFMIAANQTHAAKS-TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSS 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 388 QNKLLGSLYenyvssssdePPKAGvKEKRKKAasfqTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLV 467
Cdd:cd14872 504 KNKLIAVLF----------PPSEG-DQKTSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMS 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 468 LHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILnPAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14872 569 LEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
1-544 |
3.47e-128 |
|
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: 416.48 E-value: 3.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14890 142 LESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-T 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENT-ESADKAC 159
Cdd:cd14890 221 PVEYFYLRGECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDIAGF 239
Cdd:cd14890 301 ELLGVNEDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 240 EIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPMGILSILE--EECMFPK 316
Cdd:cd14890 381 EKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 317 AS--DMSFKAKLYDNHIGKS------------PNFQKPRPDKKRkyeaHFELVHYAGVVPYNIVGWLDKNKDPLNETVVV 382
Cdd:cd14890 460 GEeaNKKFVSQLHASFGRKSgsggtrrgssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 383 VFQKSQNKLlgslyenyvssssdeppkagvkekRKKAASFQTVSQVHkenlnKLMTNLRATQPHFVRCIIPNETKTPGAM 462
Cdd:cd14890 536 LIKQSRRSI------------------------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKF 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 463 DAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVdsrKATEKLLNsleLDHSQYKFGHTKVF 542
Cdd:cd14890 587 DGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENIEQLV---AVLSKMLG---LGKADWQIGSSKIF 660
|
..
gi 2077626420 543 FK 544
Cdd:cd14890 661 LK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
1-544 |
3.79e-127 |
|
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: 413.38 E-value: 3.79e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLIsLN 80
Cdd:cd01387 119 LEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-QE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTT-VDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADK-- 157
Cdd:cd01387 197 AEKYFYLNQGGNCeIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEiq 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 -ACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDI 236
Cdd:cd01387 277 wVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLI-EKPMGILSILEEECMFP 315
Cdd:cd01387 357 FGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFP 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLYDNHiGKSPNFQKPRPDkkrkyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSL 395
Cdd:cd01387 436 QATDHSFLEKCHYHH-ALNELYSKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 YENYVSSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNG 475
Cdd:cd01387 510 FSSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSG 589
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 476 VLEGIRICRKGFPNRLLYADFKQRYRILnpAAIPDDKFVDSRKATEKLLNSLELD-HSQYKFGHTKVFFK 544
Cdd:cd01387 590 MLETIRIRKEGYPVRLPFQVFIDRYRCL--VALKLPRPAPGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
1-544 |
1.62e-126 |
|
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: 410.90 E-value: 1.62e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE--LQDMLLiS 78
Cdd:cd01379 119 MEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDkkLAKYKL-P 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 79 LNPYDYHFCSQGVTTVDNLDDG---EELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAE----N 151
Cdd:cd01379 198 ENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSsrisN 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 152 TESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL--DTRLA-RQ 228
Cdd:cd01379 278 PEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEP 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 229 FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFG-----LDLqacidLIEKPMG 303
Cdd:cd01379 358 LSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMG 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 304 ILSILEEECMFPKASDMSFKAKLYDNHigKSPNFQKPRPDkkrkyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVV 383
Cdd:cd01379 433 LLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 384 FQKSQNKLLGslyenyvssssdeppkagvkekrkkaasfQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMD 463
Cdd:cd01379 506 LRSSENPLVR-----------------------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFD 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 464 AFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAipDDKFVDSRKATEKLLNSLELDHsqYKFGHTKVFF 543
Cdd:cd01379 557 REKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFL 632
|
.
gi 2077626420 544 K 544
Cdd:cd01379 633 K 633
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
1-544 |
3.65e-126 |
|
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: 410.71 E-value: 3.65e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElQDMLLISLN 80
Cdd:cd14903 120 LESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVE-ERLFLDSAN 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFcSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAE--AENTESADKA 158
Cdd:cd14903 199 ECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 159 CYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL--DTRLARQffIGVLDI 236
Cdd:cd14903 278 TKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLgnDAKMANH--IGVLDI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPMGILSILEEECMFPK 316
Cdd:cd14903 356 FGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPK 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 317 ASDMSFKAKLYDNHIGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLY 396
Cdd:cd14903 435 GNEESFVSKLSSIHKDEQDVIEFPRTSR-----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 397 ENYVSSSSDEPPKAGVKEKRKK--AASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCN 474
Cdd:cd14903 510 KEKVESPAAASTSLARGARRRRggALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCA 589
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 475 GVLEGIRICRKGFPNRLLYADFKQRYRILNPAAipDDKFVDSRKATEKLLNSLELDH-SQYKFGHTKVFFK 544
Cdd:cd14903 590 GVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
1-544 |
1.83e-125 |
|
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: 408.76 E-value: 1.83e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLISLN 80
Cdd:cd14892 138 LEAFGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQG-VTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEAENTESADK 157
Cdd:cd14892 217 AESFLFLNQGnCVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 ACYLMGISSADLIKGLLHpRVKVGneymTKGQNVE------QVVYAVGALAKATYDRMFKWLVTRINK----------TL 221
Cdd:cd14892 297 AAGLLGVDAAELMFKLVT-QTTST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAchkqqtsgvtGG 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 222 DTRLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEK- 300
Cdd:cd14892 372 AASPTFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKk 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 301 PMGILSILEEECMFP-KASDMSFKAKLYDNHIGKSPNFQKPRPDKKrkyeaHFELVHYAGVVPYNIVGWLDKNKDPLnet 379
Cdd:cd14892 451 PLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNL--- 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 380 vvvvfqksQNKLLGSLyenyvssssdeppkagvkEKRKKaasFQTvsqvhkeNLNKLMTNLRATQPHFVRCIIPNETKTP 459
Cdd:cd14892 523 --------HDDLRDLL------------------RSSSK---FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFP 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 460 GAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRIL-----NPAAIPDDKFVDSRKATEKLLNSLELDHSQY 534
Cdd:cd14892 567 GGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLarnkaGVAASPDACDATTARKKCEEIVARALERENF 646
|
570
....*....|
gi 2077626420 535 KFGHTKVFFK 544
Cdd:cd14892 647 QLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
1-544 |
3.64e-123 |
|
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: 402.25 E-value: 3.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14873 128 MEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-T 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQ-GVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQreeQAEAENTESADKAC 159
Cdd:cd14873 207 PENYHYLNQsGCVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFITAG---GAQVSFKTALGRSA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRlaRQF-FIGVLDIAG 238
Cdd:cd14873 284 ELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFkSIGILDIFG 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 239 FEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPMGILSILEEECMFPKAS 318
Cdd:cd14873 362 FENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQAT 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 319 DMSFKAKLYDNHiGKSPNFQKPrpdkkRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYEN 398
Cdd:cd14873 441 DSTLLEKLHSQH-ANNHFYVKP-----RVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEH 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 399 YVSSSSDEPPKAGVKEKRKkaasfqTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLE 478
Cdd:cd14873 515 VSSRNNQDTLKCGSKHRRP------TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLE 588
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 479 GIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkfvDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14873 589 TVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
1-544 |
1.30e-119 |
|
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: 393.66 E-value: 1.30e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKkPELQDMLLISLN 80
Cdd:cd01385 120 LEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGA-SEEERKELHLKQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVT-TVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQK--QREEQAEAENTESADK 157
Cdd:cd01385 199 PEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 ACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL----DTRLARQFFIGV 233
Cdd:cd01385 279 ISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 234 LDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPMGILSILEEEC 312
Cdd:cd01385 359 LDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEES 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 313 MFPKASDMSFKAKlYDNHIGKSPNFQKPrpdkkRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLL 392
Cdd:cd01385 438 NFPGATNQTLLAK-FKQQHKDNKYYEKP-----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 393 GSLY----------------------------------ENYVSSSSDEPPKAGVKEKRKKAASfqTVSQVHKENLNKLMT 438
Cdd:cd01385 512 RELIgidpvavfrwavlrafframaafreagrrraqrtAGHSLTLHDRTTKSLLHLHKKKKPP--SVSAQFQTSLSKLME 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 439 NLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIpdDKFVDSRK 518
Cdd:cd01385 590 TLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL--ISSKEDIK 667
|
570 580
....*....|....*....|....*.
gi 2077626420 519 ateKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01385 668 ---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
1-544 |
9.64e-116 |
|
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: 381.31 E-value: 9.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSG-KLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLIsL 79
Cdd:cd14891 139 LESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-L 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQ-GVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESADKA 158
Cdd:cd14891 218 SPEDFIYLNQsGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 159 ----CYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVL 234
Cdd:cd14891 298 lataAELLGVDEEALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 235 DIAGFEIFE-YNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPMGILSILEEEC 312
Cdd:cd14891 378 DIFGFESFEtKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEA 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 313 MFPKASDMSFKAKLYDNHiGKSPNFqkPRPDKKRKYEAhFELVHYAGVVPYNIVGWLDKNKDPLNETvvvvfqksqnkll 392
Cdd:cd14891 457 RNPNPSDAKLNETLHKTH-KRHPCF--PRPHPKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPED------------- 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 393 gslYENYVSSSsdeppkagvkekrkkaASFQTVSQvhkenlnKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLR 472
Cdd:cd14891 520 ---FEDLLASS----------------AKFSDQMQ-------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLR 573
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 473 CNGVLEGIRICRKGFPNRLLYADFKqryRILNPAAIPDDK--FVDSRKA-TEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14891 574 CSGILQTCEVLKVGLPTRVTYAELV---DVYKPVLPPSVTrlFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
1-544 |
1.12e-114 |
|
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: 377.88 E-value: 1.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14897 120 LEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-D 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEEL-----MATDHA--MDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTE 153
Cdd:cd14897 199 PDCHRILRDDNRNRPVFNDSEELeyyrqMFHDLTniMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 154 SADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTR-----LARQ 228
Cdd:cd14897 279 PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDkdfqiMTRG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 229 FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPMGILSI 307
Cdd:cd14897 359 PSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 308 LEEECMFPKASDMSFKAKLyDNHIGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKS 387
Cdd:cd14897 438 LDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNS 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 388 QNKLLGSLYENYVssssdeppkagvkekrkkaasfqtvsqvhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLV 467
Cdd:cd14897 512 NNEFISDLFTSYF-----------------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELV 562
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 468 LHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAaiPDDKFVDSRKATEKLLNSLELdhSQYKFGHTKVFFK 544
Cdd:cd14897 563 RRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGI--KGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
1-509 |
8.34e-114 |
|
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: 375.03 E-value: 8.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElqdmlliSLN 80
Cdd:cd14900 145 LESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEA-------ARK 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYhfcsqgvttvdnlddgEELMAtdhAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTE------- 153
Cdd:cd14900 218 RDMY----------------RRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiw 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 154 SADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL-----DTRLARQ 228
Cdd:cd14900 279 SRDAAATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 229 FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPMGILSI 307
Cdd:cd14900 359 HFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 308 LEEECMFPKASDMSFKAKLYdNHIGKSPNFQKPRPDKKRkyeAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKS 387
Cdd:cd14900 438 IDEECVMPKGSDTTLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 388 QNkllgslyenyvssssdeppkagvkekrkkaasfqtvsqvHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLV 467
Cdd:cd14900 514 LQ---------------------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERV 554
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2077626420 468 LHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIP 509
Cdd:cd14900 555 LNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
1-544 |
1.24e-110 |
|
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: 367.31 E-value: 1.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLIsLN 80
Cdd:cd14889 122 LEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL-LD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDD-GEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFkQKQREEQAEAENTESA--DK 157
Cdd:cd14889 200 PGKYRYLNNGAGCKREVQYwKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF-EMDDDEALKVENDSNGwlKA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 ACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRL-----ARQffIG 232
Cdd:cd14889 279 AAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDdssveLRE--IG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 233 VLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDL-IEKPMGILSILEEE 311
Cdd:cd14889 357 ILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQ 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 312 CMFPKASDMSFKAKLyDNHIGKSPNFQKPRpDKKRKyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKL 391
Cdd:cd14889 436 SHFPQATDESFVDKL-NIHFKGNSYYGKSR-SKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 392 LGSLYENYVSSSSDEPPKAG---VKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVL 468
Cdd:cd14889 510 LSVLFTATRSRTGTLMPRAKlpqAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQ 589
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 469 HQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRIL-NPAAIPDDKfvdsrKATEKLLNSLELdhSQYKFGHTKVFFK 544
Cdd:cd14889 590 DQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlCEPALPGTK-----QSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
1-544 |
2.46e-108 |
|
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: 360.89 E-value: 2.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFG-PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE-LQDM-LLI 77
Cdd:cd14907 147 LEAFGNAKTVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQlLQQLgLKN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 78 SLNPYDYHFCSQGVT-TVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEAENTES 154
Cdd:cd14907 227 QLSGDRYDYLKKSNCyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKET 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 155 ADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL--------DTRLA 226
Cdd:cd14907 307 LQIIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQN 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 227 RQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVF--IDFgLDLQACIDLIEK-PMG 303
Cdd:cd14907 387 KYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIG 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 304 ILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVV 383
Cdd:cd14907 466 IFNLLDDSCKLATGTDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINC 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 384 FQKSQNKLLGSLYENYVSSSSDEPPKAGVKEKRKKaasfqTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMD 463
Cdd:cd14907 541 IQNSKNRIISSIFSGEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFI 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 464 AFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNpaaipddkfvdsrkatekllnsleldhSQYKFGHTKVFF 543
Cdd:cd14907 616 QGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFM 668
|
.
gi 2077626420 544 K 544
Cdd:cd14907 669 K 669
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
1-597 |
4.04e-104 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 353.95 E-value: 4.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LISL 79
Cdd:PTZ00014 230 LEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYkLKSL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NpyDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA-----ENTES 154
Cdd:PTZ00014 310 E--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAaaisdESLEV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 155 ADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVL 234
Cdd:PTZ00014 388 FNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGML 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 235 DIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMGILSILEEECMF 314
Cdd:PTZ00014 468 DIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 315 PKASDMSFKAKLYdNHIGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGS 394
Cdd:PTZ00014 548 PGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRD 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 395 LYEnyvssssdeppkaGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCN 474
Cdd:PTZ00014 623 LFE-------------GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 475 GVLEGIRICRKGFPNRLLYADFKQRYRILNpAAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFKAGLLGHLEEM 554
Cdd:PTZ00014 690 SILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQI 768
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2077626420 555 RDERLAK---ILTMLQARIRGRLMRieyQKIISRREALYTIQWNIR 597
Cdd:PTZ00014 769 QREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
1-544 |
3.47e-102 |
|
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: 343.08 E-value: 3.47e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-KKPELQDMLLISL 79
Cdd:cd14904 120 LESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFkQKQREEQAEAENTESADKAC 159
Cdd:cd14904 200 CQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 YLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL---DTRLARQffIGVLDI 236
Cdd:cd14904 279 KMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEKPMGILSILEEECMFPK 316
Cdd:cd14904 357 FGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPR 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 317 ASDMSFKAKLYDNH--IGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGS 394
Cdd:cd14904 436 GTEEALVNKIRTNHqtKKDNESIDFPKVKR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 395 LYENYVSSSSDEPPKAGVKEKRKKAASFQtvsqvHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCN 474
Cdd:cd14904 511 LFGSSEAPSETKEGKSGKGTKAPKSLGSQ-----FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSA 585
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 475 GVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkfvDSRKATEKLLNSLELDHS-QYKFGHTKVFFK 544
Cdd:cd14904 586 GVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
1-512 |
8.03e-101 |
|
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: 339.96 E-value: 8.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG------KKPELQDM 74
Cdd:cd14908 140 LEAFGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeehEKYEFHDG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 75 LLISLN-PYDYHFCSQG-VTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQRE---EQAEA 149
Cdd:cd14908 220 ITGGLQlPNEFHYTGQGgAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDgaaEIAEE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 150 ENTESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL--DTRLAR 227
Cdd:cd14908 300 GNEKCLARVAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 228 QFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPMGILS 306
Cdd:cd14908 380 RSSVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 307 ILEEECMFP-KASDMSFKAKLYDNHIgksPNFQKPRPDKKR-------KYEAHFELVHYAGVVPYNI-VGWLDKNKDPLN 377
Cdd:cd14908 459 MLDDECRLGiRGSDANYASRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIP 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 378 ETVVVVFQKSQNkllgslyenyvssssdeppkagvkekrkkaasfqtvsqvHKENLNKLMTNLRATQPHFVRCIIPNETK 457
Cdd:cd14908 536 LTADSLFESGQQ---------------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAA 576
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 458 TPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPaAIPDDK 512
Cdd:cd14908 577 KPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVV 630
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
1-544 |
8.36e-101 |
|
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: 340.78 E-value: 8.36e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGP-----SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML 75
Cdd:cd14895 135 LESFGNARTLRNDNSSRFGKFVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLEL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 76 -LISLNPYDYHFCSQGVTTV--DNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENT 152
Cdd:cd14895 215 qLELLSAQEFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 153 ESA------------------DKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLV 214
Cdd:cd14895 295 ASApcrlasaspssltvqqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLV 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 215 TRINKTLDTRLARQF-----------FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWV 283
Cdd:cd14895 375 SKVNSASPQRQFALNpnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWN 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 284 FIDFGLDlQACIDLIE-KPMGILSILEEECMFPKASDMSFKAKLYDNHIGKSpNFQKPRPDKKrkyEAHFELVHYAGVVP 362
Cdd:cd14895 455 AVDYEDN-SVCLEMLEqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 363 YNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYVSSSSDEPPKAGVKEKRKKAA-SFQTVSQVHKENLNKLMTNLR 441
Cdd:cd14895 530 YQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVlSSVGIGSQFKQQLASLLDVVQ 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 442 ATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDkfvdsrKATE 521
Cdd:cd14895 610 QTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD------ATAS 683
|
570 580
....*....|....*....|...
gi 2077626420 522 KLLNSLELDHSQykFGHTKVFFK 544
Cdd:cd14895 684 ALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
1-505 |
3.71e-100 |
|
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: 339.18 E-value: 3.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14902 138 LESFGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQ-K 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDY-----HFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESA 155
Cdd:cd14902 217 GGKYellnsYGPSFARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 156 ---DKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFF-- 230
Cdd:cd14902 297 fhlAKCAELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsd 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 231 -------IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPM 302
Cdd:cd14902 377 edeelatIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSN 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 303 GILSILEEECMFPKASDMSFKAKLYDNHIGkspnfqkprpdkkrkyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVV 382
Cdd:cd14902 456 GLFSLLDQECLMPKGSNQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASD 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 383 VFQKSQNKLLGSL--YENYVSSSSDEPPKAGVKEKRKKAASfqtVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPG 460
Cdd:cd14902 520 ILSSSSNEVVVAIgaDENRDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPG 596
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2077626420 461 AMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNP 505
Cdd:cd14902 597 IFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
1-544 |
5.80e-99 |
|
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: 333.49 E-value: 5.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LISL 79
Cdd:cd14876 121 LEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYhLLGL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDY--HFCSQgVTTVDNLDDGEELMATDHAMdilGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA-----ENT 152
Cdd:cd14876 201 KEYKFlnPKCLD-VPGIDDVADFEEVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAaaisnESL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 153 ESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIG 232
Cdd:cd14876 277 EVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMG 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 233 VLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI---EWVFIDFgldlQACID-LIEKPMGILSIL 308
Cdd:cd14876 357 MLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSN----AEVIDvLCGKGKSVLSIL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 309 EEECMFPKASDMSFKAKLYDNhIGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQ 388
Cdd:cd14876 433 EDQCLAPGGSDEKFVSACVSK-LKSNGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQAST 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 389 NKLLGSLYEnyvssssdeppkaGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVL 468
Cdd:cd14876 508 NPVVKALFE-------------GVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVL 574
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 469 HQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPaAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14876 575 IQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
1-544 |
1.45e-93 |
|
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: 317.88 E-value: 1.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14896 119 LESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ-G 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQG-VTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESAD--K 157
Cdd:cd14896 197 PETYYYLNQGgACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 ACYLMGISsADLIKGLLHPRVKVGN-EYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFF--IGVL 234
Cdd:cd14896 277 AARLLQVP-PERLEGAVTHRVTETPyGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVV 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 235 DIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDfGLDLQACIDLI-EKPMGILSILEEECM 313
Cdd:cd14896 356 DAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTW 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 314 FPKASDMSFKAKLYDNHiGKSPNFQKPR---PDkkrkyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNK 390
Cdd:cd14896 435 LSQATDHTFLQKCHYHH-GDHPSYAKPQlplPV--------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQ 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 391 LLGSLYEnyvssssDEPPKAGVKEKRKKAAS-FQtvsqvhkENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLH 469
Cdd:cd14896 506 LVGSLFQ-------EAEPQYGLGQGKPTLASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTE 571
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 470 QLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDdkFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14896 572 QLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
1-544 |
4.03e-89 |
|
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: 305.58 E-value: 4.03e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGP-SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISL 79
Cdd:cd14875 131 MESFGNARTVRNDNSSRFGKYIKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQGVTTV------DNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQrEEQAEAENTE 153
Cdd:cd14875 211 TAQDYKCLNGGNTFVrrgvdgKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQ-NDKAQIADET 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 154 SADKACYLMGISSADLIKGLLhprVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRL--ARQFFI 231
Cdd:cd14875 290 PFLTACRLLQLDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYI 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 232 GVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPMGILSILEE 310
Cdd:cd14875 367 GLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 311 ECMFPKASDMSFKAKLYDNHIGKSPNFQKPrpdkKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNK 390
Cdd:cd14875 446 ECNFKGGTTERFTTNLWDQWANKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 391 LLGSLYenyvsssSDEPpkagVKEKRKkaasfQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQ 470
Cdd:cd14875 522 FIRTLL-------STEK----GLARRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQ 585
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 471 LRCNGVLEGIRICRKGFPNRLLYADF-KQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHS----QYKFGHTKVFFK 544
Cdd:cd14875 586 LESAGVLQTIALKRQGYPVRRPIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
1-501 |
1.43e-88 |
|
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: 305.48 E-value: 1.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHF-GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGK----KPELQDML 75
Cdd:cd14899 147 LEAFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 76 LISLNPYDYHFCSQGVTTV--DNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEAEN 151
Cdd:cd14899 227 ALSGGPQSFRLLNQSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 152 TESA----------DKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL 221
Cdd:cd14899 307 ARVMssttgafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 222 DTRLARQF---------------FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFID 286
Cdd:cd14899 387 QRQASAPWgadesdvddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVD 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 287 FGlDLQACIDLIE-KPMGILSILEEECMFPKASDMSFKAKLYDNHIGKS--PNFqkpRPDKKRKYEAHFELVHYAGVVPY 363
Cdd:cd14899 467 FP-NNRACLELFEhRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHF---RSAPLIQRTTQFVVAHYAGCVTY 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 364 NIVGWLDKNKDPLNETVVVVFQKSQNKLL-----GSLYENYVSSSSDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMT 438
Cdd:cd14899 543 TIDGFLAKNKDSFCESAAQLLAGSSNPLIqalaaGSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLS 622
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 439 NLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYR 501
Cdd:cd14899 623 TVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
1-542 |
1.15e-85 |
|
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: 295.22 E-value: 1.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE--LQDMLlis 78
Cdd:cd14880 131 MEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADerLQWHL--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 79 lnPYDYHFcSQGVTTVDNLDDgEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EAENTESA 155
Cdd:cd14880 208 --PEGAAF-SWLPNPERNLEE-DCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 156 DKACYLMGISSADLIKGLLHPRVKVGneymtKGQNVEQVVYAVG-------ALAKATYDRMFKWLVTRINKTLDTRLAR- 227
Cdd:cd14880 284 RTSALLLKLPEDHLLETLQIRTIRAG-----KQQQVFKKPCSRAecdtrrdCLAKLIYARLFDWLVSVINSSICADTDSw 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 228 QFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPMGILS 306
Cdd:cd14880 359 TTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICS 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 307 ILEEECMFPKASDmsfkAKLYDNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQK 386
Cdd:cd14880 438 LINEECRLNRPSS----AAQLQTRIESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQ 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 387 SQNKLLGSLYENYVSSSSDEPPKAgvkekRKKAASFQTVSQVhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFL 466
Cdd:cd14880 514 SQDPLLQKLFPANPEEKTQEEPSG-----QSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEE 587
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 467 VLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPaaipddkfvdSRKATEKLLNSLELDHSQYKF---GHTKVF 542
Cdd:cd14880 588 VLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR----------LRPHTSSGPHSPYPAKGLSEPvhcGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
1-544 |
1.24e-84 |
|
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: 292.18 E-value: 1.24e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LISL 79
Cdd:cd14886 125 LESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQgVTTVDNLDDGEELMATDHAMDILgFSNEEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEAENTESAD 156
Cdd:cd14886 205 ESYNFLNASK-CYDAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 157 KACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIGVLDI 236
Cdd:cd14886 283 KMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDI 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 237 AGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEKP-MGILSILEEECMFP 315
Cdd:cd14886 363 YGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQ 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 316 KASDMSFKAKLyDNHIgKSPNFQkprPDKKRkyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGsl 395
Cdd:cd14886 442 TGSSEKFTSSC-KSKI-KNNSFI---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN-- 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 396 yenyvSSSSDEPPKAGVKEKRKKAASFQTvsqvhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNG 475
Cdd:cd14886 513 -----KAFSDIPNEDGNMKGKFLGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLS 580
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 476 VLEGIRICRKGFPNRLLYADFKQRYRILNP-AAIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14886 581 IFESIQTIHRGFAYNDTFEEFFHRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
1-504 |
6.23e-77 |
|
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: 271.47 E-value: 6.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHF-GPSGKLASADIDIYLLEKSRvIFQQPGER--SYHIYYQILSGKKPELQDMLLI 77
Cdd:cd14906 131 LEAFGNSRTTKNHNSSRFGKFLKIEFrSSDGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 78 SLNPYDYHFCSQGVTTVD---------------NLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQ 142
Cdd:cd14906 210 NNDPSKYRYLDARDDVISsfksqssnknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 143 ---REEQAEAENTESADKACYLMGISSADLIKGLLHPRVKVGNE--YMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRI 217
Cdd:cd14906 290 dfsKYAYQKDKVTASLESVSKLLGYIESVFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 218 NKTLDTRLARQ-----------FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFID 286
Cdd:cd14906 370 NRKFNQNTQSNdlaggsnkknnLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSN 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 287 FgLDLQACIDLIE-KPMGILSILEEECMFPKASDMSFKAKLYDNHigkspnFQKPRPDKKRKYEAHFELVHYAGVVPYNI 365
Cdd:cd14906 450 F-IDNKECIELIEkKSDGILSLLDDECIMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQT 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 366 VGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYVSSSSDEppkagvkekRKKAASFQTVSQVHKENLNKLMTNLRATQP 445
Cdd:cd14906 523 DGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITSTTNT---------TKKQTQSNTVSGQFLEQLNQLIQTINSTSV 593
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 446 HFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILN 504
Cdd:cd14906 594 HYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
1-544 |
1.68e-75 |
|
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: 266.48 E-value: 1.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISLN 80
Cdd:cd01386 120 LEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFcsqGVTTVDNLDDGE----ELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGN---MKFKQKQREEQAeaeNTE 153
Cdd:cd01386 200 AESNSF---GIVPLQKPEDKQkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFA---RPE 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 154 SADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQV------------VYAVGALAKATYDRMFKWLVTRINKTL 221
Cdd:cd01386 274 WAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESParsssggpkltgVEALEGFAAGLYSELFAAVVSLINRSL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 222 DTRLARQFFIGVLDIAGFEIFEYN------SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEwvfIDFGLD---LQ 292
Cdd:cd01386 354 SSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 293 ACIDLIEK---------------PMGILSILEEECMFPKASDMSFKAKLYdNHIGKSPNFQKPRPDKKRKYEAHFELVHY 357
Cdd:cd01386 431 ALVALIDQapqqalvrsdlrdedRRGLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHL 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 358 AGV--VPYNIVGWLDKNK-DPLNETVVVVFQKSQNKLlgslyenyvssssdeppkAGVKekrKKAASFQTVSQVhkenlN 434
Cdd:cd01386 510 LGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQKET------------------AAVK---RKSPCLQIKFQV-----D 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 435 KLMTNLRATQPHFVRCIIPN------ETKTPGA------MDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRI 502
Cdd:cd01386 564 ALIDTLRRTGLHFVHCLLPQhnagkdERSTSSPaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQV 643
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2077626420 503 LNPA----AIPDDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd01386 644 LAPPltkkLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
1-544 |
4.04e-73 |
|
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: 258.02 E-value: 4.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14937 114 LEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR-S 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEE---LMATDHAMDIlgfsNEEKYGCYKIVGAIMHFGNMKFKQ-----KQREEQAEAENT 152
Cdd:cd14937 193 ENEYKYIVNKNVVIPEIDDAKDfgnLMISFDKMNM----HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 153 ESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQFFIG 232
Cdd:cd14937 269 ELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 233 VLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDlQACIDLIEKPMGILSILEEEC 312
Cdd:cd14937 349 ILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSC 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 313 MFPKASDMSFkAKLYDNHIGKSPNFQKprpdKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLL 392
Cdd:cd14937 428 LGPVKNDESI-VSVYTNKFSKHEKYAS----TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLV 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 393 GSLYENYVSSSSdeppkagvkEKRKKAASFQtvsqvHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLR 472
Cdd:cd14937 503 RSLYEDVEVSES---------LGRKNLITFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLF 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 473 CNGVLEGIRIcRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDhsQYKFGHTKVFFK 544
Cdd:cd14937 569 SLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
1-544 |
1.49e-71 |
|
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: 253.97 E-value: 1.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISl 79
Cdd:cd14878 122 LEAFGHAKTTLNDLSSCFIKYFELQFCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYHFCSQG----VTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAENTESA 155
Cdd:cd14878 201 NLCAHRYLNQTmredVSTAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 156 DKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTL----DTRLARQFFI 231
Cdd:cd14878 281 EQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDI 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 232 GVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACID-LIEKPMGILSILEE 310
Cdd:cd14878 361 GILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 311 ECMFPKASDMSFKAKLY------DNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVF 384
Cdd:cd14878 441 ESQMIWSVEPNLPKKLQsllessNTNAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVM 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 385 QKSQNKLLGSLYEnyvssssdeppkagvkekrkkaASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDA 464
Cdd:cd14878 521 KTSENVVINHLFQ----------------------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDN 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 465 FLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAIPDDKFVDSRKATEKLLNSLELDHSQykFGHTKVFFK 544
Cdd:cd14878 579 FYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQ--MGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
1-507 |
3.05e-71 |
|
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: 250.59 E-value: 3.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgpSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLisln 80
Cdd:cd14898 114 LEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 pyDYHFCSQGVTTVDNLDdgEELMATDHAMDILGFSNEEKYGcyKIVGAIMHFGNMKFKQkqrEEQAEAENTESADKACY 160
Cdd:cd14898 188 --DTSSTAGNKESIVQLS--EKYKMTCSAMKSLGIANFKSIE--DCLLGILYLGSIQFVN---DGILKLQRNESFTEFCK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 161 LMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLARQffIGVLDIAGFE 240
Cdd:cd14898 259 LHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFE 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 241 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPMGILSILEEECMFP--KAS 318
Cdd:cd14898 337 IFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAwgNVK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 319 DMSFKAKLYDNHigkspnFQKPRPDKKRKyeahfeLVHYAGVVPYNIVGWLDKNKdplnetvvvvfQKSQNKLLGSLyen 398
Cdd:cd14898 416 NLLVKIKKYLNG------FINTKARDKIK------VSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNL--- 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 399 yvssssdeppkaGVKEKRKKaasfQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLE 478
Cdd:cd14898 470 ------------LINDEGSK----EDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILE 533
|
490 500
....*....|....*....|....*....
gi 2077626420 479 GIRICRKGFPNRLLYADFKQRYRILNPAA 507
Cdd:cd14898 534 TIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
5-535 |
2.24e-68 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 243.87 E-value: 2.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 5 GNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LISLNPYD 83
Cdd:cd14881 119 GSAKTATNSESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPAN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 84 YHFCSQGVTTVDNLDDGEELMATDHAMDILG--FSNeekygCYKIVGAIMHFGNMKFKQKQREEQAEAENTEsADKACYL 161
Cdd:cd14881 198 LRYLSHGDTRQNEAEDAARFQAWKACLGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAAL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 162 MGISSADLIKGLlHPRVKvgneyMTKGQNVEQVVYA------VGALAKATYDRMFKWLVTRINK------TLDTRlARQF 229
Cdd:cd14881 272 LGVSGAALFRGL-TTRTH-----NARGQLVKSVCDAnmsnmtRDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 230 FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW-VFIDFgLDLQACIDLIEK-PMGILSI 307
Cdd:cd14881 345 FIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSM 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 308 LEEECMfPKASDMSFKAKLYDNHIGkSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKs 387
Cdd:cd14881 424 LDVECS-PRGTAESYVAKIKVQHRQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK- 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 388 QNKLLGslyenYVSSSSDeppkagvkekrkkaasFQTvsqvhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLV 467
Cdd:cd14881 497 QNCNFG-----FATHTQD----------------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTV 548
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 468 LHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAiPDDKFVDSRKATEKLLNSLELDHSQYK 535
Cdd:cd14881 549 VRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFR-LLRRVEEKALEDCALILQFLEAQPPSK 615
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
2-508 |
8.88e-60 |
|
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: 218.20 E-value: 8.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 2 EAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlNP 81
Cdd:cd14874 109 KSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 82 YDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQ----REEQAEAENTESADK 157
Cdd:cd14874 188 QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMSEVKW 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 158 ACYLMGISSADLIKGLLhPRVKVGNEYmtkgqNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDTRLaRQFFIGVLDIA 237
Cdd:cd14874 268 VAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 238 GFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEwvfIDFglDLQACID-------LIEKPMGILSILEE 310
Cdd:cd14874 341 GFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGIS---VDY--KVPNSIEngktvelLFKKPYGLLPLLTD 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 311 ECMFPKASDMSFKAKLYDNHIGKSpNFQKPRpdKKRKYEahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNK 390
Cdd:cd14874 416 ECKFPKGSHESYLEHCNLNHTDRS-SYGKAR--NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNP 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 391 LLGSLYENYVSSSSDEppkagvkekrkkaasFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQ 470
Cdd:cd14874 491 IIGLLFESYSSNTSDM---------------IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQ 555
|
490 500 510
....*....|....*....|....*....|....*...
gi 2077626420 471 LRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPAAI 508
Cdd:cd14874 556 IKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
2-543 |
1.30e-57 |
|
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: 212.41 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 2 EAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlNP 81
Cdd:cd14879 133 DSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD-DP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 82 YDY-----HFCSQGVTTVDNlDDGE---ELMAtdhAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEAEN 151
Cdd:cd14879 212 SDYallasYGCHPLPLGPGS-DDAEgfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 152 TESADKACYLMGISSADLiKGLLHPRVK-VGNEYMTkgqnveqvVY--AVGA------LAKATYDRMFKWLVTRINktld 222
Cdd:cd14879 288 TDVLDIVAAFLGVSPEDL-ETSLTYKTKlVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETIN---- 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 223 TRLA---RQF--FIGVLDIAGFEIF---EYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQAC 294
Cdd:cd14879 355 QKLCapeDDFatFISLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDC 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 295 IDLI-EKPMGILSILEEEC-MFPKASDMSFKAKLYDNHIGKSPnFQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKN 372
Cdd:cd14879 434 VRLLrGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERN 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 373 KDPLNETVVvvfqksqnKLLGSlyenyvssssdeppkagvkekrkkAASFQtvsqvhkENLNKLMTNLRATQPHFVRCII 452
Cdd:cd14879 513 GDVLSPDFV--------NLLRG------------------------ATQLN-------AALSELLDTLDRTRLWSVFCIR 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 453 PNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYrilnpaaIPDDKFVDSRKATEKLLNSLELDHS 532
Cdd:cd14879 554 PNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGR 626
|
570
....*....|.
gi 2077626420 533 QYKFGHTKVFF 543
Cdd:cd14879 627 DYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
1-544 |
2.01e-54 |
|
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: 204.50 E-value: 2.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQDMLLISL 79
Cdd:cd14887 131 LEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 80 NPYDYhfcsqgvttvdnlddgeELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA--------EN 151
Cdd:cd14887 211 DPEST-----------------DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvGC 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 152 TESADKACYLMGISS--------------ADLIKGLLHPRVKVGNEYM-------------TKGQNVEQVVYAVGALAKA 204
Cdd:cd14887 274 EETAADRSHSSEVKClssglkvteasrkhLKTVARLLGLPPGVEGEEMlrlalvsrsvretRSFFDLDGAAAARDAACKN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 205 TYDRMFKWLVTRINKTL-------------DTRLARQF-FIGVLDIAGFEIFE---YNSFEQLCINFTNEKLQQFFNHHM 267
Cdd:cd14887 354 LYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 268 FVLEQEEYKKEG--IEWVFIDFGLDLQACIDLIEKP------------------------MGILSILEEE-CMFPKASDM 320
Cdd:cd14887 434 ILNEHMLYTQEGvfQNQDCSAFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 321 SFKAKLYDNHIGK----SPNFQKPRPDKKRKyEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFqksqnkLLGSLY 396
Cdd:cd14887 514 RDNSDLFYEKLNKniinSAKYKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDELERLF------LACSTY 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 397 ENYVSSSSDEPPKAgVKEKRKkaasfqTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGV 476
Cdd:cd14887 587 TRLVGSKKNSGVRA-ISSRRS------TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGM 659
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 477 LEGIRICRKGFPNRLLYADFKQRYRILNPAAIpdDKFVDSRKATEKLLNSLELDHSQYKFGHTKVFFK 544
Cdd:cd14887 660 SDLLRVMADGFPCRLPYVELWRRYETKLPMAL--REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
1-492 |
4.95e-47 |
|
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: 181.26 E-value: 4.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHF---------GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPEL 71
Cdd:cd14884 128 LESMSNATTIKNNNSSRCGRINLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDED 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 72 QDMLLISLNPYDYHFCSQGV------------TTVDNLDDGEELMATD--------HAMDILGFSNEEKYGCYKIVGAIM 131
Cdd:cd14884 208 LARRNLVRNCGVYGLLNPDEshqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGIL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 132 HFGNMKFKQkqreeqaeaentesadkACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFK 211
Cdd:cd14884 288 HLGNRAYKA-----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFN 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 212 WLVTRINKTL------------DTRLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG 279
Cdd:cd14884 351 KIIEDINRNVlkckekdesdneDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYAREN 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 280 IEWVfidfGLDLQACIDLIEKPMGILSILEEECMFP----KASDMSFKAKLYDN---------HI-GKSPNFQKPRPDKK 345
Cdd:cd14884 431 IICC----SDVAPSYSDTLIFIAKIFRRLDDITKLKnqgqKKTDDHFFRYLLNNerqqqlegkVSyGFVLNHDADGTAKK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 346 RKYEAH-FELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENyvssssdeppkagvkekrKKAASFQT 424
Cdd:cd14884 507 QNIKKNiFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLREANNG------------------GNKGNFLS 568
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 425 VSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLL 492
Cdd:cd14884 569 VSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
1-543 |
1.55e-45 |
|
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: 177.47 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK--PELQDMLLIS 78
Cdd:cd14893 141 LEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 79 LNPYDYHFCSQGVTTVDNLD----DGEELMATDHAMDIlgfSNEEKYGCYKIVGAIMHFGNMKF---KQKQREEQAEAEN 151
Cdd:cd14893 221 KCVNEFVMLKQADPLATNFAldarDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpdPEGGKSVGGANST 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 152 TESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQ----------------NVEQVVYAVGALAKATYDRMFKWLVT 215
Cdd:cd14893 298 TVSDAQSCALKDPAQILLAAKLLEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 216 RINKTLD---TRLARQFF------IGVLDIAGFEIFE--YNSFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEG 279
Cdd:cd14893 378 TLNGILGgifDRYEKSNIvinsqgVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVEN 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 280 IEWV--FIDFGLDLQACIDLIE-KPMGILSILEEECMFPKASDMSFKAKLY--DNHIG--KSPN----FQKPRPDKKRKY 348
Cdd:cd14893 458 RLTVnsNVDITSEQEKCLQLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNmgadTTNEYLAPSKDW 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 349 EAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLLGSLYENYVSSSSDEPPKAGVKEKRKKAASFQTVSQV 428
Cdd:cd14893 538 RLLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASS 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 429 HKENLN--------------KLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYA 494
Cdd:cd14893 618 ARESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYG 697
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 495 DFKQRYRilnpaaipddKFVDSRKATEKLLNSLE----LDHSQYKFGHTKVFF 543
Cdd:cd14893 698 HFFRRYK----------NVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
1-544 |
1.39e-41 |
|
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: 164.14 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE--LQDMLLIS 78
Cdd:cd14882 118 ILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 79 LNPYDYHFCSQGVTTV----------DNLDDGEELMATDHAMDilgFSNEEKYGCYKIVGAIMHFGNMKFKQKQREeqAE 148
Cdd:cd14882 198 GRNYRYLRIPPEVPPSklkyrrddpeGNVERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGY--AE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 149 AENTESADKACYLMGISSADLIKGLLHPRVKVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLDtrLARQ 228
Cdd:cd14882 273 LENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMS--FPRA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 229 FF-----IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPMG 303
Cdd:cd14882 351 VFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDG 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 304 ILSILEEecmfpkASDMSFKAKLYDNHIGkspnfQKPRPDKKRKYEAHFELVHYAGVVPYNIVGWLDKNKDPLNETVVVV 383
Cdd:cd14882 431 LFYIIDD------ASRSCQDQNYIMDRIK-----EKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIET 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 384 FQKSQNKLLGSLYENyvssssdeppkAGVKEKRKKAASFQTVSQvhkENLNKLMTNLRATQPHFVRCIIPNETKTPGAMD 463
Cdd:cd14882 500 MRSSLDESVKLMFTN-----------SQVRNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFH 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 464 AFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILnpaAIPDDKFVDSRKATEKLLnSLELDHSQYKFGHTKVFF 543
Cdd:cd14882 566 SEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFL 641
|
.
gi 2077626420 544 K 544
Cdd:cd14882 642 K 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
1-496 |
1.55e-39 |
|
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: 158.33 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14905 118 LESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-D 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVT-TVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGNMKFKQKQREeqaeaenTESADKAc 159
Cdd:cd14905 197 INSYHYLNQGGSiSVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 160 ylmgissadLIKGLLH----PRVKVGNEYMT-KGQNVEQVVYAVGALAKATYDRMFKWLVTRINKTLD-TRLARQffIGV 233
Cdd:cd14905 269 ---------LIESLSHnitfDSTKLENILISdRSMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKpTQYSHT--LGI 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 234 LDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKpmgILSILEEECM 313
Cdd:cd14905 338 LDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESK 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 314 FPKASDMSFKAKLyDNHIGKSPNFQKpRPDKkrkyeahFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNKLL- 392
Cdd:cd14905 415 NINSSDQIFLEKL-QNFLSRHHLFGK-KPNK-------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLf 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 393 ---------------------------------------GSLYENYVSSSSDEPPKAGVKEKRKKAASFQTVSQVHKENL 433
Cdd:cd14905 486 srdgvfninatvaelnqmfdakntakksplsivkvllscGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSST 565
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 434 NKLMTNlRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRICRKGFP----NRLLYADF 496
Cdd:cd14905 566 NKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
950-1701 |
3.76e-35 |
|
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: 146.74 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 950 LKLRRDLEEATLQHESTAAVLrKKHADTVAELGEQIDNLQRVKQKLEK-----------EKSEMKMEVDDLSSNIEYLTK 1018
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1019 NKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLE 1098
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1099 EETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLAIRLQEA 1178
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-SKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1179 EEAVeaahakcSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRnfDRILAEWKQKFEETQAELESSQKESRSLSTE 1258
Cdd:TIGR02168 406 EARL-------ERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1259 LFKLKNAYEES---LDNLETLKRENKNLQEEIA-------DLTDQISLSGKTIHELEKVKKALE---GEksDIQAAL--- 1322
Cdd:TIGR02168 477 LDAAERELAQLqarLDSLERLQENLEGFSEGVKallknqsGLSGILGVLSELISVDEGYEAAIEaalGG--RLQAVVven 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1323 -EEAEGALEH--EESKTLRIQLELSQIKAD----VERKLAEKDEEFENLRRNHQRAMDSMQATLD------AEAKARNEA 1389
Cdd:TIGR02168 555 lNAAKKAIAFlkQNELGRVTFLPLDSIKGTeiqgNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvLVVDDLDNA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1390 IRLRKKMEGDLN---------------------------EMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHN 1442
Cdd:TIGR02168 635 LELAKKLRPGYRivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1443 DDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEA 1522
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1523 VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKgGKKQIQKLEARVRELEG 1602
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELES 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1603 ELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYR-KVQHEL 1681
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTL 953
|
810 820
....*....|....*....|
gi 2077626420 1682 DDAEERADIAETQVNKLRSR 1701
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRR 973
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
1-542 |
8.62e-31 |
|
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: 131.50 E-value: 8.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKFIRIHFgPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLISlN 80
Cdd:cd14938 143 MEAFGNAKTVKNNNSSRFSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-N 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 81 PYDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNEEKYGCYKIVGAIMHFGN-------------MKFKQKQ----- 142
Cdd:cd14938 221 IENYSMLNNEKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGqniny 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 143 ---------REEQAEAENTESADKACYLMGISSADLIKGLLHPRVkVGNEYMTKGQNVEQVVYAVGALAKATYDRMFKWL 213
Cdd:cd14938 301 etilselenSEDIGLDENVKNLLLACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 214 VTRINK---TLDTRLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLD 290
Cdd:cd14938 380 IYKINEkctQLQNININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENID 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 291 LQACID-LIEKPMGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKRKyeAHFELVHYAGVVPYNIVGWL 369
Cdd:cd14938 460 NEPLYNlLVGPTEGSLFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFV 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 370 DKNKDPLNETVVVVFQKSQNKLLGSL--YENYVSSSS--DEPPKAGVKE-----KRKKAASFQTVSQVHKENLNKLMTNL 440
Cdd:cd14938 538 EKNIDILTNRFIDMVKQSENEYMRQFcmFYNYDNSGNivEEKRRYSIQSalklfKRRYDTKNQMAVSLLRNNLTELEKLQ 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 441 RATQPHFVRCIIPNETKTP-GAMDAFLVLHQLRCNGVLEGIRICRKGFPNRLLYADFKQRYRILNPaaipddkfvDSRKA 519
Cdd:cd14938 618 ETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEK 688
|
570 580
....*....|....*....|...
gi 2077626420 520 TEKLLNSLELDHSQYKFGHTKVF 542
Cdd:cd14938 689 VEALIKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
741-1671 |
1.65e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.54 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 741 KVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALD--DLQAEEDKVN--TLTKAKVKLEQQVDDLESSL 816
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELElaLLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 817 EQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEEL 896
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 897 EEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRkKHAD 976
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 977 TVAELGEQIDNLQRVKQKLEKEKSEMKMEvdDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRG 1056
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1057 RLQTENGELSRLLEEKESF---INQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRhdcdllreQY--EEEVEA 1131
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL--------QAvvVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1132 KGELQRTLSKANAEVAQWrtkYETDAIQRTeeleeakkKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDL----- 1206
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTF---LPLDSIKGT--------EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvl 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1207 -SIDLERANSAAAALDKKQRNF----DRILAEW--KQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRE 1279
Cdd:TIGR02168 627 vVDDLDNALELAKKLRPGYRIVtldgDLVRPGGviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1280 NKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEksdIQAALEEAEgaleheesktlRIQLELSQIKADVERKLAEKDE 1359
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAE---VEQLEERIA-----------QLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1360 EFENLRrnhqramdsmqatldaeakarnEAIRLRKKMEGDLNEMEIQLSHANRQAAEsqklvrqLQAQIKDLQIELDDTL 1439
Cdd:TIGR02168 773 AEEELA----------------------EAEAEIEELEAQIEQLKEELKALREALDE-------LRAELTLLNEEAANLR 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1440 RHNDDLKEQAAALERRNNLLLAEVEELRAALEQaergrklAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEV 1519
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1520 EEAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL----QMRLDEAEQIALKgGKKQIQKLEA 1595
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseeySLTLEEAEALENK-IEDDEEEARR 972
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1596 RVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSykrQFEEAEQQANSNL 1671
Cdd:TIGR02168 973 RLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE---RFKDTFDQVNENF 1045
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
624-1492 |
2.60e-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: 114.77 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 624 EKEMATLKEEFQKLKEALEKsevkRKELEEKQITM-IQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELM- 701
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKEL----KAELRELELALlVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 702 ERLEDEEEMNA------DLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKK 775
Cdd:TIGR02168 275 EVSELEEEIEElqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 776 ALQEAHQQALDDLQAEEDKVNTLTKAkvkLEQQVDDLESSLEQEKKIRMDLERAKRKLEGdlklTQESVMDLENDKQQLE 855
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLER----LEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 856 EKLKKKEFETSQlnSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVT 935
Cdd:TIGR02168 428 KKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 936 --AVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAelgeqIDNLQRVKQKLE--KEKSEMK---MEVDD 1008
Cdd:TIGR02168 506 egVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAflKQNELGRvtfLPLDS 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1009 LSSN-IEYLTKNKANAEKLCRTYEDQLSEAKSK--------------VDELQR--QLAEVSTQRGRLQTENGELSRllee 1071
Cdd:TIGR02168 581 IKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvVDDLDNalELAKKLRPGYRIVTLDGDLVR---- 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1072 KESFINQLSRGKTSFT----QTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVA 1147
Cdd:TIGR02168 657 PGGVITGGSAKTNSSIlerrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1148 QWRTKYETDAIQRTEELEEAKKKLAIRlqeaeeavEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNF 1227
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEI--------EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1228 DRILAEWKQKFEETQAELESSQKESRSLSTELfklknayeesldnlETLKRENKNLQEEIADLTDQISLSGKTIHELEKV 1307
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRL--------------EDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1308 KKALEGEKSDIQAALEEAEGALEheesktlriqlelsqikaDVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARN 1387
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELE------------------ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1388 EAIRLRKKMEGDLN-EMEIQLSHANRQAAESQKLvrqlQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEEL 1466
Cdd:TIGR02168 937 RIDNLQERLSEEYSlTLEEAEALENKIEDDEEEA----RRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDL 1012
|
890 900 910
....*....|....*....|....*....|
gi 2077626420 1467 RAALEQAERG----RKLAEQELLEATERVN 1492
Cdd:TIGR02168 1013 TEAKETLEEAieeiDREARERFKDTFDQVN 1042
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
631-1521 |
2.52e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.14 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 631 KEEFQKL---KEALEKSEVKRKELEeKQITMIQEKNDLSLHLQAEQDNLADAEErcDLLIKTKIQLEAKVKELMERLEDE 707
Cdd:TIGR02168 175 KETERKLertRENLDRLEDILNELE-RQLKSLERQAEKAERYKELKAELRELEL--ALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 708 EEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALDD 787
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 788 LQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQqleeklkkkefetsQ 867
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA--------------S 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 868 LNSRIEDEQVLGAQLQKKIKELQARIEeleeeleaeRAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREA 947
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIE---------ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 948 EFLKLRRDLEEATLQHESTAAVLrkkhaDTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLC 1027
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARL-----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1028 R-TYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEeetkskNA 1106
Cdd:TIGR02168 544 GgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR------KA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1107 LAHALQASRHDCDL-----LREQYEEE---VEAKGELQRT---LSKANAEVAQWRTKYET---DAIQRTEELEEAKKKLA 1172
Cdd:TIGR02168 618 LSYLLGGVLVVDDLdnaleLAKKLRPGyriVTLDGDLVRPggvITGGSAKTNSSILERRReieELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1173 IRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKES 1252
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1253 RSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLtdqislsGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHE 1332
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-------NEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1333 ESKTLRIQLELSQIKADvERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANR 1412
Cdd:TIGR02168 851 SEDIESLAAEIEELEEL-IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1413 QAAESQKLVRQLQAQIKDL-QIELDDTLRHNDDLKEQAAALERRnnlllaeVEELRAALEQAERGRKLAEQELLEATERV 1491
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRR-------LKRLENKIKELGPVNLAAIEEYEELKERY 1002
|
890 900 910
....*....|....*....|....*....|
gi 2077626420 1492 NLLHSQNTGLINHKKKIEADLAQLSSEVEE 1521
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1090-1711 |
1.39e-21 |
|
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: 102.44 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1090 IEELKRQLEE-ETKSKNALA-HALQA--SRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETdAIQRTEELE 1165
Cdd:TIGR02168 195 LNELERQLKSlERQAEKAERyKELKAelRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1166 EAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAEL 1245
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1246 ESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEA 1325
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1326 EGALEHEESKTLRIQLE-LSQIKADVERKLAEKDEEFENLR-------------RNHQRAMDSMQATLDAEAKARNEAIR 1391
Cdd:TIGR02168 434 ELKELQAELEELEEELEeLQEELERLEEALEELREELEEAEqaldaaerelaqlQARLDSLERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1392 LRKKMEGDLN--------------EMEIQL-----------SHANRQAAESQK---------------LVRQLQAQIKDL 1431
Cdd:TIGR02168 514 NQSGLSGILGvlselisvdegyeaAIEAALggrlqavvvenLNAAKKAIAFLKqnelgrvtflpldsiKGTEIQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1432 QIELDDTLRHNDDLKEQAAALERRNNLLLAE---VEELRAALEQA----------------------------------- 1473
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvVDDLDNALELAkklrpgyrivtldgdlvrpggvitggsaktnssil 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1474 ERGRKLAE--QELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQ 1551
Cdd:TIGR02168 674 ERRREIEEleEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1552 DTSAHLERMKKNMEQTIKDLQMRLDEAE------QIALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRV 1625
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEaeieelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1626 KELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRDV 1705
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
....*.
gi 2077626420 1706 ITSKHE 1711
Cdd:TIGR02168 914 RRELEE 919
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1028-1605 |
1.36e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1028 RTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNAL 1107
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1108 AHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYEtDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHA 1187
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1188 KCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLstelfklknaye 1267
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL------------ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1268 esLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRiqlelsqik 1347
Cdd:COG1196 462 --LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI--------- 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1348 aDVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRkkmegdlnemEIQLSHANRQAAESQKLVRQLQAQ 1427
Cdd:COG1196 531 -GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT----------FLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1428 IKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKK 1507
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1508 IEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGK 1587
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570
....*....|....*...
gi 2077626420 1588 KQIQKLEARVRELEGELD 1605
Cdd:COG1196 760 PDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1192-1699 |
2.08e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.47 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1192 LEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLD 1271
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1272 NLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVE 1351
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1352 RKLAEKDEEfENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDL 1431
Cdd:COG1196 397 ELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1432 QIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQA-----------ERGRKLAEQELLEATERVNLLHSQNTG 1500
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagavavLIGVEAAYEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1501 LINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTikdlqmRLDEAEQ 1580
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL------LGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1581 IALKGGKKQIQKLEARVRELEGELDIEQKKNAETqkgirkyERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQF 1660
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT-------GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510
....*....|....*....|....*....|....*....
gi 2077626420 1661 EEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLR 1699
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
951-1701 |
2.32e-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: 98.60 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 951 KLRRDLEEATLQHESTAAVLRkkhadtvaELGEQIDNLQRVKQKLEK----EKSEMKMEVDDLSSNIEYLTKNKANAEKL 1026
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1027 CRTYEDQLSEAKSKVDELQRQLAEVstqRGRLQTENGELSRLLEEKesfINQLSRGKTSFTQTIEELKRQLEEETKSKNA 1106
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEI---EQLLEELNKKIKDLGEEE---QLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1107 LAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYEtDAIQRTEELEEAKKKLAIRLQEAEEAVEAAH 1186
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE-DLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1187 AKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAY 1266
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1267 EESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDI-------QAALEEAEGA------LEHEE 1333
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryATAIEVAAGNrlnnvvVEDDA 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1334 SKTLRIQ------------LELSQIKA--------------DVERKLAEKDEEFENLRRNHQR---AMDSMQAtldaeak 1384
Cdd:TIGR02169 559 VAKEAIEllkrrkagratfLPLNKMRDerrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEA------- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1385 ARNEAIRLRK-KMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEV 1463
Cdd:TIGR02169 632 ARRLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1464 EELRAALEQAERGRKLAEQELLEATERvnllhsqntglinhkkkieadLAQLSSEVEEAVQECRNAEEKAKKAITDAAMM 1543
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKER---------------------LEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1544 AEELKKEQDTSAHLERMKKnmEQTIKDLQMRLDEAEqialkggkKQIQKLEARVRELEGEL-------DIEQKKNAETQK 1616
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQKLnrltlekEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1617 GIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVN 1696
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
....*
gi 2077626420 1697 KLRSR 1701
Cdd:TIGR02169 921 ELKAK 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1090-1701 |
1.71e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1090 IEELKRQLEE-ETKSKNAL-AHALQASRHDCDLLREQYEEEveakgELQRTLSKANAEVAQWRTKYEtDAIQRTEELEEA 1167
Cdd:COG1196 195 LGELERQLEPlERQAEKAErYRELKEELKELEAELLLLKLR-----ELEAELEELEAELEELEAELE-ELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1168 KKKLAIRLQEAEE-------AVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEE 1240
Cdd:COG1196 269 LEELRLELEELELeleeaqaEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1241 TQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQA 1320
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1321 ALEEAEGALEHEESKTLRIQLELSQIKADvERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDL 1400
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1401 nemeiqlshanrQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLA 1480
Cdd:COG1196 508 ------------EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1481 EQELLEATERvnllhsqntglinhkKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 1560
Cdd:COG1196 576 FLPLDKIRAR---------------AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1561 KKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDIEQKKNAETQkgiRKYERRVKELTYQTEEDRKNLA 1640
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAEEERL 717
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1641 RMQDLIDKLQSKVKSYKRQFEEAEQQANSNLvkyRKVQHELDDAEERADIAETQVNKLRSR 1701
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELL---EEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
622-1367 |
1.91e-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: 95.52 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 622 QTEKEMAtlkEEFQKLKEALEKSE----VKRKELEEKQITMIQEKndlslhLQAEQDNLADAEERCDLLIKTKIQLEAKV 697
Cdd:TIGR02169 204 RREREKA---ERYQALLKEKREYEgyelLKEKEALERQKEAIERQ------LASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 698 KELMERLED--EEEMNA------DLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAK 769
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 770 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN 849
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 850 DKQQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQ----RAEVARELEELS 925
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQarasEERVRGGRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 926 ERLEEAGGV----------------------------TAVQLEMNKKREAEFLKlRRDLEEATL-------QHESTAAVL 970
Cdd:TIGR02169 515 VLKASIQGVhgtvaqlgsvgeryataievaagnrlnnVVVEDDAVAKEAIELLK-RRKAGRATFlplnkmrDERRDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 971 RKKHA-----------------------DTV---------------------AELGEQ---IDNLQRVKQKLEKEKSEMK 1003
Cdd:TIGR02169 594 SEDGVigfavdlvefdpkyepafkyvfgDTLvvedieaarrlmgkyrmvtleGELFEKsgaMTGGSRAPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1004 MEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGK 1083
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1084 TSFTQTIEELKRQLEEETKSKNALAHALQasrhdcDLLREQYEEEVEakgELQRTLSKANAEVAQWRtkyetdaiQRTEE 1163
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIP---EIQAELSKLEEEVSRIE--------ARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1164 LEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQA 1243
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1244 ELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKnlqeEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQaALE 1323
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALE 971
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 2077626420 1324 EAEGALEHEESKTLRIQLELSQIKADVERK---LAEKDEEFENLRRN 1367
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
626-1172 |
6.88e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.46 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 626 EMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLE 705
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 706 DEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQAL 785
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 786 DDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFET 865
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 866 SQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTA--------- 936
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqniv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 937 VQLEMNKKREAEFLKlRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEmkmevdDLSSNIEYL 1016
Cdd:COG1196 553 VEDDEVAAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY------VLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1017 TKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGktsfTQTIEELKRQ 1096
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE----ELELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1097 LEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLA 1172
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-1306 |
1.58e-18 |
|
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: 92.81 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVK 698
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMNADLTSKKRKLEDECAELKKDidDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQ 778
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 779 EAHQQ------ALDDLQAEEDK----VNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAkrkLEGDLkltQESVMDLE 848
Cdd:TIGR02168 482 RELAQlqarldSLERLQENLEGfsegVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENL 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 849 NDKQQLEEKLKKKEFETSQLnsrIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEK-------QRAEVAREL 921
Cdd:TIGR02168 556 NAAKKAIAFLKQNELGRVTF---LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLD 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 922 EELSERLEEAGGVTAVQLEMNKKREAEFLKLRRDLEEATLQHESTAavlRKKHADTVAELGEQIDNLQRVKQKLEKEKSE 1001
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRRE---IEELEEKIEELEEKIAELEKALAELRKELEE 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1002 MKMEVDDL-------SSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKES 1074
Cdd:TIGR02168 710 LEEELEQLrkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1075 FINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYE 1154
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1155 TDAIQRT------EELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSaaaaldKKQRNFD 1228
Cdd:TIGR02168 870 ELESELEallnerASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV------RIDNLQE 943
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1229 RILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEE-------SLDNLETLKRENKNLQEEIADLTDQISLSGKTI 1301
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
....*
gi 2077626420 1302 HELEK 1306
Cdd:TIGR02168 1024 EEIDR 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
880-1687 |
2.90e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 880 AQLQKKIKELQARIEELeeeleaeraaRAKVEKQRAEVARELEELSErleeaggVTAVQLEMNKKREaeflKLRRDLEEA 959
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEF----------DRKKEKALEELEEVEENIER-------LDLIIDEKRQQLE----RLRREREKA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 960 tlqhESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKS 1039
Cdd:TIGR02169 211 ----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1040 -KVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDC 1118
Cdd:TIGR02169 287 eEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1119 DLLREQYEEEVEAKGELQRTLSkanaevaqwrtkyetdaiQRTEELEEAKKKLairlqeaeeaveaahakcSSLEKTKHR 1198
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELK------------------DYREKLEKLKREI------------------NELKRELDR 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1199 LQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKR 1278
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1279 ENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDI-------QAALEEAEGA------LEHEESKTLRIQ----- 1340
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrr 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1341 -------LELSQIKA--------------DVERKLAEKDEEFENLRRNHQR---AMDSMQA-----------TLDAE--- 1382
Cdd:TIGR02169 571 kagratfLPLNKMRDerrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfe 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1383 --------AKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALER 1454
Cdd:TIGR02169 651 ksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1455 RNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQlsSEVEEAVQECRNAEEKAK 1534
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVS 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1535 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDE-AEQIALKGGKK-----QIQKLEARVRELEGELDIEQ 1608
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLK 888
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1609 KKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEaEQQANSNLVKYRKVQHELDDAEER 1687
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDVQAELQRVEEE 966
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1021-1709 |
1.39e-17 |
|
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: 89.46 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1021 ANAEKLCRTYEDQLsEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEE 1100
Cdd:pfam01576 9 AKEEELQKVKERQQ-KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1101 TKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEeLEEAKKKLAIRLQEAEE 1180
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1181 AVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELF 1260
Cdd:pfam01576 167 NLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1261 KLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQ 1340
Cdd:pfam01576 247 AALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKRE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1341 LELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKL 1420
Cdd:pfam01576 327 QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1421 VRQLQAQIKDLQIELDDTLRHNDDLKEQAAALErrnnlllAEVEELRAALEQAE-RGRKLA------EQELLEATERVNL 1493
Cdd:pfam01576 407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQ-------SELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1494 LHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQM 1573
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1574 RLDEAEQialkggkkQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKlqskv 1653
Cdd:pfam01576 560 QLEEKAA--------AYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDR----- 626
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1654 ksykrqfeeAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRDVITSK 1709
Cdd:pfam01576 627 ---------AEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
1-484 |
4.42e-16 |
|
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: 84.41 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1 MEAFGNAKTLRNDNSSRFGKF--IRIHFGPSG---KLASADIDIYLLEKSRVIFQQ------PGERSYHIYYQILSG--- 66
Cdd:cd14894 256 LEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYAMVAGvna 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 67 --------KKPELQDM---LLISLNPYDYH---FCSQGVTTVDNLDDGEELMatdHAMDILGFSNEEKYGCYKIVGAIMH 132
Cdd:cd14894 336 fpfmrllaKELHLDGIdcsALTYLGRSDHKlagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 133 FGNMKFKQKQREEQAEAENT---ESADKACYLMGISSADLIKGLLHPR---VKVGNEYMTKGQNVEQVVYAVGALAKATY 206
Cdd:cd14894 413 LGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLARLLY 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 207 DRMFKWLVTRINKT--------------LDTRLARQFFIGVL---DIAGFEIFEYNSFEQLCINFTNEKL----QQFF-- 263
Cdd:cd14894 493 QLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKLyareEQVIav 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 264 ----NHHMFVLEQEEykkegiEWVFIdfgldlqacidlIEKPMGILSILEEECMFPKASDMS----------FKAKLYDN 329
Cdd:cd14894 573 ayssRPHLTARDSEK------DVLFI------------YEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRNIYDR 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 330 HIGKSPNFQKPRPDKKRKYEA-----HFELVHYAGVVPYNIVGWLDKNKDPLNETVVVVFQKSQNK-LLGSLYENYVSSS 403
Cdd:cd14894 635 NSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSShFCRMLNESSQLGW 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 404 SDEPPKAGVKEKRKKAASFQTVSQVHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDAFLVLHQLRCNGVLEGIRIC 483
Cdd:cd14894 715 SPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEIC 794
|
.
gi 2077626420 484 R 484
Cdd:cd14894 795 R 795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1092-1689 |
1.80e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1092 ELKRQLEEETKSKNALAHALQASRHDcdllREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEEL---EEAK 1168
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAE----EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKkkaDEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1169 KKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESS 1248
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1249 QKESRSLSTELFKLKNAyeeslDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKsdiqaaleEAEGA 1328
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKA-----DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK--------KAEEA 1443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1329 LEHEESKTLRIQLElsqiKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEaKARNEAIRLRKKMEGDLNEMEIQLS 1408
Cdd:PTZ00121 1444 KKADEAKKKAEEAK----KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1409 HANRQAAESQKLVRQLQAQikdlqielddtlrhnddlkEQAAALERRNNLLLAEVEELRAALEqaergRKLAEQELLEAT 1488
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKAD-------------------EAKKAEEKKKADELKKAEELKKAEE-----KKKAEEAKKAEE 1574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1489 ERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTI 1568
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1569 KDL-QMRLDEAEQIALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLID 1647
Cdd:PTZ00121 1647 KKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2077626420 1648 KLQSKVKSYKRQFEEAEQQANSNLV---KYRKVQHELDDAEERAD 1689
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
756-1580 |
1.97e-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: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 756 LIEEMAALDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKVN----TLTKAKVKLEQQVDDLESSLEQEKKIRM----DLE 827
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKRqqleRLRREREKAERYQALLKEKREYEGYELLkekeALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 828 RAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRI----EDEQVlgaQLQKKIKELQARIEELEEELEAE 903
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQL---RVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 904 RAARAKVEKQRAE-VARELEELSERLEEAGGVTAVQLEMNK------KREAEFLKLRRDLEEAtlqhESTAAVLRKKHAD 976
Cdd:TIGR02169 314 ERELEDAEERLAKlEAEIDKLLAEIEELEREIEEERKRRDKlteeyaELKEELEDLRAELEEV----DKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 977 TVAELGE----------QIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQR 1046
Cdd:TIGR02169 390 YREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1047 QLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELK----------RQL-----EEETKSKNALAHAL 1111
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvAQLgsvgeRYATAIEVAAGNRL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1112 QASRHDCDLLRE---QYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLairlQEAEEAVEAAHAK 1188
Cdd:TIGR02169 550 NNVVVEDDAVAKeaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY----EPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1189 CSSLEKTKhRLQTEIEDLSID---LERANSAAAALDKKQRNFDRILAEwKQKFEETQAELESSQKESRSLSTELFKLKNA 1265
Cdd:TIGR02169 626 VEDIEAAR-RLMGKYRMVTLEgelFEKSGAMTGGSRAPRGGILFSRSE-PAELQRLRERLEGLKRELSSLQSELRRIENR 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1266 YEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQ 1345
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1346 IKADVER-KLAEKDEEFENLRRNHQRAMDSMQATldaeakarneairlrkkmEGDLNEMEIQLSHANRQAAESQKLVRQL 1424
Cdd:TIGR02169 784 LEARLSHsRIPEIQAELSKLEEEVSRIEARLREI------------------EQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1425 QAQIKDLQIELDDTLRHNDDLKEQAAA-------LERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQ 1497
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEEleaalrdLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1498 NTGLINHKKKIEADLAQLSSEVE-----EAVQECRNAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKNMEQTIKDL 1571
Cdd:TIGR02169 926 LEALEEELSEIEDPKGEDEEIPEeelslEDVQAELQRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
....*....
gi 2077626420 1572 QMRLDEAEQ 1580
Cdd:TIGR02169 1006 LERIEEYEK 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
886-1525 |
4.23e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 886 IKELQARIeeleeeleaeraarAKVEKQrAEVAreleelserleeaggvtavqlemnkkreAEFLKLRRDLEEatLQHES 965
Cdd:COG1196 195 LGELERQL--------------EPLERQ-AEKA----------------------------ERYRELKEELKE--LEAEL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 966 TAAVLRKKHADtVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEyltknkanaeklcrTYEDQLSEAKSKVDELQ 1045
Cdd:COG1196 230 LLLKLRELEAE-LEELEAELEELEAELEELEAELAELEAELEELRLELE--------------ELELELEEAQAEEYELL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1046 RQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQAsrhdcdlLREQY 1125
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE-------AEEAL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1126 EEEVEAKGELQRTLSKANAEVAQwrtkyetdAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIED 1205
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLE--------ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1206 LSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQE 1285
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1286 EIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTL-------------RIQLELSQIKADVER 1352
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpldkiraRAALAAALARGAIGA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1353 KLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDL---NEMEIQLSHANRQAAESQKLVRQLQAQIK 1429
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRevtLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1430 DLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIE 1509
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
650
....*....|....*.
gi 2077626420 1510 ADLAQLSSEVEEAVQE 1525
Cdd:COG1196 760 PDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
697-1571 |
4.52e-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: 81.27 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 697 VKELMERLE---DEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATEnkVKNLIEEMAALDEIIAKLTKE 773
Cdd:TIGR02169 182 VEENIERLDliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ--KEAIERQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 774 KKALQEAHQQALDDLQAEEDKVNTLTKakvkleqqvddlESSLEQEKKIRmDLERAKRKLEGDLKLTQESVMDLENDKQQ 853
Cdd:TIGR02169 260 ISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 854 LEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGG 933
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 934 VTAVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKhADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNI 1013
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1014 EYLTKNKANAEKLCRTYEDQLSEAKSKVDELQ----------RQLAEVSTQR---------GRLQTENGELSRLLEEKES 1074
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvAQLGSVGERYataievaagNRLNNVVVEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1075 FINQLSRGKTSFTqTIEELKRQLEEETKSKNALAHALQASRHDCDllrEQYEEEVeaKGELQRTLSKANAEVAQwrtKYE 1154
Cdd:TIGR02169 566 LLKRRKAGRATFL-PLNKMRDERRDLSILSEDGVIGFAVDLVEFD---PKYEPAF--KYVFGDTLVVEDIEAAR---RLM 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1155 TDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKcsSLEKTKHRLQTEIEDLSIDLERansaaaaLDKKQRNFDRILAEW 1234
Cdd:TIGR02169 637 GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSR--SEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1235 KQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADltdqislsgktiheLEKVKKALEGE 1314
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE--------------LEARIEELEED 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1315 KSDIQAALEEAEGALEHEESKTLRIQL-ELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQatldaEAKARNEAIRLR 1393
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ-----ELQEQRIDLKEQ 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1394 KKMEGD-LNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELddtlrhnDDLKEQAAALERRNNLLLAEVEELRAALEQ 1472
Cdd:TIGR02169 849 IKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLKKER-------DELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1473 AERGRKLAEQELLEATERVNLLHSQNTGlinhkkkiEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD 1552
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
890
....*....|....*....
gi 2077626420 1553 TSAHLERMKKNMEQTIKDL 1571
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEY 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1127-1697 |
4.00e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1127 EEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDL 1206
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1207 SID---LERANSAAAALDKKqrnfdrilAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNL 1283
Cdd:PTZ00121 1367 EAAekkKEEAKKKADAAKKK--------AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1284 QEEIADLTDQISLSGKTIHELEKVKKALEgEKSDIQAALEEAEGALEHEESKTlriQLELSQIKADVERKLAEKDEEFEN 1363
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAKKADEAKK---KAEEAKKKADEAKKAAEAKKKADE 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1364 LRRNHQ--------RAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIEL 1435
Cdd:PTZ00121 1515 AKKAEEakkadeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1436 DDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINhkkkiEADLAQL 1515
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-----AAEEAKK 1669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1516 SSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEA 1595
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1596 RVRELEGElDIEQKKNAETQKGirKYERRVKELTYQTEEDRKNLARMQDlidkLQSKVKSYKRQFEEAEQQAN-SNLVKY 1674
Cdd:PTZ00121 1750 KKDEEEKK-KIAHLKKEEEKKA--EEIRKEKEAVIEEELDEEDEKRRME----VDKKIKDIFDNFANIIEGGKeGNLVIN 1822
|
570 580
....*....|....*....|...
gi 2077626420 1675 RKVQHELDDAEERADIAETQVNK 1697
Cdd:PTZ00121 1823 DSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1386-1701 |
1.12e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1386 RNEAIRLRKKMEGDLN-------EMEIQLSHANRQAAESQKlVRQLQAQIKDLQIELddTLRHNDDLKEQAAALErrnnl 1458
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELE----- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1459 llAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAIT 1538
Cdd:COG1196 246 --AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1539 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDIEQ------KKNA 1612
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaaaelaAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1613 ETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAE 1692
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
....*....
gi 2077626420 1693 TQVNKLRSR 1701
Cdd:COG1196 484 EELAEAAAR 492
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
615-1474 |
4.70e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 74.62 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 615 KPLLRSAQTEKEMATLKEeFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEErcdlliKTKIQLE 694
Cdd:pfam02463 150 MKPERRLEIEEEAAGSRL-KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQL------KEKLELE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 695 AKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEK 774
Cdd:pfam02463 223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 775 KALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAK---RKLEGDLKLTQESVMDLENDK 851
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 852 QQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEA 931
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 932 GGVTAVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLss 1011
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN-- 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1012 nieYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIE 1091
Cdd:pfam02463 541 ---YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1092 ELKRQLEEETKSKnalaHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTK-YETDAIQRTEELEEAKKK 1170
Cdd:pfam02463 618 DDKRAKVVEGILK----DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1171 laIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAEL----- 1245
Cdd:pfam02463 694 --ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKselsl 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1246 -------ESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQIS--LSGKTIHELEKVKKALEGEKS 1316
Cdd:pfam02463 772 kekelaeEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEkiKEEELEELALELKEEQKLEKL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1317 DIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKM 1396
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1397 EGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLL--LAEVEELRAALEQAE 1474
Cdd:pfam02463 932 KYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEleKERLEEEKKKLIRAI 1011
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1069-1580 |
5.82e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1069 LEEKESF--INQLsrgKTSFtQTIEELKRQLEEETKSKNALAHALQasrhdcdlLREQYEEEVEAKGELQRTLSKANAEV 1146
Cdd:COG4913 218 LEEPDTFeaADAL---VEHF-DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1147 AQwrTKYETdAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTE-IEDLSIDLERANSAAAALDKKQR 1225
Cdd:COG4913 286 AQ--RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1226 NFDRILAEWKQKFEETQAELESSQKESR----SLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTI 1301
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1302 HEL-EKVKKALEGEKSD-------IQAALEE------AEGAL-----------EHE-------ESKTLRIQLELSQIKAD 1349
Cdd:COG4913 443 LALrDALAEALGLDEAElpfvgelIEVRPEEerwrgaIERVLggfaltllvppEHYaaalrwvNRLHLRGRLVYERVRTG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1350 VE-------------RKLAEKDEEF--------------------ENLRRnHQRAM---------DSMQATLDAEAKARN 1387
Cdd:COG4913 523 LPdperprldpdslaGKLDFKPHPFrawleaelgrrfdyvcvdspEELRR-HPRAItragqvkgnGTRHEKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1388 -----EAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQ---------IELDDTLRHNDDLKEQAAALE 1453
Cdd:COG4913 602 yvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswdeIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1454 RRNnlllAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQntglinhKKKIEADLAQLSSEVEEAVQECRNAEEKA 1533
Cdd:COG4913 682 ASS----DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAAEDLARLELRAL 750
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2077626420 1534 kkaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQ 1580
Cdd:COG4913 751 ----------LEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
952-1651 |
1.00e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 952 LRRDLEEATLQHESTAAVlrKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVddLSSNIEYLTKNKANAEKLCRTYE 1031
Cdd:COG4913 240 AHEALEDAREQIELLEPI--RELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1032 DQLSEAKSKVDELQRQLAEVSTQRgrLQtengELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHAL 1111
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDR--LE----QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1112 QASRHDCDLLREQYEEEVeakGELQRTLSKANAEVAQWRTkyETDAIQRT-----EELEEAKKKLAIRLQEAEEAVEAAh 1186
Cdd:COG4913 390 AALLEALEEELEALEEAL---AEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELPFV- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1187 akCSSLE-KTKHRL-QTEIE--------DLSIDLERANSAAAALDK---KQR-NFDRIlaewkqkfEETQAELESSQKES 1252
Cdd:COG4913 464 --GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1253 RSLSTEL-FKLKNAYEEsldnletlkrenknLQEEIADLTDQISLSgkTIHELEKVKKAL--EGEKSDiqaaleeAEGAL 1329
Cdd:COG4913 534 DSLAGKLdFKPHPFRAW--------------LEAELGRRFDYVCVD--SPEELRRHPRAItrAGQVKG-------NGTRH 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1330 EHEESKTLRiqlELSQIKADVERKLAEKDEEFENLRRNHQRAmDSMQATLDAEAKARNEAIRLRKKMEgDLNEMEIQLSH 1409
Cdd:COG4913 591 EKDDRRRIR---SRYVLGFDNRAKLAALEAELAELEEELAEA-EERLEALEAELDALQERREALQRLA-EYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1410 ANRQAAE----------SQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKL 1479
Cdd:COG4913 666 AEREIAEleaelerldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1480 AEQELLEatERVNLLHSQNTgLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKK--------------AITDAAMMAE 1545
Cdd:COG4913 746 ELRALLE--ERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEYLALLD 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1546 ELkKEQDTSAHLERMK----KNMEQTIKDLQMRLDEAEQIAlkggKKQIQKLEARVRELE-GE-----LDIEQKKNAEtq 1615
Cdd:COG4913 823 RL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLEARPRPDPE-- 895
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 2077626420 1616 kgIRKYERRVKELT----YQTEEDR-KNLARMQDLIDKLQS 1651
Cdd:COG4913 896 --VREFRQELRAVTsgasLFDEELSeARFAALKRLIERLRS 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
619-1146 |
1.77e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEkndlslhLQAEQDNLADAEERCDLLIKTKIQLEAKVK 698
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQ 778
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 779 EAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQES-----------VMDL 847
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAlllaglrglagAVAV 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 848 ENDKQQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSER 927
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 928 LEEAGGVTAVQLEMnkkREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVD 1007
Cdd:COG1196 609 READARYYVLGDTL---LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1008 DLSSNIEYLTKNKANAEklcrtyEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFT 1087
Cdd:COG1196 686 ERLAEEELELEEALLAE------EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 1088 QTIEELKRQLEEETKSKNAL---------AHALQASRHdcDLLREQYEEEVEAKGELQRTLSKANAEV 1146
Cdd:COG1196 760 PDLEELERELERLEREIEALgpvnllaieEYEELEERY--DFLSEQREDLEEARETLEEAIEEIDRET 825
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
986-1685 |
2.04e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.69 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 986 DNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLaEVSTQRGRLQTENGEL 1065
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1066 SRLLEEKESFINQLSRgktsfTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQrTLSKANAE 1145
Cdd:TIGR00618 266 RARIEELRAQEAVLEE-----TQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA-AHVKQQSS 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1146 VAQWRTKYETDAIQRTEELEEAKKKLAIRLQeaeeaveaahaKCSSLEKTkHRLQTEIEDLSIDLERANSAAAALDKKQR 1225
Cdd:TIGR00618 340 IEEQRRLLQTLHSQEIHIRDAHEVATSIREI-----------SCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKELDILQR 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1226 NFDRILAEwKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISlSGKTIHELE 1305
Cdd:TIGR00618 408 EQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1306 KVKKALEGEKSDIQAALE-EAEGALEHEESKTLRIQL----------------ELSQIKADVERKLAEKDEEFENLRRNH 1368
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPcPLCGSCIHPNPARQDIDNpgpltrrmqrgeqtyaQLETSEEDVYHQLTSERKQRASLKEQM 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1369 QRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTlRHNDDLKEQ 1448
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ-QCSQELALK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1449 AAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERvnllhSQNTGLINHKKKIEADLAQLSSEVEEAVQECRN 1528
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ-----SEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1529 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQ---IQKLEARVRELEGELD 1605
Cdd:TIGR00618 720 FNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAEIQFFNRLREEDTH 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1606 IEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAE 1685
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
863-1697 |
5.42e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 863 FETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELeaeraarakvEKQRAEVARELEELSERLEEAGGVTAVQLEMN 942
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE----------DARKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 943 KKREAEflklrRDLEEATLQHE-STAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVddlssniEYLTKNKA 1021
Cdd:PTZ00121 1170 RKAEDA-----KKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAV-------KKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1022 NAEKLCRTYEDQLSEAKSKVDElqRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEET 1101
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEE--ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1102 KSKNALAHALQASRhDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEE---LEEAKKKLAIRLQEA 1178
Cdd:PTZ00121 1316 KADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKAD 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1179 EEAVEAAHAKCSSLE-KTKHRLQTEIEDLSIDLERANSAAAAldKKQRNFDRILAEWKQKFEETQAELESSQKESRSLST 1257
Cdd:PTZ00121 1395 EAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1258 ELFKLKNAYEESLDNLETLKRENKNLQEEiADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTL 1337
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1338 RIQLELSqiKADVERKLAEKDEEFENLRRNHQRAMDSMQAtldaeAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAES 1417
Cdd:PTZ00121 1552 KKAEELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1418 QKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQA----ERGRKLAEQELLEATERVNl 1493
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEALKKEAEEAKK- 1703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1494 lhsqntglINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQm 1573
Cdd:PTZ00121 1704 --------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR- 1774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1574 rlDEAEQIALKGGKKqiqKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKV 1653
Cdd:PTZ00121 1775 --KEKEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAF 1849
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 2077626420 1654 KSYKRQFEEAEQQANSNLVKYRKVQHELDDAEEraDIAETQVNK 1697
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE--EIEEADEIE 1891
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1236-1455 |
7.22e-12 |
|
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: 69.02 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1236 QKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEK 1315
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1316 SDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLaekdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKK 1395
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL----QYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1396 MEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERR 1455
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
690-1616 |
7.28e-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: 70.77 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 690 KIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAK 769
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 770 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDD-LESSLEQEKKIRMDLERAKRKLEGDLKLTQESVmdle 848
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKESEKEK---- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 849 ndkqqleeklkkkefetsqlnsriedeqvlgAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERL 928
Cdd:pfam02463 324 -------------------------------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 929 eeaggvtavqlemnKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDD 1008
Cdd:pfam02463 373 --------------EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEES 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1009 LSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRqlaEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQ 1088
Cdd:pfam02463 439 IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1089 TIEELKRQLEEETKSKNALAHALQASRHD----CDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEEL 1164
Cdd:pfam02463 516 IKDGVGGRIISAHGRLGDLGVAVENYKVAistaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1165 EEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLsidLERANSAAAALDKKQRNFDRILAEWKQKFEETQAE 1244
Cdd:pfam02463 596 VLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL---KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1245 LESSQKEsrslstelfKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEE 1324
Cdd:pfam02463 673 KELLEIQ---------ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1325 AEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAmDSMQATLDAEAKARNEAIRLRKKMEGDLNEME 1404
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE-EKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1405 IQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQEL 1484
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKEL 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1485 LEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAItdaamMAEELKKEQDTSAHLERMKKN- 1563
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRLLLAKEELGKVNl 977
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1564 ---MEQTIKDLQMRLDEAEQIALKGGKKQIQKL------EARVRELEGELDIEQKKNAETQK 1616
Cdd:pfam02463 978 maiEEFEEKEERYNKDELEKERLEEEKKKLIRAiieetcQRLKEFLELFVSINKGWNKVFFY 1039
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1123-1663 |
9.57e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 9.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1123 EQYEEEVEAKGELQRTLSKanaevaqwRTKYETDAIQRTEELE----EAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHR 1198
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKR--------RIERLEKFIKRTENIEelikEKEKELEEVLREINEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1199 LQT------EIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQaELESSQKESRSLSTELFKLKNAYEESLDN 1272
Cdd:PRK03918 230 VKEleelkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1273 LETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIqAALEEAEGALEHEESKTLRIQLELSQIKADVER 1352
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1353 KLAEKDEEFENLRRNHQRAMD---SMQATLDAEAKARNEAIRLRKKMEGD----------------LNEMEIQLSHANRQ 1413
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1414 AAESQKLVRQLQAQIKDLQIELDD--TLRHNDDLKEQAAALERRNNLLlaEVEELRAALEQAERGRKLAEQ------ELL 1485
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKesELIKLKELAEQLKELEEKLKKY--NLEELEKKAEEYEKLKEKLIKlkgeikSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1486 EATERVNLLHSQNTGLINHKKKIEADLAQLS-----------SEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKEQ 1551
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLkeleelgfesvEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1552 DTSAHLERMKKNMEQTIKDLQMRLDEAEQI----ALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKE 1627
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
570 580 590
....*....|....*....|....*....|....*.
gi 2077626420 1628 LTyQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEA 1663
Cdd:PRK03918 706 RE-KAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
624-1447 |
1.04e-11 |
|
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: 70.15 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 624 EKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQ-----------AEQDNLADAEERCDLLIKTKIQ 692
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 693 LEAKVKELMERLEDEEE-------------------MNADLTSKKRKLEDECAELKKDIDDLEltlAKVEKEKHATENKV 753
Cdd:pfam15921 182 HEGVLQEIRSILVDFEEasgkkiyehdsmstmhfrsLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 754 KNLIEE-MAALDEIIAKLTKEKKALQE----AHQQAlDDLQAEEDKVNTLTKAKVKL-EQQVDDLESSLEQekkIRMDLE 827
Cdd:pfam15921 259 ELLLQQhQDRIEQLISEHEVEITGLTEkassARSQA-NSIQSQLEIIQEQARNQNSMyMRQLSDLESTVSQ---LRSELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 828 RAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIedeQVLGAQLQKKIKELQARIEELEEELEAERAAR 907
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADLHKREKELSLEKEQNKRLWDRDTGNS 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 908 AKVEKQRAEVAREleelserleeaggvtavqlEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDN 987
Cdd:pfam15921 412 ITIDHLRRELDDR-------------------NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLES 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 988 LQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGElsr 1067
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE--- 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1068 lleekesfinqlsrgktsftqtIEELKRQLEEETKSknalahalqasrhdCDLLREQYEEEVEAKGELQRTLSKANAEVA 1147
Cdd:pfam15921 550 ----------------------CEALKLQMAEKDKV--------------IEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1148 QwrtkYETDAIQRTEELEEAKkklaIRLQEAEEAVEAAHAKCSSLEKTKHRLqteiedlsidlerANSAAAALdkkqrnf 1227
Cdd:pfam15921 594 Q----LEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLELEKVKL-------------VNAGSERL------- 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1228 dRILAEWKQKFEETQAELESSQKESRSLSTElfklknayeesldnLETLKRENKNLQEEIADLTDQISLSGKTIH-ELEK 1306
Cdd:pfam15921 646 -RAVKDIKQERDQLLNEVKTSRNELNSLSED--------------YEVLKRNFRNKSEEMETTTNKLKMQLKSAQsELEQ 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1307 VKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKAdVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKAR 1386
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF-LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA 789
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1387 NEAIRLR---KKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQielddtLRHNDDLKE 1447
Cdd:pfam15921 790 GELEVLRsqeRRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK------LQHTLDVKE 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
626-1303 |
1.82e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 626 EMATLKEEFQKLKEALEKSEVKRKELEEK--QITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKiqlEAKVKELMER 703
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKaeDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAE---EAKKDAEEAK 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 704 LEDEEEMN--------ADLTSKKRKLEDECAELKKDIDDLElTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKK 775
Cdd:PTZ00121 1244 KAEEERNNeeirkfeeARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 776 ALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLE 855
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 856 EKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAeraarakveKQRAEVARELEELSERLEEAGGVT 935
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---------KKKAEEAKKAEEAKKKAEEAKKAD 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 936 AVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKhadtvaelGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEy 1015
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--------ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE- 1544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1016 ltknKANAEKLCRTYEDQLSEAKSKVDELQRQlaevsTQRGRLQTENGELSRLLEEKEsFINQLSRGKTSFTQTIEELKR 1095
Cdd:PTZ00121 1545 ----KKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK 1614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1096 qlEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQ----RTEELEEAKKKL 1171
Cdd:PTZ00121 1615 --AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAE 1692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1172 AIRLQEAEEAVEAAHAKCSSLEKTK-HRLQTEIEDLSIDLERAnsaaaaldKKQRNFDRILAEWKQKFEETQAELESSQK 1250
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1251 ESRSLSTELFKLKNAYEEsldnlETLKRENKNLQEEIADLTDQISLSGKTIHE 1303
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
804-1487 |
4.04e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 804 KLEQQVDDLESSLEQEKKIRMDLERAKRKLE--GDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDEQVlgAQ 881
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 882 LQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEmnkKREAEFLKLRRDLEEATL 961
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERE---RRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 962 QHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNK----ANAEKLCRTYEDQLSEA 1037
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1038 KSKV------------DELQRQLAE--VSTQRGRLQTENGELSRLLEekesFINQLSRGKTSFTQTIEELKRQLEEETKS 1103
Cdd:COG4913 457 EAELpfvgelievrpeEERWRGAIErvLGGFALTLLVPPEHYAAALR----WVNRLHLRGRLVYERVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1104 KNALAHALQASRHDC-DLLREQYEEE-----VEAKGELQRTlSKA---NAEVAQWRTKYETDAIQRTEEL----EEAKKK 1170
Cdd:COG4913 533 PDSLAGKLDFKPHPFrAWLEAELGRRfdyvcVDSPEELRRH-PRAitrAGQVKGNGTRHEKDDRRRIRSRyvlgFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1171 LAIrlqeaeeaveaahakcssLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIlaewkQKFEETQAELESSQK 1250
Cdd:COG4913 612 LAA------------------LEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1251 ESRSLSTELFKLknayEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALE 1330
Cdd:COG4913 669 EIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1331 HEESKTL--------------RIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKM 1396
Cdd:COG4913 745 LELRALLeerfaaalgdaverELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRL 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1397 EGD-LNEMEIQLSHANRQAAESQK--LVRQLQAQIKDLQIELD---DTLRH---NDDLKEQAAALERRNnlllAEVEELR 1467
Cdd:COG4913 825 EEDgLPEYEERFKELLNENSIEFVadLLSKLRRAIREIKERIDplnDSLKRipfGPGRYLRLEARPRPD----PEVREFR 900
|
730 740
....*....|....*....|
gi 2077626420 1468 AALEQAERGRKLAEQELLEA 1487
Cdd:COG4913 901 QELRAVTSGASLFDEELSEA 920
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1022-1682 |
1.19e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.67 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1022 NAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQtengELSRLLEEKESFINQLSRGKtsftqtiEELKRQLEEET 1101
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQ----ENRKIIEAQRKAIQELQFEN-------EKVSLKLEEEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1102 KSKNALAHALQASRHDCDLLRE--------------QYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEA 1167
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1168 KKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELES 1247
Cdd:pfam05483 221 HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1248 sqkesrslstelfkLKNAYEESLDNLETLKRENKNLQEEIADLTDQislSGKTIHELEKVKKALEGEKSDIQAALEEAEG 1327
Cdd:pfam05483 301 --------------IKMSLQRSMSTQKALEEDLQIATKTICQLTEE---KEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1328 ALEHEESKTLRIQLELSQIKADVERKLAEKdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEgdlnemEIQl 1407
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ELK- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1408 shanrqaAESQKLVRQLQAQIKDLQielddtlrhndDLKEQAAALERRNNLLLAEVEELRAALEQaergRKLAEQELLEA 1487
Cdd:pfam05483 436 -------GKEQELIFLLQAREKEIH-----------DLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAH 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1488 TERVNL----LHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD-TSAHLERMKK 1562
Cdd:pfam05483 494 CDKLLLenkeLTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDeVKCKLDKSEE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1563 NMEQTIKDLQMRLDEAEQIALKGG--KKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLA 1640
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2077626420 1641 RMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELD 1682
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
716-1349 |
1.41e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 716 SKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALD----EIIAKLTKEKKALQEAHQqaldDLQAE 791
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikDLNDKLKKNKDKINKLNS----DLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 792 EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSR 871
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 872 IEDEQVLGAQLQKKIKELQArieeleeeleaeraaraKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKrEAEFLK 951
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKK-----------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-TTEISN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 952 LRRDLEEATLQHESTAAVLRKKHADtVAELGEQIDNLQRVKQKLEKEKSEMKME-VDDLSSNIEYLTKNKanaEKLCRTY 1030
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKE-LEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQ---EKKLEEI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1031 EDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIE-------ELKRQLEEETKS 1103
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqinDLESKIQNQEKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1104 KNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYE------TDAIQRTEELEEAKKKLAIRLQE 1177
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1178 AEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQ--KESRSL 1255
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEK 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1256 STELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESK 1335
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
650
....*....|....
gi 2077626420 1336 TLRIQLELSQIKAD 1349
Cdd:TIGR04523 647 VKQIKETIKEIRNK 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
619-1289 |
1.83e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSlhlqaeqdNLADAEERCDLLIKTKIQLEAKVK 698
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK--------KKAEEAKKADEAKKKAEEAKKKAD 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMN--ADLTSKKRKLEDECAELKKDIDDLEltlaKVEKEKHATENKVKnlIEEMAALDEIIAKLTKEKKA 776
Cdd:PTZ00121 1333 AAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 777 LQEAHQQALDDLQAEEdkvntlTKAKVKLEQQVDDLESSLEQEKKIrmdlERAKRKLEGDLKLTQESVMDLENDKQQLEE 856
Cdd:PTZ00121 1407 ADELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 857 KLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRaevARELEELSERLEEAGGVTA 936
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 937 VQlEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEyl 1016
Cdd:PTZ00121 1554 AE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE-- 1630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1017 TKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQ 1096
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1097 LEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANaEVAQWRTKYETDAIQRTEEL-----EEAKKKL 1171
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEIRKEKeavieEELDEED 1789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1172 AIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRilAEWKQKFEETQAELESSQKE 1251
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD--AFEKHKFNKNNENGEDGNKE 1867
|
650 660 670
....*....|....*....|....*....|....*...
gi 2077626420 1252 SRSlSTELFKLKNAYEESLDNLETLKRENKNLQEEIAD 1289
Cdd:PTZ00121 1868 ADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
993-1584 |
2.80e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 993 QKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEk 1072
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1073 esfinqlsrgktsftqtIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANA--EVAQWR 1150
Cdd:PRK03918 240 -----------------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1151 TKYEtDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRI 1230
Cdd:PRK03918 303 EEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1231 ----LAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRE-------NKNLQEE-----IADLTDQI 1294
Cdd:PRK03918 382 tgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcGRELTEEhrkelLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1295 SLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVErKLAEKDEEFENLRRNhQRAMDS 1374
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEK-LIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1375 MQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQ-KLVRQLQAQIKDLQ-------------IELDDTLR 1440
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkdaeKELEREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1441 HNDDLKEQAAALERRNNLLLAEVEELRAALEQAERG-----RKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQL 1515
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1516 SSEVEEavqecrnaEEKAKKaitdaammaeELKKeqdtsahLERMKKNMEQTIKDLQMRLDEAEQIALK 1584
Cdd:PRK03918 700 KEELEE--------REKAKK----------ELEK-------LEKALERVEELREKVKKYKALLKERALS 743
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
882-1639 |
2.96e-10 |
|
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: 65.52 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 882 LQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAggvTAVQLEMNKKREAEFLKLRRDLeeatL 961
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA---KCLKEDMLEDSNTQIEQLRKMM----L 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 962 QHESTAAVLRKKHADTvaelgeqidnlqrvkqkleKEKSEMKMEVDDLSSNIEYLTKNKAnAEKLCRTYEDQLSEAKSKV 1041
Cdd:pfam15921 181 SHEGVLQEIRSILVDF-------------------EEASGKKIYEHDSMSTMHFRSLGSA-ISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1042 DELQRQLAEVSTQRGR-----LQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLE---EETKSKNA------- 1106
Cdd:pfam15921 241 FPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqEQARNQNSmymrqls 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1107 -LAHALQASRHDCDLLREQYEEEVEakgELQRTLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLAIRLQEAEEAVEAA 1185
Cdd:pfam15921 321 dLESTVSQLRSELREAKRMYEDKIE---ELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKREKELSLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1186 HAKCSSL-------EKTKHRLQTEIEDLSIDLERANSAAAALDKKQRnfdrilAEWKQKFEETQAELESSQKESrSLSTE 1258
Cdd:pfam15921 397 KEQNKRLwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ------GQMERQMAAIQGKNESLEKVS-SLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1259 LFKLKNAYEESLDNLETLKRENKNLQEEIADLTdqislsgKTIHELEKVKKALEGEKSDIQAALEEAEGALEH---EESK 1335
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLT-------ASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknEGDH 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1336 TLRIQLELSQIKAdverKLAEKDEEFENLRRNhqraMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAA 1415
Cdd:pfam15921 543 LRNVQTECEALKL----QMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1416 ESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERV---- 1491
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMettt 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1492 NLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEK--AKKAITDAAMMAEELKKEQDTSAHLER--MKKNMEQT 1567
Cdd:pfam15921 695 NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQitAKRGQIDALQSKIQFLEEAMTNANKEKhfLKEEKNKL 774
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1568 IKDLQMRLDEAEQIA--LKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNL 1639
Cdd:pfam15921 775 SQELSTVATEKNKMAgeLEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKEL 848
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1199-1712 |
3.35e-10 |
|
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: 65.20 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1199 LQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQkESRSLSTELFKLKNAYEESLDNLET--- 1275
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCA-EAEEMRARLAARKQELEEILHELESrle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1276 --------LKRENKNLQEEIADLTDQISlsgktihELEKVKKALEGEKSDIQA---ALEEAEGALEHEESKTLRIQLELS 1344
Cdd:pfam01576 86 eeeersqqLQNEKKKMQQHIQDLEEQLD-------EEEAARQKLQLEKVTTEAkikKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1345 QIKADVERKLAEKDEEFENL---RRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMeiqlshaNRQAAESQKLV 1421
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLsklKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDL-------QEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1422 RQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQelleatervnllhsqntgl 1501
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEK------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1502 inHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLERMKKNMEQTIKDLQMRLDEAEQ 1580
Cdd:pfam01576 293 --QRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRShEAQLQEMRQKHTQALEELTEQLEQAKR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1581 iALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELtyqteedrknlarmqdlidklQSKVKSYKRQF 1660
Cdd:pfam01576 371 -NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL---------------------QARLSESERQR 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1661 EEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRDVITSKHEE 1712
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1190-1661 |
3.60e-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: 65.04 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1190 SSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEES 1269
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1270 LDNleTLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDiqaaleeaegalehEESKTLRIQLELSQIKAD 1349
Cdd:TIGR04523 308 WNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN--------------SESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1350 VERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKmEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIK 1429
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL-QQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1430 DLQIELDDTLRHNDDLKEQAAALERrnnlllaEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIE 1509
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1510 ADLAQLSSEVEEAVQECRNAEEKAKKaitdaamMAEELKKEQdtsahLERMKKNMEQTIKDLqmrldeaeqialkggKKQ 1589
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNK-------DDFELKKEN-----LEKEIDEKNKEIEEL---------------KQT 576
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1590 IQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFE 1661
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
618-1503 |
4.43e-10 |
|
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: 64.81 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 618 LRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADaEERCDLLIKTKI-QLEAK 696
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 697 VKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEkekhatenkvknlieemaaldeiiakltKEKKA 776
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALE----------------------------EGKKR 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 777 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKltqesvmdlendkqqlee 856
Cdd:pfam01576 550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA------------------ 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 857 klkkkefetsqlnsrieDEQVLGAQLQKkikelqarieeleeeleaeraarakvEKQRAEVAReleelserleeaggvta 936
Cdd:pfam01576 612 -----------------EEKAISARYAE--------------------------ERDRAEAEA----------------- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 937 vqlemnKKREAEFLKLRRDLEEAtlqhestaavlrkkhadtvaelgeqidnlQRVKQKLEKEKSEMKMEVDDLSSNIEYL 1016
Cdd:pfam01576 632 ------REKETRALSLARALEEA-----------------------------LEAKEELERTNKQLRAEMEDLVSSKDDV 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1017 TKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTengelsrlleekesfinqlsrgktsftqTIEELKRQ 1096
Cdd:pfam01576 677 GKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV----------------------------NMQALKAQ 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1097 LEEETKSKNalahalqasrhdcdllrEQYEEEveakgelQRTLSKanaEVAQWRTKYETDAIQRTEELeEAKKKLAIRLQ 1176
Cdd:pfam01576 729 FERDLQARD-----------------EQGEEK-------RRQLVK---QVRELEAELEDERKQRAQAV-AAKKKLELDLK 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1177 EAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAaaldkkqrnfDRILAEWKQkfeetqaelesSQKESRSLS 1256
Cdd:pfam01576 781 ELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASR----------DEILAQSKE-----------SEKKLKNLE 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1257 TELFKLKnayeeslDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKT 1336
Cdd:pfam01576 840 AELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1337 LRIQLELSQIKADV--ERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAirLRKKMEGDLNEMEIQLSHANRQA 1414
Cdd:pfam01576 913 RKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQLEEQLEQESRER 990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1415 AESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLL 1494
Cdd:pfam01576 991 QAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESM 1070
|
....*....
gi 2077626420 1495 HSQNTGLIN 1503
Cdd:pfam01576 1071 NREVSTLKS 1079
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
608-1371 |
5.11e-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: 64.61 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 608 MKLFFKIKPLLRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLA---------D 678
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllklerrkvD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 679 AEERCDLLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIE 758
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 759 EMAALDEIIAKLTKEKKALQEAHQQALDDLQA----EEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE 834
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEekkeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 835 GDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDEQVLGAQLqKKIKELQARIEELEEELEAERAARAKVEKQR 914
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDG-VGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 915 AEVARELEELSERLEEAGGVTAVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQK 994
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 995 LEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLS--EAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEK 1072
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELtkELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1073 ESFINQLSRGKtsftqtIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTK 1152
Cdd:pfam02463 711 ELKKLKLEAEE------LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1153 YETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILA 1232
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1233 EWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIAdltDQISLSGKTIHELEKVKKALE 1312
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIE---ERIKEEAEILLKYEEEPEELL 941
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1313 GEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRA 1371
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
659-1290 |
7.55e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 659 IQEKNDLSLH--LQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLEDEEEmnadltskKRkleDECAELKKDIDDLE 736
Cdd:PRK02224 196 IEEKEEKDLHerLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE--------RR---EELETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 737 LTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKkALQEAHQQALDDLQAEedkvntltkakvkLEQQVDDLESSL 816
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARREE-------------LEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 817 EQEkkiRMDLERAKRKLEGdlklTQESVMDLENDKQQLEEklkkkefETSQLNSRIEDEQVLGAQLQKKIKELQARIEEL 896
Cdd:PRK02224 331 EEC---RVAAQAHNEEAES----LREDADDLEERAEELRE-------EAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 897 EEELEAERAARAKVEKQRAEVARELEELSERLEeaggvtavQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHAD 976
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREA--------ELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 977 TVAELGEQIDnlqrvkqKLEKEKSEMKMEVDDLSSNIEYLTknkanaeklcrtyedqlseakskvdelqrQLAEVSTQRG 1056
Cdd:PRK02224 469 TIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAE-----------------------------DLVEAEDRIE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1057 RLQTENGELSRLLEEKESfinqlsrgktsftqTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQ 1136
Cdd:PRK02224 513 RLEERREDLEELIAERRE--------------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1137 RTLSKANAEVAQWRTKYETDAiqRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSA 1216
Cdd:PRK02224 579 SKLAELKERIESLERIRTLLA--AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKE 656
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 1217 AAalDKKQRNFDRILAEWKQKFEETQAE---LESSQKESRSLSTELfklkNAYEESLDNLETLKRENKNLQEEIADL 1290
Cdd:PRK02224 657 RA--EEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERR----EALENRVEALEALYDEAEELESMYGDL 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
619-1233 |
1.03e-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: 63.55 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVK 698
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDE-------IIAKLT 771
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLG 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 772 KEKKALQEAHQQAL----------DDLQAEED--------------------KVNTLTKAKVKLEQQVDDLESSLEQEKK 821
Cdd:TIGR02169 532 SVGERYATAIEVAAgnrlnnvvveDDAVAKEAiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPK 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 822 IR-------------MDLERAKR--------KLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDEQVLGA 880
Cdd:TIGR02169 612 YEpafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELS 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 881 QLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEaggVTAVQLEMNKKREAEFLKLRrDLEEAT 960
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE---LEEDLSSLEQEIENVKSELK-ELEARI 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 961 LQHESTAAVLRKKHADTVAELG-EQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKS 1039
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1040 KVDELQRQLAEVSTQRGRLQTE-----------NGELSRLLEEKESFINQLSRGKtsftQTIEELKRQLEEETKSKNALA 1108
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEEleeleaalrdlESRLGDLKKERDELEAQLRELE----RKIEELEAQIEKKRKRLSELK 923
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1109 HALQASRHDCDLLREQYEEEVEAKGELQ--RTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLairlqeaeeaveaah 1186
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL--------------- 988
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1187 akcSSLEKTKHRLQTEIEDL-----SIDLERANSAAAALDKKQRNFDRILAE 1233
Cdd:TIGR02169 989 ---DELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1348-1704 |
1.16e-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: 63.55 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1348 ADVERKLAEKDEEFENLRRNHQRA---MDSMQATLDAEAKARNEAIRLrKKMEGDLNEMEIQLSHANRQAAESQKlvRQL 1424
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLdliIDEKRQQLERLRREREKAERY-QALLKEKREYEGYELLKEKEALERQK--EAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1425 QAQIKDLQIELDDtlrhnddLKEQAAALERRNNLLLAEVEELraaleqAERGRKLAEQELLEATERVNLLHSQntglinh 1504
Cdd:TIGR02169 243 ERQLASLEEELEK-------LTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGELEAE------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1505 KKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEqialk 1584
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD----- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1585 ggkKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAE 1664
Cdd:TIGR02169 378 ---KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1665 QQANSNL--------------VKYRKVQHELDDAEERADIAETQVNKLRSRTRD 1704
Cdd:TIGR02169 455 WKLEQLAadlskyeqelydlkEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1253-1696 |
1.20e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1253 RSLSTELFKLKNAYEEsldnLETLKRENKNLqEEIADLTDQISLSGKTIHELEKVKKALEGEKSdiQAALEEAEGALEHE 1332
Cdd:COG4913 228 DALVEHFDDLERAHEA----LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1333 ESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANR 1412
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1413 QAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQA-----------AALERRNNLLLAEVEELRAALEQAergRKLAE 1481
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrrelreleaeiASLERRKSNIPARLLALRDALAEA---LGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1482 Q------ELLE----------ATERVnlLHSQNTGLI--------------NHKKKIEADLAQLSSEVEEAVQE------ 1525
Cdd:COG4913 458 AelpfvgELIEvrpeeerwrgAIERV--LGGFALTLLvppehyaaalrwvnRLHLRGRLVYERVRTGLPDPERPrldpds 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1526 ----------------------------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTIKDL 1571
Cdd:COG4913 536 lagkldfkphpfrawleaelgrrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1572 QMRLDEAEQiALKGGKKQIQKLEARVRELEGELDIEQK--KNAETQKGIRKYERRVKELtyqtEEDRKNLARMQDLIDKL 1649
Cdd:COG4913 616 EAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAAL 690
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2077626420 1650 QSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVN 1696
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
618-1104 |
1.43e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 618 LRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEK--QITMIQEKNDLSLHLQAEQDNLADAEERcdlLIKTKIQLEA 695
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEEYLDELRE---IEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 696 KVKELMERLEDEEEMNadltSKKRKLEDECAELKKDIDDLEltlakvekEKHATENKVKNLIEEMAALDEIIAKLTKEKk 775
Cdd:PRK03918 322 EINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTGLTPEK- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 776 alqeahqqALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE-GDLKLTQESVMDLENDKQQL 854
Cdd:PRK03918 389 --------LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvCGRELTEEHRKELLEEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 855 EEKLKKKEFETSQLNSRIEDEQVlgaQLQKKIKElQARIEELEEELEAERAARAKVEKQRAE-VARELEELSERLEEAGG 933
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELR---ELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 934 VTAVQLEMNK--KREAEFLKLRRDLEEATLQHESTAA----VLRKKHADTVAELGEQIDNLQR----------VKQKLEK 997
Cdd:PRK03918 537 LKGEIKSLKKelEKLEELKKKLAELEKKLDELEEELAellkELEELGFESVEELEERLKELEPfyneylelkdAEKELER 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 998 EKSEMKMEVDDLSSNIEYLTKNKANAEKLcrtyEDQLSEAKSKVDELQRQlaevstqrgRLQTENGELSRLLEEKESFIN 1077
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEEL----RKELEELEKKYSEEEYE---------ELREEYLELSRELAGLRAELE 683
|
490 500
....*....|....*....|....*..
gi 2077626420 1078 QLSRGKTSFTQTIEELKRQLEEETKSK 1104
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAK 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1127-1712 |
1.72e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1127 EEVEAKGELQRTLSKANAEVAqwRTKYETDAIQRTEELEEAKKKLAIRlQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDL 1206
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAA--RKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1207 SIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFK---LKNAYEESLDNLETLKRENKNL 1283
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKKADAAKKKAEEA 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1284 QEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEG-ALEHEESKTLRIQLELSQIKADVERKLAEKDEEFE 1362
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1363 NLRRNHQRAMDSMQATLDAEAKARNEaiRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHN 1442
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1443 DDLKEQAAALERRNNLLLAE----VEELRAALE--QAERGRKLAEQELLEATERVN-LLHSQNTGLINHKKKIEADLAQL 1515
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEeakkADEAKKAEEakKADEAKKAEEKKKADELKKAEeLKKAEEKKKAEEAKKAEEDKNMA 1579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1516 SSEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkggkkqiqkle 1594
Cdd:PTZ00121 1580 LRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK------------ 1647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1595 arvrelegelDIEQKKNAETQKGIRKYERRVKEltyqtEEDrknlarmqdlidklqskvksyKRQFEEAEQQANSNlvky 1674
Cdd:PTZ00121 1648 ----------KAEELKKAEEENKIKAAEEAKKA-----EED---------------------KKKAEEAKKAEEDE---- 1687
|
570 580 590
....*....|....*....|....*....|....*...
gi 2077626420 1675 RKVQHELDDAEERADIAETQVNKLRSRTRDVITSKHEE 1712
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
625-1171 |
1.97e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 625 KEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERL 704
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 705 EDEEEMNADLtskkRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKnLIEEMAALDEIIAKLTKEKKALQE---AH 781
Cdd:PRK03918 252 GSKRKLEEKI----RELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEeinGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 782 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEgdlKLTQESVMDLENDKQQLEEKLKKK 861
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKK---RLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 862 EFETSQLNSRIEDEQVLGAQLQKKIKELQA---------RIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEag 932
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE-- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 933 gvtAVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVlrkkhadtvaelgeqidNLQRVKQKlEKEKSEMKMEVDDLSSN 1012
Cdd:PRK03918 482 ---LRELEKVLKKESELIKLKELAEQLKELEEKLKKY-----------------NLEELEKK-AEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1013 IEYLTKNKANAEKLcrtyEDQLSEAKSKVDELQRQLAEVSTQRGRLQTEN-GELSRLLEEKESFINQLSRGKTSFTQTIE 1091
Cdd:PRK03918 541 IKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDAEKELER 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1092 ELKRQLEEETKSKNALAH------ALQASRHDCDLLR-----EQYEEEVEAKGELQRTLSKANAEVAQWRTKYET----- 1155
Cdd:PRK03918 617 EEKELKKLEEELDKAFEElaetekRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRREEikktl 696
|
570
....*....|....*..
gi 2077626420 1156 -DAIQRTEELEEAKKKL 1171
Cdd:PRK03918 697 eKLKEELEEREKAKKEL 713
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
625-1548 |
2.04e-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: 62.76 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 625 KEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKnDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERL 704
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 705 EDEEEMNADLTSKKRKLEDECAELKKDIDdleltlakvekekHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAH--- 781
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 782 --QQALDDLQAEEDKVNTLTKAKVKLEQQ----VDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLE 855
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 856 EKLKKKEFETSQLNSRIEDEQVLgaqLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVT 935
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 936 AVQLEmNKKREAEFLKLRRDLEEATLQHESTA-----AVLRKK-------------HADTVAELGEQIDN---LQRVKQK 994
Cdd:TIGR00606 503 VKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTrtqmeMLTKDKmdkdeqirkiksrHSDELTSLLGYFPNkkqLEDWLHS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 995 LEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLS-------------EAKSKVDELQRQLAEVSTQRGRLQTE 1061
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfdvcgsqDEESDLERLKEEIEKSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1062 NGELSRLLEEKES----------FINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEA 1131
Cdd:TIGR00606 662 TAVYSQFITQLTDenqsccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1132 K----GELQRTLSKANAEVAQWRTKYETDAIQRteELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEdlS 1207
Cdd:TIGR00606 742 KekeiPELRNKLQKVNRDIQRLKNDIEEQETLL--GTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ--G 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1208 IDLERAnsaAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKN---AYEESLDNLETLKRENKNLQ 1284
Cdd:TIGR00606 818 SDLDRT---VQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELS 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1285 EEIADLTDQISLSGKTIHELEKVKKALEGEKsdiqaaleeaEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENL 1364
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEKDQQEK----------EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI 964
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1365 RRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMeiqlshanRQAAESQKLV-RQLQAQIKDLQIElddtlrhnD 1443
Cdd:TIGR00606 965 QDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLM--------RQDIDTQKIQeRWLQDNLTLRKRE--------N 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1444 DLKEqaaaLERRNNLLLAEVEELRAaLEQAERGRKLaEQELLEATERVNLLHSQNTGLINHKKKIEADLAQlsseveeav 1523
Cdd:TIGR00606 1029 ELKE----VEEELKQHLKEMGQMQV-LQMKQEHQKL-EENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--------- 1093
|
970 980
....*....|....*....|....*
gi 2077626420 1524 QECRNAEEKAKKAITDAAMMAEELK 1548
Cdd:TIGR00606 1094 PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
767-1706 |
2.54e-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: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 767 IAKLTKEKKALQEAHQ------QALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLT 840
Cdd:TIGR00606 178 IFSATRYIKALETLRQvrqtqgQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 841 QE---SVMDLENDKQQLEEKLKKKEFETSQLNS-RIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAE 916
Cdd:TIGR00606 258 EHnlsKIMKLDNEIKALKSRKKQMEKDNSELELkMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 917 VARELEELSERLEEAGGVTAVQLEMNKKREAEFLKLRRDLEEATLQHEstaavlrkkhadtvAELGEQIDNLQRVKQKLE 996
Cdd:TIGR00606 338 LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERG--------------PFSERQIKNFHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 997 KEKSEMkmevddlssnieyltknkanAEKLCRTYEDQLSEAKSKVDELQrqlAEVSTQRGRLQTENGELSRLLEEKESFI 1076
Cdd:TIGR00606 404 EDEAKT--------------------AAQLCADLQSKERLKQEQADEIR---DEKKGLGRTIELKKEILEKKQEELKFVI 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1077 NQLSRgktsFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAkgELQRTLSKANAEVAQWRTKYETd 1156
Cdd:TIGR00606 461 KELQQ----LEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQLNHHTTT- 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1157 aiqRTEELEEAKKKLAIRLQEAEEAVEAAHAKCS---------SLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQ--- 1224
Cdd:TIGR00606 534 ---RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKnhi 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1225 RNFDRILAEWKQKFEET----------QAELESSQKESRSLSTELFKLKNAYEESLDNLETLKREN-------------- 1280
Cdd:TIGR00606 611 NNELESKEEQLSSYEDKlfdvcgsqdeESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcqrvfqte 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1281 KNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKsdiqaalEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDEE 1360
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR-------DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1361 FENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLR 1440
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1441 HNDDLKEQAAALERRNNLLLAEVEELRAAL----EQAERGRKLAEQELLEATErvnlLHSQNTGLINHKKKIEADLAQLS 1516
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKlqigTNLQRRQQFEEQLVELSTE----VQSLIREIKDAKEQDSPLETFLE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1517 SEVEEAVQECRNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkggkk 1588
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK-------- 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1589 QIQKLEARVRELEGELDIE--QKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQdlidKLQSKVKSYKRQFEEAEQQ 1666
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ----VLQMKQEHQKLEENIDLIK 1067
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 2077626420 1667 ANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRDVI 1706
Cdd:TIGR00606 1068 RNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMM 1107
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1091-1651 |
2.58e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1091 EELKRQLEE-ETKSKNALAHALQASRHDCDLLREQYEEEVEAKgelQRTLSKANAEVAQWRTKYEtdaiqRTEELEEAKK 1169
Cdd:PRK02224 190 DQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQA---RETRDEADEVLEEHEERRE-----ELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1170 KLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQrnfdrilaewkQKFEETQAELESSQ 1249
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR-----------EELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1250 KESRSLSTELFKLKNAYEESLDNLET----LKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEA 1325
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEEraeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1326 EGALEHEESKTLRIQLELSQIKADVeRKLAEKDEEFENLRRN------HQRAMDSMQATLDAEAKARNEairlrkKMEGD 1399
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATL-RTARERVEEAEALLEAgkcpecGQPVEGSPHVETIEEDRERVE------ELEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1400 LNEMEIQLSHANRQAAESQKLVrQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKL 1479
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1480 AEQELLEATERVNLLHSQNTGLinhKKKIEA--DLAQLSSEVEEAVQECRNAEEKAKkaitDAAMMAEELKkeqdtsahl 1557
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAEL---KERIESleRIRTLLAAIADAEDEIERLREKRE----ALAELNDERR--------- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1558 ERMKKNMEQtIKDLQMRLDEAeqiALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELtyqtEEDRK 1637
Cdd:PRK02224 627 ERLAEKRER-KRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRE 698
|
570
....*....|....
gi 2077626420 1638 NLARMQDLIDKLQS 1651
Cdd:PRK02224 699 RREALENRVEALEA 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1355-1586 |
2.99e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1355 AEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIE 1434
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1435 LDdtlRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQ 1514
Cdd:COG4942 99 LE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1515 LSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGG 1586
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
713-1331 |
4.39e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 713 DLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMaalDEIIAKLTKEKKALQEAHQqaldDLQAEE 792
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQI---KDLNDKLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 793 DKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRI 872
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 873 EDEQVLGAQLQKKIKELQArieeleeeleaeraaraKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKrEAEFLKL 952
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKK-----------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-TTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 953 RRDLEEATLQHESTAAVLRKKHADtVAELGEQIDNLQRVKQKLEKEKSEMKME-VDDLSSNIEYLTKNKanaEKLCRTYE 1031
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE-LEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQ---EKKLEEIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1032 DQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIE-------ELKRQLEEETKSK 1104
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqinDLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1105 NALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYE------TDAIQRTEELEEAKKKLAIRLQEA 1178
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1179 EEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQ--KESRSLS 1256
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKN 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1257 TELFKLKNAYEESLDN-------LETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGAL 1329
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKqeekqelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
..
gi 2077626420 1330 EH 1331
Cdd:TIGR04523 648 KQ 649
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1315-1704 |
4.96e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1315 KSDIQAALEEAEGALEHEESKTLRIQLelsqikADVERKLAEKDEEFENL---RRNHQRAMDSMQATLDAEAKARNEAIR 1391
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1392 LrkkmEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALE 1471
Cdd:PRK02224 256 L----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1472 QAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVE---EAVQECRNAEEKAKKAITDAAmmaEELK 1548
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAP---VDLG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1549 KEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGgkkqiQKLEARVRELEGELDIEQKKNAETqkgIRKYERRVKEL 1628
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLRTARERVEEA-----EALLEAGKCPECGQPVEGSPHVET---IEEDRERVEEL 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1629 TYQTEEDRKNLARMQDLIDKLQSKVksykrqfeEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRD 1704
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLV--------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
695-918 |
5.80e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 695 AKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEK 774
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 775 KALQEAHQQALDDLQaeedKVNTLTKAKVKLEQQ-VDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQ 853
Cdd:COG4942 100 EAQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 854 LEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVA 918
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
988-1517 |
6.19e-09 |
|
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: 60.91 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 988 LQRVKQKLEKEKSEMK-MEVDDLSSNIEYLTKNKANAEKLCRTyEDQLSEAKSKVDELQRQLAEVST------QRGRLQT 1060
Cdd:pfam05557 4 LIESKARLSQLQNEKKqMELEHKRARIELEKKASALKRQLDRE-SDRNQELQKRIRLLEKREAEAEEalreqaELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1061 ENGE-LSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLRE---QYEEEVEAKGELQ 1136
Cdd:pfam05557 83 KYLEaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAkasEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1137 RTLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLA--IRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERan 1214
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQE-QDSEIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLER-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1215 saaaaldkkqrnfdrilaewkqkFEETQAELESSQKESRSLSTELFKLKNAYEESLDNL---ETLKRENKNLQEEIADLT 1291
Cdd:pfam05557 240 -----------------------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1292 DQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQlelsqikadveRKLAEKDEEFENLRRNHQRA 1371
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAILESY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1372 MDSMQATLDAEAKARN--EAIRLRKKMEGDLNEMEIQLSHANRQA-----------AESQKLVRQ-LQAQIKDLQIELDD 1437
Cdd:pfam05557 366 DKELTMSNYSPQLLERieEAEDMTQKMQAHNEEMEAQLSVAEEELggykqqaqtleRELQALRQQeSLADPSYSKEEVDS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1438 TLRHNDDLKEQAAALERRNNLLLAEVE--ELRAALEQAE-RGRKLAEQELLEATER----VNLLHSQNTGLINHKKKIEA 1510
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELErrCLQGDYDPKKtKVLHLSMNPAAEAYQQrknqLEKLQAEIERLKRLLKKLED 525
|
....*..
gi 2077626420 1511 DLAQLSS 1517
Cdd:pfam05557 526 DLEQVLR 532
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
631-1369 |
1.04e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 60.37 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 631 KEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLaDAEERCDLLIKTKIQLEAKVKELMERLEDEEEM 710
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL-CTPCMPDTYHERKQVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 711 NADLTSK------KRKLEDECAELKKDIDDLELTLAKVEKEKHATE--NKVKNLIEEMAALDEIIAKLT------KEKKA 776
Cdd:TIGR00618 242 HAYLTQKreaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQIEQQAQrihtelQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 777 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQ--ESVMDLENDKQQL 854
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 855 EEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIkELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGV 934
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 935 TAVQLEMNKKREAEFL----KLRRDLEEATLQHESTAAVLRKKHADT---------VAELGEQIDN----LQRVKQKLEK 997
Cdd:TIGR00618 481 IHLQETRKKAVVLARLlelqEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrgeqtYAQLETSEEDvyhqLTSERKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 998 EKSEMKMEVDDLSSNIEYLTKNKANAEKLcRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFIN 1077
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNL-QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1078 QLSRGKTSFTQTIEELKRQLEEetksknalaHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKyetda 1157
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVR---------EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL----- 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1158 iqrTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDlsidlERANSAAAALDKKQRNFDRILAEWK-- 1235
Cdd:TIGR00618 706 ---LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKARTEAHFNNNEEVTAALQtg 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1236 QKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKR-ENKNLQEEIADLTDQISLSGKTIHELEKVKKALEgE 1314
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE-E 856
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 1315 KSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQ 1369
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQ 911
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
630-1100 |
1.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 630 LKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDlslHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLE--DE 707
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELK---EAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 708 EEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKalqEAHQQALDD 787
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE---EELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 788 LQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQ 867
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 868 LNSRIedEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREA 947
Cdd:COG4717 281 LVLGL--LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 948 EFLKLRRDLEEATLQhestaAVLRKKHADTVAELGEQIDNLQRvKQKLEKEKSEMKMEVDDLSSNIEYL--TKNKANAEK 1025
Cdd:COG4717 359 LEEELQLEELEQEIA-----ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELleALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1026 LCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTEnGELSRLLEEKESFINQLSRGKTSFT------QTIEELKRQLEE 1099
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAalklalELLEEAREEYRE 511
|
.
gi 2077626420 1100 E 1100
Cdd:COG4717 512 E 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1269-1522 |
1.16e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1269 SLDNLETLKREN----KNLQEEIADLTDQISlsgktihELEKVKKALEGEKSDIQAaLEEAEGAleHEESKTLRIQLE-L 1343
Cdd:COG4913 205 PIGDLDDFVREYmleePDTFEAADALVEHFD-------DLERAHEALEDAREQIEL-LEPIREL--AERYAAARERLAeL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1344 SQIKADV-----ERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEG----DLNEMEIQLSHANRQA 1414
Cdd:COG4913 275 EYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1415 AESQKLVRQLQAQIKDLQIELDDTLrhnDDLKEQAAALERRnnllLAEVEELRAALEQAERGRKLAEQELLEATERvnlL 1494
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASA---EEFAALRAEAAAL----LEALEEELEALEEALAEAEAALRDLRRELRE---L 424
|
250 260
....*....|....*....|....*...
gi 2077626420 1495 HSQNTGLINHKKKIEADLAQLSSEVEEA 1522
Cdd:COG4913 425 EAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
994-1578 |
1.18e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 994 KLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKE 1073
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1074 SFINQLSRGKTSftQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKY 1153
Cdd:TIGR04523 295 SEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1154 ET------DAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNF 1227
Cdd:TIGR04523 373 EKlkkenqSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1228 DRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKV 1307
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1308 KKALEGEKSDIQAALEEAEGALEheesktlriqlelsqiKADVERKLAEKDEEFENLRRNhqramdsmQATLDAEAKarn 1387
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELK----------------KENLEKEIDEKNKEIEELKQT--------QKSLKKKQE--- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1388 eairlrkkmegdlnemeiqlshanrqaaESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELR 1467
Cdd:TIGR04523 586 ----------------------------EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1468 AALEQAERGRKLAEQELLEATERVNLLHSQNTGLinhkKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEEL 1547
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES----KTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKY 713
|
570 580 590
....*....|....*....|....*....|.
gi 2077626420 1548 KKEQDTSAHLERMKKNMEQTIKDLQMRLDEA 1578
Cdd:TIGR04523 714 KEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1020-1485 |
1.59e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1020 KANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKEsfinQLSRGKTSFTQTIEELKRQLEE 1099
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1100 ETKSKnaLAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAE 1179
Cdd:COG4717 128 LPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1180 EAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDR-----ILAEWKQKFEETQAELESSQKESRS 1254
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallaLLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1255 LS---TELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEH 1331
Cdd:COG4717 286 LAllfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1332 EESKTLRIQLeLSQIKADVERKLAEKDEEFENlRRNHQRAMDSMQATLDAEAKARNEAIRlrkkmEGDLNEMEIQLSHAN 1411
Cdd:COG4717 366 EELEQEIAAL-LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1412 RQAAESQKLVRQLQAQIKDLQIELDDTLRHN--DDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELL 1485
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1199-1605 |
1.65e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 59.32 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1199 LQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEEtqaeLESSQKESRSLSTELFKLKNA------------- 1265
Cdd:pfam05622 64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvet 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1266 YEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQaaleEAEGALEHEESKTLRIQLELSQ 1345
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1346 IKADVERKLAEKD----------EEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAA 1415
Cdd:pfam05622 216 LEEKLEALQKEKErliierdtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1416 ESQKLvrQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAErgrklaeqelleatervnllh 1495
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG--------------------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1496 SQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 1567
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 2077626420 1568 IKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELD 1605
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1393-1612 |
2.13e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1393 RKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALE- 1471
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1472 -QAERGRKLAEQELLEATERVNLLHSQN--TGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1548
Cdd:COG4942 102 qKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1549 KEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDIEQKKNA 1612
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
1-24 |
2.19e-08 |
|
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: 55.43 E-value: 2.19e-08
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
632-1417 |
2.73e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 632 EEFQKLKEALEKSEVKRKELEEKQITMIQekndlslhlQAEQDNLADAEERCDLLIKTKiqlEAKVKELMERLEDEEEMN 711
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDAR---------KAEEARKAEDAKRVEIARKAE---DARKAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 712 AdltSKKRKLEDECAELKKDIDDLELTLA-KVEKEKHATENKV---KNLIEEMAALDEIIAKLTKEKKALQEAHQQALDD 787
Cdd:PTZ00121 1180 A---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 788 LQAEEDKVNTLTKAKVKLEQ--QVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFET 865
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 866 SQLNSRIEDEqVLGAQLQKKIKELQARIEELEEELEAERAARAKVE---KQRAEVARELEELSERLEEAGGVTAVQLEMN 942
Cdd:PTZ00121 1337 KAEEAKKAAE-AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 943 KKREAEflKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLE--------KEKSEMKMEVDDLSSNIE 1014
Cdd:PTZ00121 1416 AKKKAD--EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkadeaKKKAEEAKKADEAKKKAE 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1015 YLTKN----KANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESfinqlsrGKTSFTQTI 1090
Cdd:PTZ00121 1494 EAKKKadeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL-------KKAEEKKKA 1566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1091 EELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYET-DAIQRTEELEEAKK 1169
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkKKVEQLKKKEAEEK 1646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1170 KLAIRLQeaeEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKqrnfdrilAEWKQKFEETQAELESSQ 1249
Cdd:PTZ00121 1647 KKAEELK---KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--------AEEAKKAEELKKKEAEEK 1715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1250 KESRslstelfKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEaegAL 1329
Cdd:PTZ00121 1716 KKAE-------ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE---EL 1785
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1330 EHEESKTlriqlelsqiKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSH 1409
Cdd:PTZ00121 1786 DEEDEKR----------RMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFN 1855
|
....*...
gi 2077626420 1410 ANRQAAES 1417
Cdd:PTZ00121 1856 KNNENGED 1863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
669-1064 |
3.43e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 669 LQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHA 748
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 749 TENKVKNLIEEMAALDEIIAKLtkekkalqeahQQALDDLQAEED--KVNTLTKAKVKLEQQVDDLESSLEqekkirmDL 826
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKL-----------EEALNDLEARLShsRIPEIQAELSKLEEEVSRIEARLR-------EI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 827 ERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDeqvlgaqLQKKIKELQARIEELEEELEAERAA 906
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 907 RAKVEKQRAEVARELEELSERLEEAG---GVTAVQLEMNKKREAEFLKLRRDLEEatlqhESTAAVLRKKHADTVAELGE 983
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRkrlSELKAKLEALEEELSEIEDPKGEDEE-----IPEEELSLEDVQAELQRVEE 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 984 QIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKV-----DELQRQLAEVSTQRGRL 1058
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAfeainENFNEIFAELSGGTGEL 1045
|
....*.
gi 2077626420 1059 QTENGE 1064
Cdd:TIGR02169 1046 ILENPD 1051
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1134-1553 |
3.64e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1134 ELQRTLSKANAEVAQWRTKYET--DAIQRTEELEEAKKKLAIRLQEAEEAVEAAhakcsSLEKTKHRLQTEIEDLSIDLE 1211
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1212 RANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSlstELFKLKNAYEESLDNLETLKRENKNLQEEIADLT 1291
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1292 DQISLSGKTIHELEKVKKALEGEKS-DIQAALEEAEGALEHEESKTLRI-------------QLELSQIKADVERKLAEK 1357
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1358 DEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQkLVRQLQAQIKDLQIELDD 1437
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1438 TLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLA---------EQELLEATERVNLLHSQNTGLINHKKKI 1508
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeeleelEEELEELEEELEELREELAELEAELEQL 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2077626420 1509 EAD--LAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1553
Cdd:COG4717 466 EEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
975-1191 |
3.98e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 975 ADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQ 1054
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1055 RGRLQTENGELSR------------LLEEKESFiNQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLR 1122
Cdd:COG4942 99 LEAQKEELAELLRalyrlgrqpplaLLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1123 EQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSS 1191
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
693-1290 |
4.20e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 693 LEAKVKELMERLED--EEEMNADLTSKKRKLEDECAELKKDIDDLEltlakvEKEKHATENK--VKNLIEEMAALDEIIA 768
Cdd:PRK02224 181 VLSDQRGSLDQLKAqiEEKEEKDLHERLNGLESELAELDEEIERYE------EQREQARETRdeADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 769 KLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLE 848
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 849 NDKqqleeklkkkefetSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEEleaERAARAKVEKQRAEVARELEELSERL 928
Cdd:PRK02224 335 VAA--------------QAHNEEAESLREDADDLEERAEELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 929 EEAGGvTAVQLEmnkkREAEFLKLRRDLEEAtlqhestaavLRKKHADTVAELGEQIDNLQRVKQKLEKEK-SEMKMEVD 1007
Cdd:PRK02224 398 ERFGD-APVDLG----NAEDFLEELREERDE----------LREREAELEATLRTARERVEEAEALLEAGKcPECGQPVE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1008 DlSSNIEYLTKNKANAEKLcrtyEDQLSEAKSKVDELQ------RQLAEVSTQRGRLQTENGELSRLLEEKESfinqlsr 1081
Cdd:PRK02224 463 G-SPHVETIEEDRERVEEL----EAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRE------- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1082 gktsftqTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAiqRT 1161
Cdd:PRK02224 531 -------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA--AI 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1162 EELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANsaaaaldkkqrnfdrilaewKQKFEET 1241
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARED--------------------KERAEEY 661
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2077626420 1242 QAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADL 1290
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL 710
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
632-1445 |
5.29e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 58.13 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 632 EEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDN-LADAEERCDLLIKTK-----------IQLEAKVKE 699
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHiRARDSLIQSLATRLEldgfergpfseRQIKNFHTL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 700 LMERLEDEEEMNA----DLTSKKRKLEDECAELKKDIDDLELTL----AKVEKEKHATENKVKNLIEEMAALDEIIAKLT 771
Cdd:TIGR00606 399 VIERQEDEAKTAAqlcaDLQSKERLKQEQADEIRDEKKGLGRTIelkkEILEKKQEELKFVIKELQQLEGSSDRILELDQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 772 KEKKALQEAhqqaldDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDK 851
Cdd:TIGR00606 479 ELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 852 QQLEEKLKKKEFETSQLNSRIEDEQVLgAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEA 931
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWL-HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 932 GGVTAVqlemnkkrEAEFLKLRRDLEEATLQHESTAAVlRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSS 1011
Cdd:TIGR00606 632 CGSQDE--------ESDLERLKEEIEKSSKQRAMLAGA-TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1012 NIEYLTKNKANAEKLCRTYEDQLSE----AKSKVDELQRQLAEVSTQRGRLQTENGELSRL---LEEKESFIN------Q 1078
Cdd:TIGR00606 703 KLRLAPDKLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLkndIEEQETLLGtimpeeE 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1079 LSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASrhDCDLLREQYEEEVEAKGELQRTLSKA---NAEVAQWRTKYET 1155
Cdd:TIGR00606 783 SAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKielNRKLIQDQQEQIQ 860
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1156 DAIQRTEELEEAKKKLAIRLQeaeeaveaahaKCSSLEKTKHRLQTEIEDLSIDLeransaaaaldKKQRNFDRILAEWK 1235
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQ-----------RRQQFEEQLVELSTEVQSLIREI-----------KDAKEQDSPLETFL 918
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1236 QKFEETQAELESSQKESRSLSTelfklknayeeslDNLETLKRENKNLQEEIADLTDQISlSGKtihelEKVKKALEGEK 1315
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQ-------------DKVNDIKEKVKNIHGYMKDIENKIQ-DGK-----DDYLKQKETEL 979
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1316 SDIQAALEEAEGALE--HEESKTLRIQLELSQIKADV------ERKLAEKDEEFENLRRNHQRAMDSMQAT-LDAEAKAR 1386
Cdd:TIGR00606 980 NTVNAQLEECEKHQEkiNEDMRLMRQDIDTQKIQERWlqdnltLRKRENELKEVEEELKQHLKEMGQMQVLqMKQEHQKL 1059
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1387 NEAIRLRKKME----GDLNEMEIQLSHANRQAAESQklVRQLQAQIKDLQIELDDTLRHNDDL 1445
Cdd:TIGR00606 1060 EENIDLIKRNHvlalGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
625-1145 |
6.17e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 625 KEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEkndlslhLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERL 704
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 705 EDEEEMNADLTSKKRKLEDECAELKKDIDD---LELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAH 781
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 782 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMdlERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKK 861
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 862 EFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGvtavQLEM 941
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE----QIKK 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 942 NKKREAEFLKLRRDLEEATLQHESTAAVLRKKhaDTVAELgeQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKA 1021
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKEL--IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1022 NAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFT---------QTIEE 1092
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeideknKEIEE 572
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1093 LKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAE 1145
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
957-1404 |
6.19e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 957 EEATLQHESTAAvlRKKHADTVAELGEQIDNLQRV----KQKLEKEKSEMK---MEVDDLSSNIEYLTKNKANAEKLCRT 1029
Cdd:pfam05483 332 EKEAQMEELNKA--KAAHSFVVTEFEATTCSLEELlrteQQRLEKNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1030 YEDQLSEAKSKVDElQRQLAEVSTQrgrLQTENGELSRLLEEKESFIN----QLSRGKTS---FTQTIEELKRQLEEEtK 1102
Cdd:pfam05483 410 LKKILAEDEKLLDE-KKQFEKIAEE---LKGKEQELIFLLQAREKEIHdleiQLTAIKTSeehYLKEVEDLKTELEKE-K 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1103 SKNALAHAlqasrhDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRtKYETDAIQRTEELEEAKKKLAIRLQ--EAEE 1180
Cdd:pfam05483 485 LKNIELTA------HCDKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDELEsvREEF 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1181 AVEAAHAKCSSLEKTKHRLQTEIEDLsidleRANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELf 1260
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVL-----KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQL- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1261 klkNAYEESLDNLETLKRENKNLQEEIADLTDQislsgktihELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQ 1340
Cdd:pfam05483 632 ---NAYEIKVNKLELELASAKQKFEEIIDNYQK---------EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1341 LELSQIKADVER------KLAEKDEEFENLRRNHQRAMDSMQATLDAE-AKARNEAIRLRKKMEGDLNEME 1404
Cdd:pfam05483 700 HKIAEMVALMEKhkhqydKIIEERDSELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKE 770
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1251-1607 |
6.76e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 57.00 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1251 ESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALE 1330
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1331 HEESKTLRIQLELSQ---IKADVERKLAEKDEefenlrrnHQRAMDSMQATLDAEAKARNEAirlrkkmegdLNEMEIQL 1407
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETE--------QNRALEEENKALREEAQAAEKA----------LQRAEGEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1408 SHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLlaeveELRAALEQAERGRKLAEQELLEA 1487
Cdd:pfam19220 163 ATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRAL-----EGQLAAEQAERERAEAQLEEAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1488 TERVNL--LHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 1565
Cdd:pfam19220 238 AHRAERasLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQ 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2077626420 1566 QTIKDLQMRLD------EAEQIALKGGKKQIQKLEARVRELEGELDIE 1607
Cdd:pfam19220 318 RARAELEERAEmltkalAAKDAALERAEERIASLSDRIAELTKRFEVE 365
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1425-1663 |
1.06e-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: 56.31 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1425 QAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINH 1504
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1505 KKKIEADLAQLsseVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALK 1584
Cdd:COG4942 99 LEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA-ERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1585 GGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELtyqteedRKNLARMQDLIDKLQSKVKSYKRQFEEA 1663
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
677-1312 |
1.35e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 677 ADAEERCDLLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEdecaELKKDIDDLELTLAKVEKEKHATENKVKNL 756
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 757 IEEMAALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLtKAKVKLEQQVDDLES---SLEQEKKIRMDLERAKRKL 833
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEeinGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 834 EGDLKLTQESVMDLENDKQQLEEKLKKKEfETSQLNSRIEDEQVlgAQLQKKIKELQARIEELEEELEAERAARAKVEKQ 913
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 914 RAEVAREleelserleeaggvtavqLEMNKKREAEFLKLRRDLEE---ATLQHESTAAVlrKKHADTVAELGEQIDNLQR 990
Cdd:PRK03918 421 IKELKKA------------------IEELKKAKGKCPVCGRELTEehrKELLEEYTAEL--KRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 991 VKQKLEKEKSEMKmevdDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTEngelsrlLE 1070
Cdd:PRK03918 481 ELRELEKVLKKES----ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-------LE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1071 EKESFINQLsrgktsftQTIEELKRQLEEETKsknalahalqasrhdcDLLREQYEEEVEAKGELQRTLskanaevaqwr 1150
Cdd:PRK03918 550 KLEELKKKL--------AELEKKLDELEEELA----------------ELLKELEELGFESVEELEERL----------- 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1151 tkyetdaiqrtEELEEAKKKLaIRLQEAEEAVEaahakcsSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKqrnfdri 1230
Cdd:PRK03918 595 -----------KELEPFYNEY-LELKDAEKELE-------REEKELKKLEEELDKAFEELAETEKRLEELRKE------- 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1231 LAEWKQKFeeTQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTdqislsgKTIHELEKVKKA 1310
Cdd:PRK03918 649 LEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-------KAKKELEKLEKA 719
|
..
gi 2077626420 1311 LE 1312
Cdd:PRK03918 720 LE 721
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1091-1486 |
1.51e-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: 56.06 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1091 EELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEA----KGELQRTLSKANAEVAQWRTKYEtDAIQRTEELEE 1166
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqRRELESRVAELKEELRQSREKHE-ELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1167 AKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERansaaaaLDKKQRNFDRILAEWKQKFEETQAELE 1246
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1247 SSQKESRSLSTELFKLKNAYEESLDNLETlkrenknLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAE 1326
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1327 GALEheesktlriqlELSQIKADVERKLAEKdeefenlrrnHQRAMDSMQATL---DAEAKARNEAIRLRKKMEGDLNEM 1403
Cdd:pfam07888 255 GLGE-----------ELSSMAAQRDRTQAEL----------HQARLQAAQLTLqlaDASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1404 EIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERrnnlllaEVEELRAALE--QAERGRKLAE 1481
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR-------ELQELKASLRvaQKEKEQLQAE 386
|
....*.
gi 2077626420 1482 -QELLE 1486
Cdd:pfam07888 387 kQELLE 392
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
426-453 |
1.80e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 52.73 E-value: 1.80e-07
10 20
....*....|....*....|....*...
gi 2077626420 426 SQVHKENLNKLMTNLRATQPHFVRCIIP 453
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1218-1658 |
1.90e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1218 AALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLS 1297
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1298 G--KTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSM 1375
Cdd:COG4717 129 PlyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1376 QATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDL----KEQAAA 1451
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1452 LERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEE 1531
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1532 KAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALkggKKQIQKLEARVRELE 1601
Cdd:COG4717 369 EQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EEELEELEEELEELE 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 1602 GELDIEQKKNAETQKGIRKYERRvkeltyqtEEDRKNLARMQDLIDKLQSKVKSYKR 1658
Cdd:COG4717 446 EELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAEEWAA 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-1083 |
2.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 625 KEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQD--NLADAEERCDLLIKTKIQLEAKVKELME 702
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 703 RLEDEEEMNADLTSKKRKLEDECAEL----KKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQ 778
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 779 EAHQQAlddlqaEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMdlerakrkLEGDLKLTQESVMDLENDKQQLEEKL 858
Cdd:COG4717 241 LEERLK------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLF--------LVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 859 KKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQ 938
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 939 LEMNKKREAEFLKLRRDLEEATLQ-HESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLT 1017
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1018 KNKANAEKlcrtyEDQLSEAKSKVDELQR-----QLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGK 1083
Cdd:COG4717 467 EDGELAEL-----LQELEELKAELRELAEewaalKLALELLEEAREEYREERLPPVLERASEYFSRLTDGR 532
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1224-1701 |
2.54e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1224 QRNFDRILAEWKQKFEETQAELESS----QKESRSLSTELFKLKNAYEE---SLDNLETLKRENKNLQEeiaDLTDQISl 1296
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESnelhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQE---DLRNQLQ- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1297 sgKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESktlrIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQ 1376
Cdd:pfam15921 149 --NTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEG----VLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1377 ATLdaeakarneairlrkkmegdLNEMEIQLSHANRQAAESQKlvrQLQAQIKDLQIELDDTLRHNDDLKEQaaalerrn 1456
Cdd:pfam15921 223 SKI--------------------LRELDTEISYLKGRIFPVED---QLEALKSESQNKIELLLQQHQDRIEQ-------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1457 nlLLAEVE-ELRAALEQAERGRKLA-----EQELLEATERvnllhSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAE 1530
Cdd:pfam15921 272 --LISEHEvEITGLTEKASSARSQAnsiqsQLEIIQEQAR-----NQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1531 EKAKKAITDAAMMAEELKKEQDTSA--------HLERMKKNMEQTIKDLQMRLDEAEQI----------------ALKGG 1586
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSqesgnlddQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrrELDDR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1587 KKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARmqdLIDKLQSKvksyKRQFEEAEQQ 1666
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK---VVEELTAK----KMTLESSERT 497
|
490 500 510
....*....|....*....|....*....|....*
gi 2077626420 1667 ANSnlvkyrkVQHELDDAEERADIAETQVNKLRSR 1701
Cdd:pfam15921 498 VSD-------LTASLQEKERAIEATNAEITKLRSR 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
624-849 |
2.62e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 624 EKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMER 703
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 704 LED-EEEMNADLTSKKRKLEDECAELKKdIDDLELTLAKVEKEKHATENKVKNLIEEmaaLDEIIAKLTKEKKALQEAHQ 782
Cdd:PRK03918 572 LAElLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRK 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 783 QaLDDLQAE--EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN 849
Cdd:PRK03918 648 E-LEELEKKysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
622-844 |
3.92e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 622 QTEKEMATLKEEFQKLKEALEKSEVKRK------ELEEKQITMIQEKNDLSlHLQAEQDNLAD--AEERCDLLIKTKIQL 693
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqiellePIRELAERYAAARERLA-ELEYLRAALRLwfAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 694 EAKVKELMERLEDEEEMNADLTSKKRKLEDECAELK-KDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTK 772
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 773 EKKALQEAHQQALDDLQAEEDKVNT----LTKAKVKLEQQVDDLES---SLEQEKK-IRMDLERAKRKLEGDLKLTQESV 844
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLERRKSnIPARLLALRDALAEALGLDEAEL 460
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1412-1704 |
5.47e-07 |
|
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: 54.80 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1412 RQAAESQKLVRQLQA---QIKDLQIELDDTLRHNDDLKEQAAALE---RRNNLLLAEVEELRAALeqAERGRKLaEQELL 1485
Cdd:pfam01576 2 RQEEEMQAKEEELQKvkeRQQKAESELKELEKKHQQLCEEKNALQeqlQAETELCAEAEEMRARL--AARKQEL-EEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1486 EATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEavQECRNAEEKAKKAITDAAM--MAEELKKEQDTSAHLERMKKN 1563
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTTEAKIkkLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1564 MEQTIKDLQMRLDEAEQIAlKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQ 1643
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1644 DLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRD 1704
Cdd:pfam01576 236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRD 296
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
624-829 |
6.35e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 624 EKEMATLKEEFQKLKEALEKSEVKRKELEEKQitmiqekndlslhlqaeqDNLADAEERCDLLIKTKiQLEAKVKELMER 703
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERR------------------EALQRLAEYSWDEIDVA-SAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 704 LEDEEEMNADLtskkRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHqq 783
Cdd:COG4913 677 LERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-- 750
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2077626420 784 aLDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKirmDLERA 829
Cdd:COG4913 751 -LEERFAAALGDAVERELRENLEERIDALRARLNRAEE---ELERA 792
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
618-834 |
7.49e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 618 LRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMiqeknDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKV 697
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 698 KELMERLEDEEEMNADLTSkkrklEDECAELKKDIDDLELTLAkvEKEKHATEN--KVKNLIEEMAALdeiiakltkeKK 775
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 776 ALQEAHQQALDDLQAEedkVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE 834
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
682-1359 |
8.30e-07 |
|
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: 54.20 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 682 RCDLLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHAT----ENKVKNLI 757
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 758 EEMAALDEIIAKLTKEKKALQEAH--QQALDDLQAEEDKVNTLTKAKVKLEQQVD----------DLESSLEQEKKIRMD 825
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQERINrarkaaplaaHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 826 LERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDEQVLG--AQLQKKIKELQ---ARIEELEEEL 900
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQhihTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 901 EAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVqlemnkKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAE 980
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA------KKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 981 -LGEQIDNLQRVKQKLEKEKSEMKMEVDDLssniEYLTKNKANAEKLCRTYEDQLSEAkSKVDELQRQLAEVSTQRGRLQ 1059
Cdd:TIGR00618 467 sLKEREQQLQTKEQIHLQETRKKAVVLARL----LELQEEPCPLCGSCIHPNPARQDI-DNPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1060 TENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHdcdLLREQYEEEVEAKGELQRTL 1139
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD---LTEKLSEAEDMLACEQHALL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1140 SKANAEVAQWRTKYETDAIQRTEELEE-AKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHR------LQTEIEDLSID--- 1209
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRqlalqkMQSEKEQLTYWkem 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1210 LERANSAAAALDKKQRNFDRILAEWKQKFEETQAEL--------ESSQKESRSLSTELFKLKNAYEESLDNLETLKRENK 1281
Cdd:TIGR00618 699 LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLaaredalnQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGA 778
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 1282 NLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDE 1359
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEE 856
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1447-1667 |
1.15e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1447 EQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQEC 1526
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1527 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQmrlDEAEQIalkggKKQIQKLEARVRELEG 1602
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEEL-----RADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 1603 ELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQA 1667
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1397-1595 |
1.28e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1397 EGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALeqAERG 1476
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1477 RKLAEQ-----------------ELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQEcrnAEEKAKKAITD 1539
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1540 AAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEA 1595
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1378-1698 |
1.99e-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: 52.72 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1378 TLDAEAKARNEAIRLRKKmegDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNN 1457
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKE---QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1458 LLLAEVEELRAALEQAERGRKLAEQELL---EATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAK 1534
Cdd:TIGR04523 177 LLEKEKLNIQKNIDKIKNKLLKLELLLSnlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1535 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRL----DEAEQIALKGGKKQIQKLEARVRELEGELDIEQKK 1610
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1611 NAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADI 1690
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
....*...
gi 2077626420 1691 AETQVNKL 1698
Cdd:TIGR04523 417 LQQEKELL 424
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1200-1419 |
2.11e-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: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1200 QTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRE 1279
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1280 NKN------------LQEEIADLTDQISL-------SGKTIHELEKVKKALEGEKSDIQAALEEAEGALEheesktlriq 1340
Cdd:COG3883 95 LYRsggsvsyldvllGSESFSDFLDRLSAlskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKA---------- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1341 lELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQAtLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQK 1419
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1365-1675 |
2.30e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1365 RRNHQRAMDSMQATLD--AEAKARNEAI-RLRKKME----GDLNEMEIQLSHANRQAAesQKLVRQLQAQIKDLQIELdd 1437
Cdd:COG3206 93 RPVLERVVDKLNLDEDplGEEASREAAIeRLRKNLTvepvKGSNVIEISYTSPDPELA--AAVANALAEAYLEQNLEL-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1438 tlrhnddlkeQAAALERRNNLLLAEVEELRAALEQAERgrKLA----EQELLEATERVNLLHSQNTGLINHKKKIEADLA 1513
Cdd:COG3206 169 ----------RREEARKALEFLEEQLPELRKELEEAEA--ALEefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1514 QLSSEVEeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQMRLDEAEQIAL 1583
Cdd:COG3206 237 EAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRIL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1584 KGGKKQIQKLEARVRELEGELDieqkknaetqkgirKYERRVKELTyqteEDRKNLARMQDLIDKLQSKVKSYKRQFEEA 1663
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLA--------------QLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
330
....*....|..
gi 2077626420 1664 EQQANSNLVKYR 1675
Cdd:COG3206 378 RLAEALTVGNVR 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
613-1105 |
2.73e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 613 KIKPLLRSAQTEKEMATLK--EEFQKLKEALEKSEVKRKELEEKQITMIQEKndlslhlQAEQDNLADAEERCDLLIKTK 690
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKkeEAKKKADAAKKKAEEKKKADEAKKKAEEDKK-------KADELKKAAAAKKKADEAKKK 1426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 691 IQLEAKVKELMERLEdeEEMNADLTSKKRKLEDECAELKKdiddleltlaKVEKEKHATENKVKnlIEEMAALDEIIAKL 770
Cdd:PTZ00121 1427 AEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKA 1492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 771 TKEKKALQEAHQQALDDLQAEEDKvntltkakvKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEND 850
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAK---------KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 851 KQQLEEKLKKkefETSQLNSRIEDEqvlGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSErlee 930
Cdd:PTZ00121 1564 KKAEEAKKAE---EDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK---- 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 931 aggvtavQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHAD--TVAELGEQIDNLQRVKQKLEKEKSEMKMEVDD 1008
Cdd:PTZ00121 1634 -------KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1009 LSSNIEyltKNKANAEKLCRTYEdqlsEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQ 1088
Cdd:PTZ00121 1707 LKKKEA---EEKKKAEELKKAEE----ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
490 500
....*....|....*....|...
gi 2077626420 1089 TIEE------LKRQLEEETKSKN 1105
Cdd:PTZ00121 1780 VIEEeldeedEKRRMEVDKKIKD 1802
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1031-1248 |
3.13e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1031 EDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHA 1110
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1111 LQasrhdcDLLREQYEeeVEAKGELQRTLSKANAEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAIRLQEAE 1179
Cdd:COG4942 106 LA------ELLRALYR--LGRQPPLALLLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1180 EAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESS 1248
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
617-834 |
3.27e-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: 51.30 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 617 LLRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAK 696
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 697 VKELMERLEDEEEMNADLTSKKRKLEDECAEL----KKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTK 772
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 773 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE 834
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
621-913 |
3.37e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 621 AQTEKEMATLKEEFQKLKEALEKSEV----KRKELEEKQITMIQEKNDLSLHLQAEQDnladaeercdlLIKTKIQLEAK 696
Cdd:TIGR04523 331 SQNNKIISQLNEQISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIKN-----------LESQINDLESK 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 697 VKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKA 776
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 777 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESV--MDLENDKQQL 854
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkDDFELKKENL 559
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 855 EEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQ 913
Cdd:TIGR04523 560 EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1127-1687 |
3.55e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1127 EEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAhakcsslEKTKHRLQTEIEDl 1206
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN-------EKVSLKLEEEIQE- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1207 SIDLERANSAAaaldkkqRNFDRILAEWKQKFEETQAELESSQKESRS----LSTELFKLKNAYEESL------------ 1270
Cdd:pfam05483 143 NKDLIKENNAT-------RHLCNLLKETCARSAEKTKKYEYEREETRQvymdLNNNIEKMILAFEELRvqaenarlemhf 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1271 ---DNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKalegeksDIQAALEEAEGALEHEESKTlriQLELSQIK 1347
Cdd:pfam05483 216 klkEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK-------DLTFLLEESRDKANQLEEKT---KLQDENLK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1348 ADVERKlAEKDEEFENLRRNHQRAMdSMQATLDAEAKARNEAIRLRKKmegdlnEMEIQLSHANRQAAESQKLVRQLQAQ 1427
Cdd:pfam05483 286 ELIEKK-DHLTKELEDIKMSLQRSM-STQKALEEDLQIATKTICQLTE------EKEAQMEELNKAKAAHSFVVTEFEAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1428 IKDLQIEL---DDTLRHNDD--------LKEQAAALE---RRNNLLLAEVEELRAALEQAE-------RGRKLAEQ---- 1482
Cdd:pfam05483 358 TCSLEELLrteQQRLEKNEDqlkiitmeLQKKSSELEemtKFKNNKEVELEELKKILAEDEklldekkQFEKIAEElkgk 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1483 -----ELLEATER-VNLLHSQNTGLINHKKKIEADLAQLSSEVE-------EAVQECRNAEEKAKKAITDAAMMAEELKK 1549
Cdd:pfam05483 438 eqeliFLLQAREKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklkniELTAHCDKLLLENKELTQEASDMTLELKK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1550 EQDTSAHLERMKKNMEQTIKDLQmrldEAEQIALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELT 1629
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLE----EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE 593
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 1630 YQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEER 1687
Cdd:pfam05483 594 NKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1259-1706 |
3.59e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.78 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1259 LFKLKNAYEEsLDNLETLKRE--NKNLQEEIADLtDQISLSGKTIHELEKVKK----ALEGEKSDIQAALEEAEGALE-H 1331
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKkwddIVTKSLPDIEELLFEAEELNDkY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1332 EESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLR-------KKMEGDLNEME 1404
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRfsygpaiDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1405 IQLSH-----ANRQAAESQKLVRQLQAQIKDLQielddtlrhnDDLKEQAAALERRNNLLLAEVEELRAALEQ-AERGRK 1478
Cdd:pfam06160 160 EEFSQfeeltESGDYLEAREVLEKLEEETDALE----------ELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGYA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1479 LAEQELLEATERVNLLHSQNTGLIN--HKKKIEADLAQLSSEVEeAVQECRNAEEKAKKaitdaammaeELKKEQDT-SA 1555
Cdd:pfam06160 230 LEHLNVDKEIQQLEEQLEENLALLEnlELDEAEEALEEIEERID-QLYDLLEKEVDAKK----------YVEKNLPEiED 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1556 HLERMKKNMEQTIKDLQM-----RLDEAEQIALKGGKKQIQKLEARVRELEG----------ELDIEQKKNAETQKGIRK 1620
Cdd:pfam06160 299 YLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVErleekevaysELQEELEEILEQLEEIEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1621 YERRVKELTYQTEED----RKNLARMQDLIDKLQSKVK---------SYKRQFEEAEQQANSNLVKYRKVQHELDDAEER 1687
Cdd:pfam06160 379 EQEEFKESLQSLRKDeleaREKLDEFKLELREIKRLVEksnlpglpeSYLDYFFDVSDEIEDLADELNEVPLNMDEVNRL 458
|
490
....*....|....*....
gi 2077626420 1688 ADIAETQVNKLRSRTRDVI 1706
Cdd:pfam06160 459 LDEAQDDVDTLYEKTEELI 477
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
618-1176 |
4.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 618 LRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQA---EQDNLADAEERCDLLIKTKIQLE 694
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheeRREELETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 695 AKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEK 774
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 775 KALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQEsvmdlendkqql 854
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE------------ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 855 eeklkkkefETSQLNSRIedeqvlgAQLQKKIKELQARIEeleeeleaeraarakvEKQRAEVARELEELSERLEEAGGV 934
Cdd:PRK02224 420 ---------ERDELRERE-------AELEATLRTARERVE----------------EAEALLEAGKCPECGQPVEGSPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 935 TAVQlemnkKREAEFLKLRRDLEEATLQHESTAAvlRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIE 1014
Cdd:PRK02224 468 ETIE-----EDRERVEELEAELEDLEEEVEEVEE--RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1015 YLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRL------LEEKESFINQLSRGKTSFTQ 1088
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1089 TIEELKRQLEEETKSKNALAHALQASR-HDCDLLREQYEEEVEAKGELQRTLSKANAEVaQWRTKYETDAIQRTEELEEA 1167
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDL-QAEIGAVENELEELEELRER 699
|
....*....
gi 2077626420 1168 KKKLAIRLQ 1176
Cdd:PRK02224 700 REALENRVE 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
618-849 |
4.56e-06 |
|
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: 51.61 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 618 LRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKV 697
Cdd:TIGR02169 777 LEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 698 KELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKAL 777
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 778 QEAHQQALDDLQAEEDkVNTLTKAKVKLEQQVDDLES-------SLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN 849
Cdd:TIGR02169 937 EDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
613-834 |
5.63e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 613 KIKPLLRSAQTEKEM-ATLKEEFQKLKEALEKSEVKRKEL----EEKQ---------ITMIQEKNDLSL----HLQAEQD 674
Cdd:pfam15921 462 KVSSLTAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLtaslQEKEraieatnaeITKLRSRVDLKLqelqHLKNEGD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 675 NLADAEERCDLLiktKIQLEAK---VKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDD--LELTLAKVEKEKHAT 749
Cdd:pfam15921 542 HLRNVQTECEAL---KLQMAEKdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDrrLELQEFKILKDKKDA 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 750 -----ENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQ-EKKIR 823
Cdd:pfam15921 619 kirelEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETtTNKLK 698
|
250
....*....|.
gi 2077626420 824 MDLERAKRKLE 834
Cdd:pfam15921 699 MQLKSAQSELE 709
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
617-1144 |
5.95e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 617 LLRSAQTEKEMATL-------KEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKT 689
Cdd:pfam05483 246 LIQITEKENKMKDLtflleesRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 690 KIQLEAKVKELMERLEDEE--------EMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMA 761
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 762 ALDEIIAKLTKEKKALQEAHQ--QALDDLQAEEDKVNTLTKAKVK----LEQQVDDLESS----LEQEKKIRMDLERAKR 831
Cdd:pfam05483 406 ELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAREKeihdLEIQLTAIKTSeehyLKEVEDLKTELEKEKL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 832 KlegDLKLTQES-VMDLENDKQQLEEKLKkkefeTSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKV 910
Cdd:pfam05483 486 K---NIELTAHCdKLLLENKELTQEASDM-----TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 911 EKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREAEFLKLRRDLEEAT-----LQHESTAavLRKKHADTVAELGEQI 985
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNknieeLHQENKA--LKKKGSAENKQLNAYE 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 986 DNLQRVKQKLEKEKSEMKMEVDDLSSNIEyltKNKANAEKLCrtyeDQLSEAKSKVDELQRQLAEVSTqrgRLQTENGEL 1065
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNYQKEIE---DKKISEEKLL----EEVEKAKAIADEAVKLQKEIDK---RCQHKIAEM 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1066 SRLLEEKESFINQLSRGKTSftqTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANA 1144
Cdd:pfam05483 706 VALMEKHKHQYDKIIEERDS---ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1201-1711 |
6.08e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1201 TEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKL------KNAYEESLDNLE 1274
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssledmKNRYESEIKTAE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1275 TLKR-------ENKNLQEEIADLT--------DQISLSGKTIHELEKVKKALEGEKSDIQAAleeaegaleHEESKTLRi 1339
Cdd:PRK01156 263 SDLSmeleknnYYKELEERHMKIIndpvyknrNYINDYFKYKNDIENKKQILSNIDAEINKY---------HAIIKKLS- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1340 qlELSQIKADVERKLAEKDE------EFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQ 1413
Cdd:PRK01156 333 --VLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1414 AAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNnllLAEVEELRAALEQAERGRKLAEQELLEATERVNL 1493
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQS---VCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1494 LHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELK---------KEQDTSAHLERMKKNM 1564
Cdd:PRK01156 488 IEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdkhdkyeeiKNRYKSLKLEDLDSKR 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1565 EQTIKDLQMRLD---EAEQIALKGGKKQIQKLEARVRELEGELdieQKKNAETQKGIRKYERRVKELTYQTEEDRKNLAr 1641
Cdd:PRK01156 568 TSWLNALAVISLidiETNRSRSNEIKKQLNDLESRLQEIEIGF---PDDKSYIDKSIREIENEANNLNNKYNEIQENKI- 643
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1642 mqdLIDKLQSKVKSYKRQFEEAEQqansnlvkyrkVQHELDDAEERADIAETQVNKLRSRTRDVITSKHE 1711
Cdd:PRK01156 644 ---LIEKLRGKIDNYKKQIAEIDS-----------IIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
619-1051 |
7.62e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVK 698
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMNAdltskkrklEDECAELKKDIDDLELTLAKVEKEkhatenkvknliEEMAALDEIIAKLTKEKKALQ 778
Cdd:PRK02224 437 TARERVEEAEALLE---------AGKCPECGQPVEGSPHVETIEEDR------------ERVEELEAELEDLEEEVEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 779 EAHQQAlDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKL 858
Cdd:PRK02224 496 ERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 859 KKKEFETSQLNSRIEDEQVLgAQLQKKIKELQARIEELEEELEAERAarakVEKQRAEVARELEelserleeaggvtavq 938
Cdd:PRK02224 575 AELNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALAE----LNDERRERLAEKR---------------- 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 939 lEMNKKREAEFLKLRrdLEEATLQHESTAAVLRKKhADTVAELGEQIDNLQR----VKQKLEkEKSEMKMEVDDLSSNIE 1014
Cdd:PRK02224 634 -ERKRELEAEFDEAR--IEEAREDKERAEEYLEQV-EEKLDELREERDDLQAeigaVENELE-ELEELRERREALENRVE 708
|
410 420 430
....*....|....*....|....*....|....*...
gi 2077626420 1015 YLTKNKANAEKLCRTYEDQLSEAKSK-VDELQRQLAEV 1051
Cdd:PRK02224 709 ALEALYDEAEELESMYGDLRAELRQRnVETLERMLNET 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1272-1701 |
7.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1272 NLETLKRENKNLQE-------EIADLTDQISLSG-----------------KTIHELEKVKKALEGEKSDIQAALEEAEG 1327
Cdd:PRK03918 156 GLDDYENAYKNLGEvikeikrRIERLEKFIKRTEnieelikekekeleevlREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1328 ALEHEESKTLRIQLELSQIKA------DVERKLAEKDEEFENLRRNHQRAMDsmqatLDAEAKARNEAIRLRKKMEGDLN 1401
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKleekirELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1402 EMEIQLSHANRQAAESQKLVRQLQ---AQIKDLQIELDDTLRHNDDLKEQAAALER-----------RNNLLLAEVEELR 1467
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEakakkeelerlKKRLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1468 AALEQAERGRKLAEQELLEATERVNLLHSQNTGLI----------------------NHKKKIEADLAQLSSEVEEAVQE 1525
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1526 CRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELD 1605
Cdd:PRK03918 471 IEEKERKLRKE-------LRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1606 I---EQKKNAETQKGIRKYERRVKELtyqtEEDRKNLAR---------MQDLIDKLQSKVKSYKRQFE--EAEQQANSNL 1671
Cdd:PRK03918 543 SlkkELEKLEELKKKLAELEKKLDEL----EEELAELLKeleelgfesVEELEERLKELEPFYNEYLElkDAEKELEREE 618
|
490 500 510
....*....|....*....|....*....|
gi 2077626420 1672 VKYRKVQHELDDAEERADIAETQVNKLRSR 1701
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
938-1569 |
7.75e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 938 QLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEY-- 1015
Cdd:pfam10174 71 HLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETqk 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1016 --LTKNKANAEKLCRTYEDQ--LSEAKSKVDELQRQLAEVSTQ----RGRLQTENGELSRLLEE-KESFINQLSRGKTSF 1086
Cdd:pfam10174 151 qtLGARDESIKKLLEMLQSKglPKKSGEEDWERTRRIAEAEMQlghlEVLLDQKEKENIHLREElHRRNQLQPDPAKTKA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1087 TQTIEELK-RQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAK--------------GELQRTLSKANAEVAQWRT 1151
Cdd:pfam10174 231 LQTVIEMKdTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMevykshskfmknkiDQLKQELSKKESELLALQT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1152 KYET------DAIQRTEELEE---AKKK-----------LAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLE 1211
Cdd:pfam10174 311 KLETltnqnsDCKQHIEVLKEsltAKEQraailqtevdaLRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLD 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1212 RANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEES------------------LDNL 1273
Cdd:pfam10174 391 VKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKeriierlkeqreredrerLEEL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1274 ETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEH--EESKTLRIQLELSQIKADVE 1351
Cdd:pfam10174 471 ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAV 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1352 RKLAEKDEEFENLRRNHQRAMDS---MQATLDAEAKARNEAIRLRKKMEGDLNEMEiqlSHANRQAAESQKLVRQL---- 1424
Cdd:pfam10174 551 RTNPEINDRIRLLEQEVARYKEEsgkAQAEVERLLGILREVENEKNDKDKKIAELE---SLTLRQMKEQNKKVANIkhgq 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1425 QAQIKDLQIELDDTLRHNDDLKEQAAALerrnnlllaEVEELRAALEQaergrklAEQELLEATERVNLLHSQNTGLINH 1504
Cdd:pfam10174 628 QEMKKKGAQLLEEARRREDNLADNSQQL---------QLEELMGALEK-------TRQELDATKARLSSTQQSLAEKDGH 691
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1505 KKKIEADLAQLSSEVEEAVQECRNAEEKAKKA-ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1569
Cdd:pfam10174 692 LTNLRAERRKQLEEILEMKQEALLAAISEKDAnIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1228-1477 |
7.86e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1228 DRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISlsgKTIHELEKV 1307
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE---ERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1308 KKAL--EGEKSDIQAALEEAEGALEHeesktlriqleLSQIKAdverklaekdeeFENLRRNHQRAMDSMQATLDAEAKA 1385
Cdd:COG3883 92 ARALyrSGGSVSYLDVLLGSESFSDF-----------LDRLSA------------LSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1386 RNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELddtlrhnDDLKEQAAALERRNNLLLAEVEE 1465
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL-------AELEAELAAAEAAAAAAAAAAAA 221
|
250
....*....|..
gi 2077626420 1466 LRAALEQAERGR 1477
Cdd:COG3883 222 AAAAAAAAAAAA 233
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1245-1694 |
7.95e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1245 LESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQIslsgktiHELEKVKKALEGEKSDIQAALEE 1324
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-------EELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1325 AEGALEHeesktlriqLELSQIKADVERKLAEKDEEFENLR------RNHQRAMDSMQATL-DAEAKARNEAIRLRKKME 1397
Cdd:COG4717 121 LEKLLQL---------LPLYQELEALEAELAELPERLEELEerleelRELEEELEELEAELaELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1398 GDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTlrhNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGR 1477
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLLLLIAAALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1478 KLAEQELLEA-TERVNLLHSQNTGLINHKKKIEADLAQLsseveEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaH 1556
Cdd:COG4717 269 LSLILTIAGVlFLVLGLLALLFLLLAREKASLGKEAEEL-----QALPALEELEEEELEELLAALGLPPDLSPE-----E 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1557 LERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVrELEGELDIEQKknAETQKGIRKYERRVKELTYQTEEDR 1636
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA-GVEDEEELRAA--LEQAEEYQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1637 KNLARMQDLIDK--LQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQ 1694
Cdd:COG4717 416 GELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
1402-1525 |
8.65e-06 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 50.43 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1402 EMEIQLSHANRQAAESQKLVRQLQAQIKDLQIEL---DDTLrHNDDLKEQAAALERRNNLLLAEVEELRA---ALEQAER 1475
Cdd:pfam14817 314 HVQQFLNELAETRSRCQQLQARLQGLKDEAELESlgiGDTS-QNDSLLRQVLELELQAAGLAASRDTLRSecqQLNKLAR 392
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 1476 GRKLAEQEL-------LEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQE 1525
Cdd:pfam14817 393 ERQEALRSLqkkwqriLDFRQLVSELQEQIRALIKGNSAAKAFLIRQPAEAREFVQD 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
669-849 |
1.03e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 669 LQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHA 748
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 749 TENKVKNLI---------------------EEMAALDEIIAKLTKEKKALQEAHQQALDDLQAE----EDKVNTLTKAKV 803
Cdd:COG4942 102 QKEELAELLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALraelEAERAELEALLA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2077626420 804 KLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN 849
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1229-1434 |
1.09e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1229 RILAEWKQKFEETQAEL--ESSQKESRSLSTELFKLKNAYEESLDNLETLKRENK--NLQEEIADLTDQISLSGKTIHEL 1304
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1305 EKVKKALEGEKSDIQAALEEAEGALEhEESKTLRIQLELSQIkADVERKLAEK--------------DEEFENLRRNHQR 1370
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALP-ELLQSPVIQQLRAQL-AELEAELAELsarytpnhpdvialRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1371 AMDSMQATLDAE---AKARNEAIR-----LRKKMEgDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIE 1434
Cdd:COG3206 310 EAQRILASLEAEleaLQAREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1247-1704 |
1.25e-05 |
|
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: 50.02 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1247 SSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAE 1326
Cdd:TIGR04523 72 NSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1327 GALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKarneaIRLRKKMEGDLNEMEIQ 1406
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-----IQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1407 LSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQaaaLERRNNlllaEVEELRAALEQAERGRKLAEQEL-- 1484
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---LSEKQK----ELEQNNKKIKELEKQLNQLKSEIsd 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1485 LEATERVNLLHSQNTGLINHKKKIEADLAQLSsEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNM 1564
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKELTNSESENSEKQRE------LEEKQNEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1565 EQTIKDLQMRLDEAEQIalkggKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQD 1644
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNL-----ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1645 LIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRD 1704
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
956-1592 |
1.32e-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: 50.22 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 956 LEEATLQHESTAAVLRKKHADTVAELGEQIDNLQ-RVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQL 1034
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELNQLLRTLDdQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETA 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1035 SEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQlsRGKTSFTQTIEELKRQLEEETKSKNALAHALQAS 1114
Cdd:pfam12128 343 AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE--QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1115 rhdCDLLREQYEEEVEAKGELQRTLSKANAEVaqwrtKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKcsslek 1194
Cdd:pfam12128 421 ---ESELREQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATATPELLLQLENFDERIERAREEQEAANAE------ 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1195 tkhrlqteiedlsidLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQK----ESRSLSTELFKLKNAYEESL 1270
Cdd:pfam12128 487 ---------------VERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpQAGTLLHFLRKEAPDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1271 DNL---ETLKRENKNLQEEIADLTDQISLSGKTIHeLEKVK----KALEGEksdIQAALEEAEGALEHEESKTLRIQLEL 1343
Cdd:pfam12128 552 GKVispELLHRTDLDPEVWDGSVGGELNLYGVKLD-LKRIDvpewAASEEE---LRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1344 SQIKADVE---RKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQK- 1419
Cdd:pfam12128 628 VQANGELEkasREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKe 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1420 ----LVRQLQAQIKDLQIELDDTLrhnDDLKEQAAAL-------------ERRNNL------------LLAEVEELRAAL 1470
Cdd:pfam12128 708 qkreARTEKQAYWQVVEGALDAQL---ALLKAAIAARrsgakaelkaletWYKRDLaslgvdpdviakLKREIRTLERKI 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1471 EQAERGRK--------LAEQELLEATERVNLLHSQNTGLinhkKKIEADLAQLSSEVEEAVQECrnaeEKAKKAITDAAM 1542
Cdd:pfam12128 785 ERIAVRRQevlryfdwYQETWLQRRPRLATQLSNIERAI----SELQQQLARLIADTKLRRAKL----EMERKASEKQQV 856
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 1543 MA-EELKKEQDTSAHLERMK--KNMEQTIKDLQMRLDEAEQIALK--GGKKQIQK 1592
Cdd:pfam12128 857 RLsENLRGLRCEMSKLATLKedANSEQAQGSIGERLAQLEDLKLKrdYLSESVKK 911
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1087-1572 |
1.44e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1087 TQTIEELKRQLEEETKSKNA---LAHALQASRHdcdllreqYEEEVEAKGELQRTLSKANAEvaQWRTKYETDAIqrtEE 1163
Cdd:COG3096 251 TQSDRDLFKHLITEATNYVAadyMRHANERREL--------SERALELRRELFGARRQLAEE--QYRLVEMAREL---EE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1164 LEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRlQTEIEDLSIDLERANSAAAALDKKQrnfdrilaewkqkfEETQA 1243
Cdd:COG3096 318 LSARESDLEQDYQAASDHLNLVQTALRQQEKIERY-QEDLEELTERLEEQEEVVEEAAEQL--------------AEAEA 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1244 ELESSQKESRSLSTELFKlknaYEESLDNLETlkrenKNLQEEIAdltdqislsgktIHELEKVKKALEGEKSDIQAALE 1323
Cdd:COG3096 383 RLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAIQYQQA------------VQALEKARALCGLPDLTPENAED 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1324 EAEGALEHEESKTLRIqLELSQIKADVERKLAEKDEEFENLrrnhqRAMDSMQATLDAEAKARnEAIRL---RKKMEGDL 1400
Cdd:COG3096 442 YLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELV-----CKIAGEVERSQAWQTAR-ELLRRyrsQQALAQRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1401 NEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDtlrhNDDLKEQAAALErrnnlllAEVEELRAALEQAERGRKLA 1480
Cdd:COG3096 515 QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA----AEELEELLAELE-------AQLEELEEQAAEAVEQRSEL 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1481 EQELLEATERVNLLHSQNTGLInhkkKIEADLAQLSSEVEEAVQECRnaeekakkAITDAamMAEELKKEQDTSA---HL 1557
Cdd:COG3096 584 RQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQ--------EVTAA--MQQLLEREREATVerdEL 649
|
490
....*....|....*
gi 2077626420 1558 ERMKKNMEQTIKDLQ 1572
Cdd:COG3096 650 AARKQALESQIERLS 664
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1127-1486 |
1.58e-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: 49.74 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1127 EEVEAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAkkkLAIRLQEAEEAVEAAHAKCSSLEKtkHRLQTEIEDL 1206
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQL---LHIVQHQKAVSERQQQEKFEKMEQ--ERLRQEKEEK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1207 SIDLERANSAAAALDKKQRNFDR---ILAEWKQKFEETQAELESSQKESRslstelfklknayeesldnletlKRENKNL 1283
Cdd:pfam17380 309 AREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER-----------------------KRELERI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1284 QEEiadltdQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKtlriqlelsqikadvERKLAEKDEEFEN 1363
Cdd:pfam17380 366 RQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEER---------------QRKIQQQKVEMEQ 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1364 LRRNHQRAMDSMQATLDAEAKARNEAIRLRkkmegdlnEMEIQlshanrqaaESQKLVRQLQAQIKDLQIELDDTLRhnd 1443
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLE--------EQERQ---------QQVERLRQQEEERKRKKLELEKEKR--- 484
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2077626420 1444 dlkEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLE 1486
Cdd:pfam17380 485 ---DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1466-1668 |
1.83e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1466 LRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEavqecrnAEEKAKKAitdaammae 1545
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK-------WEEKARLA--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1546 eLKKEQDTSAH--LERmKKNMEQTIKDLQMRLDEAEQIALKgGKKQIQKLEARVRELEGELD--IEQKKNAETQKGIRKY 1621
Cdd:COG1842 78 -LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEK-LKEALRQLESKLEELKAKKDtlKARAKAAKAQEKVNEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1622 ERRVkeltyQTEEDRKNLARMQDLIDKLQSKVKSYK---------RQFEEAEQQAN 1668
Cdd:COG1842 155 LSGI-----DSDDATSALERMEEKIEEMEARAEAAAelaagdsldDELAELEADSE 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
621-792 |
2.14e-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: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 621 AQTEKEMATLKEEFQKLKEALEksevKRKELEEKQITMIQEKNDLSLHLQA--EQDNLADAEERCDLLiktkIQLEAKVK 698
Cdd:COG3883 61 EALQAEIDKLQAEIAEAEAEIE----ERREELGERARALYRSGGSVSYLDVllGSESFSDFLDRLSAL----SKIADADA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEmnaDLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQ 778
Cdd:COG3883 133 DLLEELKADKA---ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
170
....*....|....
gi 2077626420 779 EAHQQALDDLQAEE 792
Cdd:COG3883 210 AAAAAAAAAAAAAA 223
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1076-1628 |
2.59e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1076 INQLSRGKTSFTQTIEELKrqleEETKSKNALAHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYE- 1154
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLR----AEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNn 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1155 -TDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIED--------------LSIDLERANSAAAA 1219
Cdd:PRK01156 237 lKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDpvyknrnyindyfkYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1220 LDKKQRNFDRIL--AEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISls 1297
Cdd:PRK01156 317 IDAEINKYHAIIkkLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS-- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1298 gKTIHELEKVKKALEGEKSDIQAALEEAEGALEheeSKTLRIQlELSQIKADVERKLA-----------------EKDEE 1360
Cdd:PRK01156 395 -EILKIQEIDPDAIKKELNEINVKLQDISSKVS---SLNQRIR-ALRENLDELSRNMEmlngqsvcpvcgttlgeEKSNH 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1361 FENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIqlshanRQAAESQKLVRQLQAQIKDLQIELDdTLR 1440
Cdd:PRK01156 470 IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEI------NKSINEYNKIESARADLEDIKIKIN-ELK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1441 HNDDLKEQAaaLERRNNLLLAEVEELRAALEQAERGRKLAEQELLEAteRVNLLHSQNTGLINHKKKIEADLAQLSSEVE 1520
Cdd:PRK01156 543 DKHDKYEEI--KNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRS--RSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1521 EAVQECR---NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARV 1597
Cdd:PRK01156 619 KSIREIEneaNNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIED-NLKKSRKALDDAKANR 697
|
570 580 590
....*....|....*....|....*....|.
gi 2077626420 1598 RELEGELDIEQKKNAETQKGIRKYERRVKEL 1628
Cdd:PRK01156 698 ARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
692-1072 |
2.75e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 692 QLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLT 771
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 772 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDK 851
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 852 QQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVAreleelserlEEA 931
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 932 GGVTAVQLEMNKKR-EAEFLKLRrdLEEATLQ---HESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVD 1007
Cdd:pfam07888 265 AQRDRTQAELHQARlQAAQLTLQ--LADASLAlreGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 1008 DLSSNIeyltknkaNAEKLCRTYedQLSEAKSKVDELQRQLAEVSTQRGRLQTENGEL---SRLLEEK 1072
Cdd:pfam07888 343 KLEVEL--------GREKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1213-1667 |
3.57e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.64 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1213 ANSAAAALDK--KQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAyeesldnLETLKRENKNLQEEIADL 1290
Cdd:PRK10246 408 ADEVAAALAQhaEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAA-------LNEMRQRYKEKTQQLADV 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1291 tdqislsgKTIHELEKVKKALEGEKSDIQAALE------------EAEGALEHEESKTLRIQLE-------------LSQ 1345
Cdd:PRK10246 481 --------KTICEQEARIKDLEAQRAQLQAGQPcplcgstshpavEAYQALEPGVNQSRLDALEkevkklgeegaalRGQ 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1346 IKAdVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDlNEMEIQLSHANR------QAAESQK 1419
Cdd:PRK10246 553 LDA-LTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQ-EEHERQLRLLSQrhelqgQIAAHNQ 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1420 LVRQLQAQIKDLQIELDDTLRH-------NDD-----------------LKEQAAALERRNNLLLAEVEELRAALEQAER 1475
Cdd:PRK10246 631 QIIQYQQQIEQRQQQLLTALAGyaltlpqEDEeaswlatrqqeaqswqqRQNELTALQNRIQQLTPLLETLPQSDDLPHS 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1476 GRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKaitdAAMMAEElkkeqdTSA 1555
Cdd:PRK10246 711 EETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFL----AALLDEE------TLT 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1556 HLERMKKNMEQTIKDLQMRLDEAEQialkggkKQIQKLEARVRELEGELDIEQKKNAETQ--KGIRKYERRVKELTYQTE 1633
Cdd:PRK10246 781 QLEQLKQNLENQRQQAQTLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLK 853
|
490 500 510
....*....|....*....|....*....|....
gi 2077626420 1634 EDRKNLARMQDLIdklqskvksykRQFEEAEQQA 1667
Cdd:PRK10246 854 QDADNRQQQQALM-----------QQIAQATQQV 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1156-1389 |
3.68e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1156 DAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWK 1235
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1236 QKFEETqaeLESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTdqislsgKTIHELEKVKKALEGEK 1315
Cdd:COG4942 104 EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-------ADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1316 SDIQAALEEaegaLEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEA 1389
Cdd:COG4942 174 AELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
613-811 |
4.33e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 613 KIKPLLRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERcdlliktkiq 692
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 693 lEAKVKELMERLEDEEEMNAdltskkrkLEDECAELKKDIDDLEltlakvEKEKHATEnKVKNLIEEMAALDEIIAKLTK 772
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA--------LQKEIESLKRRISDLE------DEILELME-RIEELEEELAELEAELAELEA 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 2077626420 773 EKKALQEAHQQALDDLQAEEDKvntLTKAKVKLEQQVDD 811
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEE---LEAEREELAAKIPP 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
655-830 |
5.27e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 655 QITMIQEKNDLSLHLQAEQ-----DNLADAEERCDLLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELK 729
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQrkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 730 KDIDdlelTLAKVEK--EKHATENKVKNLIEEMaalDEIIAKLTKEKKALQ---EAHQQALDDLQAEEDKVNTLTKA--- 801
Cdd:PHA02562 269 SKIE----QFQKVIKmyEKGGVCPTCTQQISEG---PDRITKIKDKLKELQhslEKLDTAIDELEEIMDEFNEQSKKlle 341
|
170 180 190
....*....|....*....|....*....|
gi 2077626420 802 -KVKLEQQVDDLESSLEQEKKIRMDLERAK 830
Cdd:PHA02562 342 lKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
626-1323 |
5.58e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 626 EMATLKEEFQKLKEALEKSEVKRKEL--EEKQITMIQE-----KNDLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVK 698
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYksDETLIASRQEerqetSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMNADLTSKKRKLE--------DECAELKKDIDDLELTLAKVEKEKHATENKVK-NLIEEMAALDEIIAK 769
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADqeqlpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 770 LtKEKKALQeaHQQALDDLQAEEDKVNTltkakvKLEQQVDDLEsslEQEKKIRMDLERAKRKLEgDLKLTQESVMDLEN 849
Cdd:pfam12128 402 I-REARDRQ--LAVAEDDLQALESELRE------QLEAGKLEFN---EEEYRLKSRLGELKLRLN-QATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 850 DKQQLEEKLKkkefETSQLNSRIEDEQVLGAQLQKKIKELQARIEEleeeleaeraarakvEKQRAEvareleELSERLE 929
Cdd:pfam12128 469 FDERIERARE----EQEAANAEVERLQSELRQARKRRDQASEALRQ---------------ASRRLE------ERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 930 EAggvtAVQLEMNKKREAEFLKlrrdlEEATLQHESTAAVLRKK-------HADTVAELGEQIDNLQRVKQKLEK-EKSE 1001
Cdd:pfam12128 524 EL----ELQLFPQAGTLLHFLR-----KEAPDWEQSIGKVISPEllhrtdlDPEVWDGSVGGELNLYGVKLDLKRiDVPE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1002 MKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLaevSTQRGRLQTENGELSRLLEEKESFINQLSR 1081
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE---TFARTALKNARLDLRRLFDEKQSEKDKKNK 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1082 GKTSFTQTIEELKRQLEEEtksKNALAHALQA-SRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQR 1160
Cdd:pfam12128 672 ALAERKDSANERLNSLEAQ---LKQLDKKHQAwLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAE 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1161 TEELEEAKKKlairlqeaeeaveaAHAKCSSLEKTKHRLQTEIEDLSIDLERA---NSAAAALDKKQR--------NFDR 1229
Cdd:pfam12128 749 LKALETWYKR--------------DLASLGVDPDVIAKLKREIRTLERKIERIavrRQEVLRYFDWYQetwlqrrpRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1230 ILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADL-----TDQISLS-GKTIHE 1303
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLkedanSEQAQGSiGERLAQ 894
|
730 740
....*....|....*....|
gi 2077626420 1304 LEKVKKALEGEKSDIQAALE 1323
Cdd:pfam12128 895 LEDLKLKRDYLSESVKKYVE 914
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
669-847 |
7.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 669 LQAEQDNLADAEERCDLLIKTKIQLEAKVKELMER------LEDEEEMNADLTSkkrkLEDECAELKKDIDDLELT---L 739
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERrealqrLAEYSWDEIDVAS----AEREIAELEAELERLDASsddL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 740 AKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAkvKLEQQVDDLESSlEQE 819
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-AVE 764
|
170 180
....*....|....*....|....*...
gi 2077626420 820 KKIRMDLERAKRKLEGDLKLTQESVMDL 847
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1452-1696 |
9.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1452 LERRNnlLLAEVEELRAALEQAERgrklAEQELLEATERVNLLhsqnTGLINHKKKIEADLAQLsseveEAVQECRNAEE 1531
Cdd:COG4913 218 LEEPD--TFEAADALVEHFDDLER----AHEALEDAREQIELL----EPIRELAERYAAARERL-----AELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1532 kAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE-QIALKGGkkqiqkleARVRELEGELDIEQKK 1610
Cdd:COG4913 283 -LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGG--------DRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1611 NAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELddAEERADI 1690
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEIASL 431
|
....*.
gi 2077626420 1691 AETQVN 1696
Cdd:COG4913 432 ERRKSN 437
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
946-1108 |
1.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 946 EAEFLKLRRDLEEATLQHEStaavLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEV------------------- 1006
Cdd:COG3883 36 QAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAralyrsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1007 ---DDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGK 1083
Cdd:COG3883 112 esfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|....*
gi 2077626420 1084 TSFTQTIEELKRQLEEETKSKNALA 1108
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1387-1683 |
1.02e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1387 NEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNddlKEQAAALERRNNL------LL 1460
Cdd:PLN02939 93 SDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLN---QARLQALEDLEKIltekeaLQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1461 AEVEELRAALEQAERGRKLAEQELLeateRVNLLHSQntgLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDA 1540
Cdd:PLN02939 170 GKINILEMRLSETDARIKLAAQEKI----HVEILEEQ---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1541 AMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDIEQK---KNAET 1614
Cdd:PLN02939 243 QFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNqveKAALV 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1615 QKGIRKYERRVKELTYQTEEdrKNLARMQ-DLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDD 1683
Cdd:PLN02939 323 LDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1330-1666 |
1.10e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1330 EHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRN---HQRAMDSMQATLDAeAKAR----NEAIRLRKKME---GD 1399
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQA-ASDHlnlvQTALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1400 LNEMEIQL-------SHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQA-------AALERRNNLLLA---E 1462
Cdd:PRK04863 357 LEELEERLeeqnevvEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAiqyqqavQALERAKQLCGLpdlT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1463 VEELRAALEQAERGRKLAEQELLEATERVNL---LHSQNTGLINHKKKIEADLAQlSSEVEEAVQECRNAEEKAKKAITD 1539
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVaqaAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLREQRHLAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1540 AAMMAE--ELKKEQDTSAHLERMKK----------NMEQTIKDLQMRLdEAEQIALKGGKKQIQKLEARVRELEGELDIE 1607
Cdd:PRK04863 516 QQLRMRlsELEQRLRQQQRAERLLAefckrlgknlDDEDELEQLQEEL-EARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1608 QKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQ 1666
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAAR 653
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
619-776 |
1.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATL--KEEFQKLKEALEK-SEVKRKELEEKQITMIQEKNDLslhlqaeqdnladaEERCDLLIKTKIQLEA 695
Cdd:PRK12704 49 KEAEAIKKEALLeaKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 696 KVKELMERLEDEEEMNADLTSKKRKLEDE---CAELKKDiDDLELTLAKVEKE-KHATENKVKNLIEEmaaldeiiAKLT 771
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEE 185
|
....*
gi 2077626420 772 KEKKA 776
Cdd:PRK12704 186 ADKKA 190
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
995-1314 |
1.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 995 LEKEKSEMKMEVDDLSSnieyltKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKes 1074
Cdd:pfam00038 23 LEQQNKLLETKISELRQ------KKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1075 finqlSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVeakGELQRTLSKANAEVaqwrtkyE 1154
Cdd:pfam00038 95 -----LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEV---RELQAQVSDTQVNV-------E 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1155 TDAIqRTEELEEAKKKlaIRLQEAEEAVEaahakcsSLEKTKHRLQTEIEDLSIDLERaNSAAAALDKKQrnfdriLAEW 1234
Cdd:pfam00038 160 MDAA-RKLDLTSALAE--IRAQYEEIAAK-------NREEAEEWYQSKLEELQQAAAR-NGDALRSAKEE------ITEL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1235 KQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNletLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGE 1314
Cdd:pfam00038 223 RRTIQSLEIELQSLKKQKASLERQLAETEERYELQLAD---YQELISELEAELQETRQEMARQLREYQELLNVKLALDIE 299
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
1396-1517 |
1.33e-04 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 46.11 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1396 MEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALE---------RRNNLLLAEVEEL 1466
Cdd:COG2959 58 QQAELAQLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQqllqslsgsSRDDWLLAEAEYL 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1467 -RAALEQAERGR--KLAEQELLEATERvnLLHSQNTGLINHKKKIEADLAQLSS 1517
Cdd:COG2959 138 lRLAGQQLQLEGdvKTALAALQSADAR--LARLNDPSLLPVRRAIARDIARLRA 189
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
639-850 |
1.34e-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: 46.30 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 639 EALEKSEVKRKELEEKqitmIQEKNDLSLHLQAEQDNLADAEErcdlliktkiQLEAKVKELMERLEDEEEMNADLTSKK 718
Cdd:COG4942 20 DAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLA----------ALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 719 RKLEDECAELKKDIDDLELTLAKVEKE--KHATENKVKNL-----IEEMAALDEIIAKLTKEKKALQEAHQQALDDLQAE 791
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 792 EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRmdlERAKRKLEGDLKLTQESVMDLEND 850
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQE 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1505-1708 |
1.36e-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: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1505 KKKIEADLAQLSS---EVEEAVQECRNAEEKAKkAITDAAMMAEELKKEQDTSAHLERMKK-----NMEQTIKDLQMRLD 1576
Cdd:COG4913 220 EPDTFEAADALVEhfdDLERAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1577 EAEQiALKGGKKQIQKLEARVRELEGELD-IEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKS 1655
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDeLEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1656 YKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTRDVITS 1708
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1328-1466 |
1.37e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1328 ALEHEESKTLRIQLELSQIKADVERKLAEKDEefenlrrnhqramdsMQATLDAEAKARNEAIRLRKKMEGDLNEmEIQL 1407
Cdd:PRK09039 68 LLSLERQGNQDLQDSVANLRASLSAAEAERSR---------------LQALLAELAGAGAAAEGRAGELAQELDS-EKQV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1408 SH-ANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLA-EVEEL 1466
Cdd:PRK09039 132 SArALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAqRVQEL 192
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
510-825 |
1.54e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 510 DDKFVDSRKATEKLLNSLELDHSQYKFGHtkvFFKAGLLGHLEEMRDERLAKILTMLQARIRGrLMRIEyqKIISRREAL 589
Cdd:PLN02939 95 DDHNRASMQRDEAIAAIDNEQQTNSKDGE---QLSDFQLEDLVGMIQNAEKNILLLNQARLQA-LEDLE--KILTEKEAL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 590 YTiQWNIRAFNAVKNWSWMKLffkikpllrSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEE---KQITMIQEKN--- 663
Cdd:PLN02939 169 QG-KINILEMRLSETDARIKL---------AAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHslsKELDVLKEENmll 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 664 -DLSLHLQAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLEDEEEmnaDLtSKKRKLEDECaeLKKDIDDLELTLA-- 740
Cdd:PLN02939 239 kDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQE---DV-SKLSPLQYDC--WWEKVENLQDLLDra 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 741 --KVEK------EKHATENKVKNLIEEMAAldeiiAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQV--- 809
Cdd:PLN02939 313 tnQVEKaalvldQNQDLRDKVDKLEASLKE-----ANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESike 387
|
330
....*....|....*...
gi 2077626420 810 --DDLESSLEQEKKIRMD 825
Cdd:PLN02939 388 fqDTLSKLKEESKKRSLE 405
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1207-1541 |
2.16e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1207 SIDLERANSAAAALDKKQRNFdrilaewKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEE 1286
Cdd:PLN02939 99 RASMQRDEAIAAIDNEQQTNS-------KDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1287 IADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKadvERKLAEKDEefenlrr 1366
Cdd:PLN02939 172 INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLK---EENMLLKDD------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1367 nhqraMDSMQATLDAEAKARNEAIRLRKK---MEGDLNEMEIQLSHANRQAAESQKL-VRQLQAQIKDLQIELDDTLRHn 1442
Cdd:PLN02939 242 -----IQFLKAELIEVAETEERVFKLEKErslLDASLRELESKFIVAQEDVSKLSPLqYDCWWEKVENLQDLLDRATNQ- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1443 ddlKEQAAALERRNNLLLAEVEELRAALEQAERGRklaeqellEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEA 1522
Cdd:PLN02939 316 ---VEKAALVLDQNQDLRDKVDKLEASLKEANVSK--------FSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
|
330 340
....*....|....*....|....
gi 2077626420 1523 VQECRNA-----EEKAKKAITDAA 1541
Cdd:PLN02939 385 IKEFQDTlsklkEESKKRSLEHPA 408
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1239-1710 |
2.16e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1239 EETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTihelekvKKALEGEKS-- 1316
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLP-------KKSGEEDWErt 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1317 ----DIQAALEEAEGALEHEESKTLRIQLEL---SQIKADVERKLA------EKDEEFENLRRNHQRAMDSMQATldaea 1383
Cdd:pfam10174 185 rriaEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKTKAlqtvieMKDTKISSLERNIRDLEDEVQML----- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1384 kaRNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQ---AQIKDLQIELD-------DTLRHNDDLKEQAAALE 1453
Cdd:pfam10174 260 --KTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSkkeSELLALQTKLEtltnqnsDCKQHIEVLKESLTAKE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1454 RRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERvnllHSQNTGLINH---------------KKKIEadlaQLSSE 1518
Cdd:pfam10174 338 QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----KSTLAGEIRDlkdmldvkerkinvlQKKIE----NLQEQ 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1519 VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQTIKDLQMRLDEAEQIalkggKKQIQKLEARV 1597
Cdd:pfam10174 410 LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESL-----KKENKDLKEKV 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1598 RELEGELD------IEQKKNAETQ-KGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQskvksykrQFEEAEQQANSN 1670
Cdd:pfam10174 485 SALQPELTekesslIDLKEHASSLaSSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEI 556
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2077626420 1671 LVKYRKVQHELDDAEERADIAETQVNKLRSRTRDVITSKH 1710
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKN 596
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1437-1711 |
2.25e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.08 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1437 DTLRHNDDLKEQAAALERRNN--------LLLAEVEELRAALEQaergrkLAEQELLEATERVNLLHSQNTglinhkkkI 1508
Cdd:PLN03188 961 EVLRTKIELKRVQDELEHYRNfydmgereVLLEEIQDLRSQLQY------YIDSSLPSARKRNSLLKLTYS--------C 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1509 EADLAQLSSEVEEAVQECrnAEEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI 1581
Cdd:PLN03188 1027 EPSQAPPLNTIPESTDES--PEKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQM 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1582 ALKGGKKQIQK----------LEARVREL-EGeldIEQKKNAETQKGIRKYERR--------VKELTYQTEEDRKNLarm 1642
Cdd:PLN03188 1105 AMEGHARMLEQyadleekhiqLLARHRRIqEG---IDDVKKAAARAGVRGAESKfinalaaeISALKVEREKERRYL--- 1178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1643 QDLIDKLQSKVksykRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAE-------TQVNKLRSRTRDVITSKHE 1711
Cdd:PLN03188 1179 RDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRKHENEISTLNQ 1250
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
961-1172 |
2.45e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 961 LQHESTAAVLRKKHADtVAELGEQIDNLQRVKQKLEKEKSE-MKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKS 1039
Cdd:PRK05771 36 LKEELSNERLRKLRSL-LTKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELEN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1040 KVDELQRQLAEVStqrgRLQTENGELSRLLEEK--ESFINQLSRGKTSFTQTIEElKRQLEEETKSKN-----ALAHALQ 1112
Cdd:PRK05771 115 EIKELEQEIERLE----PWGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESD-VENVEYISTDKGyvyvvVVVLKEL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1113 ASRHDCDLLREQYEE-EVEAKGELQRTLSKANAEVAQWRTKYEtdaiQRTEELEEAKKKLA 1172
Cdd:PRK05771 190 SDEVEEELKKLGFERlELEEEGTPSELIREIKEELEEIEKERE----SLLEELKELAKKYL 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
747-1001 |
2.50e-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: 45.53 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 747 HATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQekkirmdL 826
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 827 ERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEF----ETSQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEA 902
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 903 ERAARAKVEKQRAEVAreleelserleeaggvtavqlemnkkreaeflKLRRDLEEATLQHESTAAVLRKK---HADTVA 979
Cdd:COG4942 169 LEAERAELEALLAELE--------------------------------EERAALEALKAERQKLLARLEKElaeLAAELA 216
|
250 260
....*....|....*....|..
gi 2077626420 980 ELGEQIDNLQRVKQKLEKEKSE 1001
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAA 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1173-1368 |
2.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1173 IRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELES--SQK 1250
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1251 ESRSLSTElfklknayeesldnLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALE 1330
Cdd:COG1579 90 EYEALQKE--------------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 2077626420 1331 HEESKtlrIQLELSQIKADVERKLAEKdeeFENLRRNH 1368
Cdd:COG1579 156 AELEE---LEAEREELAAKIPPELLAL---YERIRKRK 187
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
617-780 |
2.97e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 617 LLRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLslhLQAEQDNLADAEERCDLLIKTKIQLEAK 696
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE---EALEEQLEAEREELLEELLEEEELLEEE 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 697 VKELMERLEDEEEMNADLTSKKRKLE----------DECAELKKDIDDLeltlakveKEKHATenkvknLIEEMAALDEI 766
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEalgpvnllaiEEYEELEERYDFL--------SEQRED------LEEARETLEEA 817
|
170
....*....|....*
gi 2077626420 767 IAKLTKEKK-ALQEA 780
Cdd:COG1196 818 IEEIDRETReRFLET 832
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1279-1490 |
2.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1279 ENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEgalehEESKTLRIQLelsqikADVERKLAEKD 1358
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-----AEIDKLQAEI------AEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1359 EEFENLRRNHQRA----------------------MDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAE 1416
Cdd:COG3883 86 EELGERARALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1417 SQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATER 1490
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1235-1546 |
3.64e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.70 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1235 KQKFEeTQAELESSQKESRSLSTELFKLKNAYEesLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGE 1314
Cdd:PLN03188 953 KEKYE-NHPEVLRTKIELKRVQDELEHYRNFYD--MGEREVLLEEIQDLRSQLQYYIDSSLPSARKRNSLLKLTYSCEPS 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1315 K----SDIQAALEE-AEGALEHE-------ESKTLRIQLELsQIKADVERKLAEKDE-EFENLRRNHQRAMDSMQATL-- 1379
Cdd:PLN03188 1030 QapplNTIPESTDEsPEKKLEQErlrwteaESKWISLAEEL-RTELDASRALAEKQKhELDTEKRCAEELKEAMQMAMeg 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1380 ---------DAEAKARNEAIRLRKKMEGdLNEMEIQLSHANRQAAESqKLVRQLQAQIKDLQIELDDTLRHNDD------ 1444
Cdd:PLN03188 1109 harmleqyaDLEEKHIQLLARHRRIQEG-IDDVKKAAARAGVRGAES-KFINALAAEISALKVEREKERRYLRDenkslq 1186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1445 --LKEQAAALERRNNLL--LAEVEElraALEQAERGRKLAEQELLEATERVNLLhsqntglinhKKKIEADLaqlsSEVE 1520
Cdd:PLN03188 1187 aqLRDTAEAVQAAGELLvrLKEAEE---ALTVAQKRAMDAEQEAAEAYKQIDKL----------KRKHENEI----STLN 1249
|
330 340
....*....|....*....|....*.
gi 2077626420 1521 EAVQECRNAEEKAKKAITDAAMMAEE 1546
Cdd:PLN03188 1250 QLVAESRLPKEAIRPACNDDCMAKYD 1275
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1286-1492 |
3.99e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.02 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1286 EIADLTDQISLSGKTIHELEKV-----KKALEGEKSDIQAALEEAEGALEHEESKTLRiQLELSQIKA---DVERKLAEK 1357
Cdd:pfam05667 276 DLAELLSSFSGSSTTDTGLTKGsrfthTEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEqleDLESSIQEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1358 DEEFENLRRNHQRAMDSMQaTLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDD 1437
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELE-ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIE 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 1438 TLRhndDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQ---ELLEATERVN 1492
Cdd:pfam05667 434 EYR---ALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEElykQLVAEYERLP 488
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
984-1173 |
4.09e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 984 QIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRgrlqteng 1063
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1064 ELSRLLEEKESfinqLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEakgELQRTLSKAN 1143
Cdd:COG1579 90 EYEALQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELE 162
|
170 180 190
....*....|....*....|....*....|
gi 2077626420 1144 AEVAQWRTKYETDAIQRTEELEEAKKKLAI 1173
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRKRKNGLAV 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
700-1137 |
4.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 700 LMERLEdeEEMNADLTSKKRKLEDECAELKKDIDDLeltlakveKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQE 779
Cdd:COG4717 47 LLERLE--KEADELFKPQGRKPELNLKELKELEEEL--------KEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 780 aHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRmDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLK 859
Cdd:COG4717 117 -ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 860 KKEFET-SQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQR--------AEVARELEELSERLEE 930
Cdd:COG4717 195 QDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 931 AGGVTAVQLEM-----------NKKREAEFLKLRRDLEEATLQHESTAAVLRKKHADT------VAELGEQIDNLQRVKQ 993
Cdd:COG4717 275 IAGVLFLVLGLlallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeeLLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 994 KLEKEKSEMKMEvddlssniEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKE 1073
Cdd:COG4717 355 EAEELEEELQLE--------ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1074 SfiNQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDcDLLREQYEEEVEAKGELQR 1137
Cdd:COG4717 427 E--EELEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRE 487
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1590-1699 |
4.86e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1590 IQKLEARVRELEGE-----LDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQfEEAE 1664
Cdd:COG2433 382 LEELIEKELPEEEPeaereKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE-ERRE 460
|
90 100 110
....*....|....*....|....*....|....*....
gi 2077626420 1665 QQANSNLVKYRK----VQHELDDAEERADIAETQVNKLR 1699
Cdd:COG2433 461 IRKDREISRLDReierLERELEEERERIEELKRKLERLK 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1342-1555 |
5.16e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1342 ELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLV 1421
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1422 RQLQA--------QIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNL 1493
Cdd:COG3883 107 VLLGSesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1494 LHSQntglinhKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1555
Cdd:COG3883 187 LSAE-------EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1557-1678 |
5.17e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1557 LERMKK-NMEQTIKDLQMRLDEAE------QIALKGGKKQIQKLEARVRELEGELDIEQKKNAETQkgirkyeRRVKELT 1629
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2077626420 1630 YQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVkyRKVQ 1678
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
880-1115 |
5.96e-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: 44.37 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 880 AQLQKKIKELQARIEELEEeleaeraaraKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREAeflkLRRDLEEA 959
Cdd:COG4942 23 AEAEAELEQLQQEIAELEK----------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 960 TLQhestAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKS 1039
Cdd:COG4942 89 EKE----IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1040 KVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHALQASR 1115
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
829-1055 |
7.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 829 AKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIedeqvlgAQLQKKIKELQARIEELEEELEAERAARA 908
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 909 KVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREAEFLKLRRDLEEATLQHESTAAVLRKkhadTVAELGEQIDNL 988
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA----DLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 989 QRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQR 1055
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
696-1311 |
8.04e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 696 KVKELMERLEDEEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEiiakltkekk 775
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 776 alqeahqqALDDLQAEEDKVNTLTKAKVKLEQqvdDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLE 855
Cdd:PRK01156 240 --------ALNELSSLEDMKNRYESEIKTAES---DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 856 EKLKKKEFETSQLNSRIEdeqvlgaqLQKKIKELQArieeleeeleaERAARAKVEKQRAEVARELEELSERLEEAGGVT 935
Cdd:PRK01156 309 NKKQILSNIDAEINKYHA--------IIKKLSVLQK-----------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 936 AVQLEMNKKREAEFLKLRR---DLEEATLQHESTAAVLRKKHadtvAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSN 1012
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1013 IEYL-----------TKNKANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGEL-SRLLEEKESFINQLS 1080
Cdd:PRK01156 446 MEMLngqsvcpvcgtTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1081 RGKTSFTQTIEELKRQLEEETKSKNALAhalQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKYETDAIQR 1160
Cdd:PRK01156 526 SARADLEDIKIKINELKDKHDKYEEIKN---RYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1161 TEELEeakkklaIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERansaaaaLDKKQRNFDRILAEwKQKFEE 1240
Cdd:PRK01156 603 LQEIE-------IGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK-------LRGKIDNYKKQIAE-IDSIIP 667
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1241 TQAELESSQKESrslSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKAL 1311
Cdd:PRK01156 668 DLKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
884-1325 |
8.15e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 8.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 884 KKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSErleeaggVTAVQLEMNKKREAEFLKLRRDLEEATLQH 963
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-------LREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 964 ESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVD-DLSSNIEYLTKNKANAEKLCRTYEDQLSEAKSKVD 1042
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1043 ELQRQLAEVSTQRgrlqtENGELSRLLEEKESFINQLSR--GKTSFTQTIEELKRQLEEETKSKNALAHALQASRHDCDL 1120
Cdd:COG4717 224 ELEEELEQLENEL-----EAAALEERLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1121 LREQYEEEVEAKGELQRTlskANAEVAQWRTKYETDAIQRTEELEEAKKKLA-IRLQEAEEAVEAAHAKCSSLEKTKHRL 1199
Cdd:COG4717 299 SLGKEAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLELLDRIEeLQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1200 QTEIedLSIDLERANSAAAALDKKQrnfdrilaEWKQKFEETQAELESSQKESRSLSTELFK--LKNAYEESLDNLETLK 1277
Cdd:COG4717 376 LAEA--GVEDEEELRAALEQAEEYQ--------ELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELE 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2077626420 1278 RENKNLQEEIADLTDQISLSGKTiHELEKVKKALEGEKSDIQAALEEA 1325
Cdd:COG4717 446 EELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEW 492
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
631-893 |
8.46e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 631 KEEFQKLKEALEKSEVKRKELEEKQITMIQ--EKNDLSLH--LQAEQDNLADAEErcdllikTKIQLEAKVKELMERLED 706
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRlkKKYLEALNkkLNEKESQLADARE-------VISCLKNELSELRRQIQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 707 EEEMNADLTSKKRKLEDECAELKKDIDDLEL---TLAKVEKEKHATENKVKNLIEEMA--ALDEIIAKLTKEKKALQEAH 781
Cdd:pfam05557 123 AELELQSTNSELEELQERLDLLKAKASEAEQlrqNLEKQQSSLAEAEQRIKELEFEIQsqEQDSEIVKNSKSELARIPEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 782 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIR---MDLERAKRKLEGDLK----------LTQESVMDLE 848
Cdd:pfam05557 203 EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYReeaATLELEKEKLEQELQswvklaqdtgLNLRSPEDLS 282
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2077626420 849 NDKQQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQARI 893
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKI 327
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
712-891 |
1.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 712 ADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQALDDLQ-- 789
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 790 -------------------------------AEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLK 838
Cdd:COG3883 99 ggsvsyldvllgsesfsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 839 LTQESVMDLENDKQQLEEKLKKKEFETSQLNSRIEDEQVLGAQLQKKIKELQA 891
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
622-835 |
1.22e-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: 43.35 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 622 QTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQitmiQEKNDLSLHLQAEQDNLADAEErcdlliktkiQLEAKVKELm 701
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSEELSEEKDALLAQRA----------AHEARIREL- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 702 erledeEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMaaldeiiAKLTKEKKALQEAH 781
Cdd:pfam07888 135 ------EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL-------RSLSKEFQELRNSL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 782 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEG 835
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1314-1474 |
1.24e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1314 EKSDIQAALEEAEGALEHEESKTLRIQLELSQIKAdVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLR 1393
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQA-LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1394 KKMEGDLNEMEiQLSHANRQAAESQKLVRQLQAQIKdlQIELDDTLRHNDDLKEQAAALERRNnlllAEVEELRAALEQA 1473
Cdd:pfam00529 131 VLAPIGGISRE-SLVTAGALVAQAQANLLATVAQLD--QIYVQITQSAAENQAEVRSELSGAQ----LQIAEAEAELKLA 203
|
.
gi 2077626420 1474 E 1474
Cdd:pfam00529 204 K 204
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1499-1695 |
1.27e-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: 42.40 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1499 TGLINHKKKIEADLAQLSSEVEEAVQECRNAEEK---AKKAITDAAMMAEEL-KKEQDTSAHLERMKKNMEQTIKDLQMR 1574
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQieiLEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1575 LDEAEQIAlkggkKQIQKLEARVRELEGELDIE-----QKKNAETQKGIRkyERRVKELTYQTEEDRKNLARMQDLIDKL 1649
Cdd:pfam06008 88 AEAIKNLI-----DNIKEINEKVATLGENDFALpssdlSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2077626420 1650 QSKVKSYKRQFEEAEQQANSNLVKYrkvQHELDDAEERADIAETQV 1695
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKT 203
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1270-1485 |
1.51e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1270 LDNLETLKRENKNLQEEIADLTDQI--------SLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEH---------- 1331
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKISELRQKKgaepsrlySLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDfrqkyedeln 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1332 ------EESKTLRIQL-ELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLD--------------------AEAK 1384
Cdd:pfam00038 97 lrtsaeNDLVGLRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdtqvnvemdaarkldltsalAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1385 ARNEAIRLRKKMEGDlNEMEIQLSHANRQAAESQKLVRQLQAQIKD-------LQIELDDTLRHNDDLKEQAAALERRNN 1457
Cdd:pfam00038 177 AQYEEIAAKNREEAE-EWYQSKLEELQQAAARNGDALRSAKEEITElrrtiqsLEIELQSLKKQKASLERQLAETEERYE 255
|
250 260 270
....*....|....*....|....*....|....*
gi 2077626420 1458 LLLAEVEELRAALEQA------ERGRKLAE-QELL 1485
Cdd:pfam00038 256 LQLADYQELISELEAElqetrqEMARQLREyQELL 290
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1344-1712 |
1.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1344 SQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAK--ARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLV 1421
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKktETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAE 1143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1422 RQLQAQiKDLQIELDDTLRHNDDLKEQAAALERRnnlllaEVEELRAALE--QAERGRKLAEQELLEATERvnllhsqnt 1499
Cdd:PTZ00121 1144 EARKAE-DAKRVEIARKAEDARKAEEARKAEDAK------KAEAARKAEEvrKAEELRKAEDARKAEAARK--------- 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1500 glinhkkkieadlaqlsSEVEEAVQECRNAEEKAKkaiTDAAMMAEELKKEQDTSAHLERMKKNME-QTIKDLQMRLDEA 1578
Cdd:PTZ00121 1208 -----------------AEEERKAEEARKAEDAKK---AEAVKKAEEAKKDAEEAKKAEEERNNEEiRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1579 EQIALKGGKK----QIQKLEaRVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKnlarmqdlidklqsKVK 1654
Cdd:PTZ00121 1268 RQAAIKAEEArkadELKKAE-EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK--------------KAD 1332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2077626420 1655 SYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRSRTrDVITSKHEE 1712
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAEE 1389
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1033-1143 |
1.65e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1033 QLSEAKSKVDELqrqLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKS--KNALAHA 1110
Cdd:PRK00409 510 LIGEDKEKLNEL---IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaiKEAKKEA 586
|
90 100 110
....*....|....*....|....*....|....
gi 2077626420 1111 LQASRHDCDLLREQYEEEVEAK-GELQRTLSKAN 1143
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHElIEARKRLNKAN 620
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1202-1709 |
1.74e-03 |
|
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: 43.50 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1202 EIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTEL----FKLKNAYEESLDNLETLK 1277
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgFERGPFSERQIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1278 REN-----KNLQEEIADLTDQISLSGKTIHELEKvkkalegEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVER 1352
Cdd:TIGR00606 400 IERqedeaKTAAQLCADLQSKERLKQEQADEIRD-------EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1353 KLAEKDEEFENLRRNHQRAMDSMQATLDAEAKA-RNEAIRLRKKMEGDLNEMEiQLSHANRQAAESQKLVRQlqAQIKDL 1431
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKD--KMDKDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1432 QIElDDTLRHNDDLKEQAAALERRnnlllaevEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEAD 1511
Cdd:TIGR00606 550 QIR-KIKSRHSDELTSLLGYFPNK--------KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1512 LAQLSSEVEEAV------QECRNAEEKAKKAITDAAMMA----------EELKKEQDTSAHL----ERMKKNMEQTIKDL 1571
Cdd:TIGR00606 621 LSSYEDKLFDVCgsqdeeSDLERLKEEIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVcqrvFQTEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1572 QMRLDEAEQiALKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQS 1651
Cdd:TIGR00606 701 QSKLRLAPD-KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMP 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1652 KVKSYK------------------------------------RQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQV 1695
Cdd:TIGR00606 780 EEESAKvcltdvtimerfqmelkdverkiaqqaaklqgsdldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
570
....*....|....
gi 2077626420 1696 NKLRSRTRDVITSK 1709
Cdd:TIGR00606 860 QHLKSKTNELKSEK 873
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
731-844 |
1.83e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 731 DIDDLELTLAKVEKEKHATENkvknliEEMAALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVD 810
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....
gi 2077626420 811 DLESSLEQekkirmdLERAKRKLEGDLKLTQESV 844
Cdd:COG0542 486 KIPELEKE-------LAELEEELAELAPLLREEV 512
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
637-779 |
1.85e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 637 LKEALEKSEVKRKELEEKqitmiqeknDLSLHLQAEQDNLADAEERCDlliktkiQLEAKVKELMERLEDeeemnadlts 716
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIR-------RLEEQVERLEAEVEE---------- 431
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 717 kkrkLEDECAELKKDIDDLELTLAKV---EKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQE 779
Cdd:COG2433 432 ----LEAELEEKDERIERLERELSEArseERREIRKDREISRLDREIERLERELEEERERIEELKR 493
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
685-822 |
1.97e-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: 42.31 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 685 LLIKTKIQLEAKV------KELMERLEDEEEMNADLtskkrkLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIE 758
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrMKLLEGLKEGLDENLEG------LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQ 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2077626420 759 -----------EMAALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKI 822
Cdd:smart00787 194 ledeledcdptELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGF 268
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1531-1712 |
2.04e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1531 EKAKKAITdaamMAEELKKEQDTSAHLERmkKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDIEQKK 1610
Cdd:COG1196 210 EKAERYRE----LKEELKELEAELLLLKL--RELEAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1611 NAETQKGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADI 1690
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180
....*....|....*....|..
gi 2077626420 1691 AETQVNKLRSRTRDVITSKHEE 1712
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEEL 384
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1421-1523 |
2.43e-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: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1421 VRQLQAQIKDLQIELDDTLRHNDDL-KEQAAALERRnnllLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNT 1499
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEAsFERLAELRDE----LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|....
gi 2077626420 1500 GLINHKKKIEADLAQLSSEVEEAV 1523
Cdd:COG0542 489 ELEKELAELEEELAELAPLLREEV 512
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1316-1475 |
2.43e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.96 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1316 SDIQAALEEAEGALEheeskTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAmdsmQATLDaeakaRNEaiRLRKK 1395
Cdd:COG1566 79 TDLQAALAQAEAQLA-----AAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLA----QRELE-----RYQ--ALYKK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1396 meGDLNEMEIQLSHANRQAAESQklVRQLQAQIKDLQIELDDtlrhnddlKEQAAALErrnnlllAEVEELRAALEQAER 1475
Cdd:COG1566 143 --GAVSQQELDEARAALDAAQAQ--LEAAQAQLAQAQAGLRE--------EEELAAAQ-------AQVAQAEAALAQAEL 203
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
866-1490 |
2.49e-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: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 866 SQLNSRIEDEQVLGAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEaggvtaVQLEMNKKR 945
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKD------LIKENNATR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 946 E-AEFLKLR-RDLEEATLQHESTAAVLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYL----TKN 1019
Cdd:pfam05483 155 HlCNLLKETcARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLeeeyKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1020 KANAEKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQtengELSRLLEEKesfINQLSRGKTSFTQTIEELKRQLEE 1099
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE----EKTKLQDEN---LKELIEKKDHLTKELEDIKMSLQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1100 ETKSKNALAHALQASRHDCDLLREQYEEEVEakgelqrTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAE 1179
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQME-------ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1180 EAVEAAHAKCSSLE---KTKHRLQTEIEDLSIDLERANSaaaaLDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLS 1256
Cdd:pfam05483 381 IITMELQKKSSELEemtKFKNNKEVELEELKKILAEDEK----LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1257 TELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLsgktiheLEKVKKALEGEKSDIQAALEEAEGALEHEESKT 1336
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK-------LLLENKELTQEASDMTLELKKHQEDIINCKKQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1337 LRIqleLSQIKADVERKLAEKDeEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAE 1416
Cdd:pfam05483 530 ERM---LKQIENLEEKEMNLRD-ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 1417 SQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATER 1490
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEK 679
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1340-1599 |
2.50e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1340 QLELSQIKADVERKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARneairlRKKMEGDLNEMEIQL-SHANRQAAESQ 1418
Cdd:NF041483 82 QIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQR------RQQLDQELAERRQTVeSHVNENVAWAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1419 KLVRQLQAQIKDL----QIELDDTLRHNDDLKEQAAALERRNnlLLAEVEELRAALEQ--------AERGRKLAEQELLE 1486
Cdd:NF041483 156 QLRARTESQARRLldesRAEAEQALAAARAEAERLAEEARQR--LGSEAESARAEAEAilrrarkdAERLLNAASTQAQE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1487 ATERVNLLHSQNTGLINHKKKIEADLA----QLSSEVEEAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTSAHLER 1559
Cdd:NF041483 234 ATDHAEQLRSSTAAESDQARRQAAELSraaeQRMQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTRTAKEE 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2077626420 1560 MKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRE 1599
Cdd:NF041483 314 IARLVGEATKEAEALKAEAEQ-ALADARAEAEKLVAEAAE 352
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1328-1698 |
2.51e-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: 42.63 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1328 ALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAMDS----MQATLDAEAKARNEA------IRLRKKME 1397
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHlnlvQTALRQQEKIERYQEdleeltERLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1398 GdLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDdtLRHNDDLKEQAA--ALERRNNLLLA----------EVEE 1465
Cdd:COG3096 369 V-VEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALD--VQQTRAIQYQQAvqALEKARALCGLpdltpenaedYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1466 LRAALEQAERGRKLAEQELLEATERvnllHSQntglinHKKKIEAdLAQLSSEVEEAvqecrNAEEKAKKAITDA----- 1540
Cdd:COG3096 446 FRAKEQQATEEVLELEQKLSVADAA----RRQ------FEKAYEL-VCKIAGEVERS-----QAWQTARELLRRYrsqqa 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1541 -AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMR----LDEAEQIALkggkkQIQKLEARVRELEGELDIEQKKNAETQ 1615
Cdd:COG3096 510 lAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRigqqLDAAEELEE-----LLAELEAQLEELEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1616 KGIRKYERRVKELTYQTEEDRKNLARMQDLIDKLQSKVKSyKRQFEEAEQQAnsnLVKYRKVQHELDDAEERADIAETQV 1695
Cdd:COG3096 585 QQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALAD-SQEVTAAMQQL---LEREREATVERDELAARKQALESQI 660
|
...
gi 2077626420 1696 NKL 1698
Cdd:COG3096 661 ERL 663
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
543-850 |
2.91e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 543 FKAGLLGHLEEMRDERLAKILTMLQ-ARIRGRLMRIEYQKIISRREALYTIQWNIRAFNAVKNWSWMKLFF----KIKPL 617
Cdd:pfam15818 5 FKTSLLEALEELRMRREAETQYEEQiGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAleeeKGKYQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 618 LRSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKqitmiqekndLSLHLQAEQDNLADAEE--RCDLLIKTKIQLea 695
Cdd:pfam15818 85 LATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQK----------LQLHLLAKEDHHKQLNEieKYYATITGQFGL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 696 kVKELMERLE----DEEEMNADLTSKKRKLEDECAELKKDIDDL--ELTLAKVE-KEKHATEN--------KVKNLIEEM 760
Cdd:pfam15818 153 -VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqKFQELQERL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 761 AALDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEqqvddleSSLEQEKKIRMDLERAKRKLEGDLKLT 840
Cdd:pfam15818 232 NMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEME-------AELKALKENNQTLERDNELQREKVKEN 304
|
330
....*....|
gi 2077626420 841 QESVMDLEND 850
Cdd:pfam15818 305 EEKFLNLQNE 314
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
808-1353 |
3.12e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 808 QVDDLESSLEQEKKIRMD-------LERAKRKLEGDLKLTQESVMDLENdkqqLEEKLKKKEFETSQLNSRIEDEQVLGA 880
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDeileinsLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 881 QLQKKIKELQARIEELEEEL----------EAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEM-------NK 943
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYnnlksalnelSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIindpvykNR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 944 KREAEFLKLRRDLEEATLQHESTAAVLRKKHADTvaelgEQIDNLQRVKQKLEKEKSEMkmevDDLSSNIEYLTKNKANA 1023
Cdd:PRK01156 295 NYINDYFKYKNDIENKKQILSNIDAEINKYHAII-----KKLSVLQKDYNDYIKKKSRY----DDLNNQILELEGYEMDY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1024 EKLCRTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKS 1103
Cdd:PRK01156 366 NSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1104 KNALAHALQASRHDCDL-------LREQYEEEV----EAKGELQRTLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLA 1172
Cdd:PRK01156 446 MEMLNGQSVCPVCGTTLgeeksnhIINHYNEKKsrleEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1173 ---IRLQEAEEAVEAAHAKCSSLEKTKHRLQT-EIEDL---------------SIDLERANSAAAALDKKQRNFDRILAE 1233
Cdd:PRK01156 526 sarADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLdskrtswlnalavisLIDIETNRSRSNEIKKQLNDLESRLQE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1234 WKQKFEETQAELESSQKEsrsLSTELFKLKNAYEESLDN---LETLKRENKNLQEEIADLtDQISLSGKTIH----ELEK 1306
Cdd:PRK01156 606 IEIGFPDDKSYIDKSIRE---IENEANNLNNKYNEIQENkilIEKLRGKIDNYKKQIAEI-DSIIPDLKEITsrinDIED 681
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2077626420 1307 VKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERK 1353
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESM 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-780 |
3.14e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKsevKRKELEEKQITMIQEKNDLSLHLQAEQDNLADA--------------EERCD 684
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEA---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkylaparREQAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 685 LLIKTKIQLEAKVKELMERLEDEEEMNADLTSKKRKLEDECAELKKdiddlelTLAKVEKEKHATENKVKNLIEEMAALD 764
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK-------LLARLEKELAELAAELAELQQEAEELE 226
|
170
....*....|....*.
gi 2077626420 765 EIIAKLTKEKKALQEA 780
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
694-795 |
3.33e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.31 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 694 EAKVKELMERLED--EEEMNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLT 771
Cdd:NF033838 310 EKKVEEAKKKAKDqkEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLE 389
|
90 100
....*....|....*....|....*...
gi 2077626420 772 K----EKKALQEAHQQAlddlqAEEDKV 795
Cdd:NF033838 390 KiktdRKKAEEEAKRKA-----AEEDKV 412
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1410-1490 |
3.35e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.06 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1410 ANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATE 1489
Cdd:pfam11932 25 AVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERELVPLMLKMLD 104
|
.
gi 2077626420 1490 R 1490
Cdd:pfam11932 105 R 105
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1231-1699 |
3.35e-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: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1231 LAEWKQKFEETQAELESSQKESRSlstELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKA 1310
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKR---ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1311 LEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVER---KLAEKDEEFENLRRNHQ------RAMDSMQATLDA 1381
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRaelELQSTNSELEELQERLDllkakaSEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1382 EAKARNEAIRLRKKMEGDLNEMEiqlshanrQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEqaaaLERRNNLLLA 1461
Cdd:pfam05557 161 QQSSLAEAEQRIKELEFEIQSQE--------QDSEIVKNSKSELARIPELEKELERLREHNKHLNE----NIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1462 EVEELRAALEQAERGRKLA----------EQELLE-----------------ATERVNLLHSQNTGLINHKKKIEADLAQ 1514
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAatlelekeklEQELQSwvklaqdtglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1515 LSSEVEEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQMRLDE 1577
Cdd:pfam05557 309 LEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1578 AEQIALKGgKKQIQKLEARVRELEGELDI--EQKKNAETQKGIRKYERRVKELTYQTEED---RKNLARMQDLIDKLQSK 1652
Cdd:pfam05557 385 AEDMTQKM-QAHNEEMEAQLSVAEEELGGykQQAQTLERELQALRQQESLADPSYSKEEVdslRRKLETLELERQRLREQ 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2077626420 1653 VKSYKRQFEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLR 1699
Cdd:pfam05557 464 KNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQ 510
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
630-1108 |
3.36e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 630 LKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQA---EQDNLADAEERCDLLIKTKIQLEAKVKELMERLED 706
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 707 EEEMNADLTS--------------KKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIakltk 772
Cdd:PRK01156 268 ELEKNNYYKEleerhmkiindpvyKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI----- 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 773 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQE------------------KKIRMDLERAKRKLE 834
Cdd:PRK01156 343 KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiseilkiqeidpdaiKKELNEINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 835 GDLKLTQESVMDLENDKQQLEEKLKKKEF-------------------------ETSQLNSRIEDEQVLGAQLQKKIKEL 889
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhyneKKSRLEEKIREIEIEVKDIDEKIVDL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 890 QAR--------IEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGVTAVQLEMNKKREAEFLKL---RRDLEE 958
Cdd:PRK01156 503 KKRkeyleseeINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNAlavISLIDI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 959 ATLQHESTAavLRKKHADTVAELGEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDqLSEAK 1038
Cdd:PRK01156 583 ETNRSRSNE--IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN-YKKQI 659
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 1039 SKVDELQRQLAEVSTQRGRLQTENGELSRLLE-------EKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALA 1108
Cdd:PRK01156 660 AEIDSIIPDLKEITSRINDIEDNLKKSRKALDdakanraRLESTIEILRTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1347-1540 |
3.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1347 KADVERKLAEKDEEFENLRRNHQRAMDSMQAtlDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQA 1426
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1427 QIKDLQIELDDTLRHNDDLKEQAAALErrnnlllAEVEELRA-ALEQAERGRKL----AEQELLEATErvnllhsqntgl 1501
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKE-------EELEELIEeQLQELERISGLtaeeAKEILLEKVE------------ 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 2077626420 1502 inhkKKIEADLAQLSSEVEEAVQEcrNAEEKAKKAITDA 1540
Cdd:PRK12704 165 ----EEARHEAAVLIKEIEEEAKE--EADKKAKEILAQA 197
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
630-849 |
3.54e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 630 LKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSLHLQAEQDNLADAEERCDLLiktkiqlEAKVKELMERLEDEEE 709
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 710 MNADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEIIAKLTKEKKALQEAHQQA----- 784
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdtalt 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2077626420 785 -LDDLQAEEDKV-NTLTKAKVKLEQQVDDLESSLEQEKKirmDLERAKRKLEGDLKLTQESVMDLEN 849
Cdd:pfam10174 440 tLEEALSEKERIiERLKEQREREDRERLEELESLKKENK---DLKEKVSALQPELTEKESSLIDLKE 503
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1164-1359 |
3.57e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1164 LEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEI-------EDLSIDLERANSAAAALDKKQRNFDRILAEW-- 1234
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYek 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1235 -------KQKFEETQAELESSQKESRSLSTELFKLKNAYEEsldnLETLKRENKNLQEEIADLTDQISLSGKTIhelekv 1307
Cdd:PHA02562 284 ggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE----LEEIMDEFNEQSKKLLELKNKISTNKQSL------ 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2077626420 1308 kKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDE 1359
Cdd:PHA02562 354 -ITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1480-1669 |
3.90e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1480 AEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1558
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1559 RMKKNMEQT-----------IKDLQMRLDEAEQIAlKGGKKQIQKLEARVRELEGELDIEQKKNAETQKGIRKYERRVKE 1627
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2077626420 1628 LTYQTEEDRKNLARMQDLIDKLQSKVKSYKRQFEEAEQQANS 1669
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK05560 |
PRK05560 |
DNA gyrase subunit A; Validated |
694-801 |
4.01e-03 |
|
DNA gyrase subunit A; Validated
Pssm-ID: 235502 [Multi-domain] Cd Length: 805 Bit Score: 41.94 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 694 EAKvKELMERLE-DEEEMNA--D-----LTSKKR-KLEDECAELKKDIDDLELTLAKvekekhatENKVKNLIEEmaALD 764
Cdd:PRK05560 400 EAK-EGLMERFGlSEIQAQAilDmrlqrLTGLERdKIEDEYKELLALIADLKDILAS--------PERLLEIIKE--ELL 468
|
90 100 110
....*....|....*....|....*....|....*....
gi 2077626420 765 EIIAKLTKEKKALQEAHQQALD--DLQAEEDKVNTLTKA 801
Cdd:PRK05560 469 EIKEKFGDPRRTEIIEGEGDIDdeDLIPEEDVVVTLTHG 507
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
712-849 |
4.09e-03 |
|
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: 41.20 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 712 ADLTSKKRKLEDECAELKKDIDDLELTLAKVEKEKHATENKVKNLIEEMAALDEII-AKLTKEKKALQeahQQALDDLQA 790
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALkDLLTDEGGAIA---RKEIKDLQK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2077626420 791 EEDKVNTLTKAKVK-----LEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN 849
Cdd:cd22656 187 ELEKLNEEYAAKLKakideLKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1042-1428 |
4.14e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1042 DELQRQLAEVsTQRGRLQTENGELSRLLEEKESFINQLSRGKtsftQTIEELKRQLE---EETKSKNALAHALQASrhDC 1118
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAqapAKLRQAQAELEALKDD--ND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1119 DLLREQYE----EEVEAK--------GELQRTLSKANAEVAQWRTKYE------TDAIQRTEELEEAKKKLAIrlqeaee 1180
Cdd:PRK11281 112 EETRETLStlslRQLESRlaqtldqlQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKGGKV------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1181 aveaahAKCSSLEKTKHRLQTEIE--DLSIDLER----ANSAAAALDKKQRNF----------------DRILAEWKQKF 1238
Cdd:PRK11281 185 ------GGKALRPSQRVLLQAEQAllNAQNDLQRksleGNTQLQDLLQKQRDYltariqrlehqlqllqEAINSKRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1239 EETQAELESSQKESRS-----LSTEL---FKLKNAYEESLDNLETLKREN--------------KNLQEEIADLTDQISL 1296
Cdd:PRK11281 259 EKTVQEAQSQDEAARIqanplVAQELeinLQLSQRLLKATEKLNTLTQQNlrvknwldrltqseRNIKEQISVLKGSLLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1297 SgkTIheLEKVKKALEGEKSDIQAALEEAEGALEheesktlriQLELSQikadvER-KLAEKDEEFENLRRNHQRAMDsm 1375
Cdd:PRK11281 339 S--RI--LYQQQQALPSADLIEGLADRIADLRLE---------QFEINQ-----QRdALFQPDAYIDKLEAGHKSEVT-- 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 1376 qatlDAEAKARNEAIRLRKKMEGDLN-EMEIQLSHA-----NRQ--AAESQKLVRQLQAQI 1428
Cdd:PRK11281 399 ----DEVRDALLQLLDERRELLDQLNkQLNNQLNLAinlqlNQQqlLSVSDSLQSTLTQQI 455
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
687-779 |
4.19e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 41.13 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 687 IKTKIQLEAKVKELMERLEdeeemnaDLTSKKRKLEDECAELKKDIDdlELTLAKVEKEKHATENKVKNLIEEMAALDEI 766
Cdd:pfam03961 141 TKTEIEVGVDFPELKEKLE-------ELEKELEELEEELEKLKKRLK--KLPKKARGQLPPEKREQLEKLLETKNKLSEE 211
|
90
....*....|...
gi 2077626420 767 IAKLTKEKKALQE 779
Cdd:pfam03961 212 LEELEEELKELKE 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1391-1541 |
4.53e-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: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1391 RLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQIELDDTLRHNDDLKEQ--AAALERRNNLLLAEVEELra 1468
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESL-- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1469 aleqaERGRKLAEQELLEATERVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAA 1541
Cdd:COG1579 102 -----KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1273-1439 |
4.57e-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: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1273 LETLKRENKNLQEEIADLTDQISlsgktihELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELSQIKADVER 1352
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1353 KLAEKdeEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQLQAQIKDLQ 1432
Cdd:COG1579 92 EALQK--EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
....*..
gi 2077626420 1433 IELDDTL 1439
Cdd:COG1579 170 AKIPPEL 176
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1191-1338 |
4.62e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1191 SLEKTKHRLQTEIEDLSidlERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESL 1270
Cdd:pfam09787 65 KLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1271 DNLETlkrenknlqeEIADLTDQI---SLSGKTIHELEK--------------VKKALEGEKSDIQAALEEAEGALEHEE 1333
Cdd:pfam09787 142 KDREA----------EIEKLRNQLtskSQSSSSQSELENrlhqltetliqkqtMLEALSTEKNSLVLQLERMEQQIKELQ 211
|
....*
gi 2077626420 1334 SKTLR 1338
Cdd:pfam09787 212 GEGSN 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1031-1258 |
4.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1031 EDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKRQLEEETKSKNALAHA 1110
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1111 LQASRHDCDLLreqyEEEVEAKG--------ELQRTLSKANAEVAQwrtkyetDAIQRTEELEEAKKKLAIRLQEAEEAV 1182
Cdd:COG3883 95 LYRSGGSVSYL----DVLLGSESfsdfldrlSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2077626420 1183 EAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRILAEWKQKFEETQAELESSQKESRSLSTE 1258
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1305-1685 |
5.17e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1305 EKVKKALEGEKSDIQAALEEAEGALEHEE-SKTLRIQLELSQIKADVERKLAEKDEEFEnlrrnhqramdsmqATLDAEA 1383
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhTQNVALNKKLSDIKTEYLYELNVLKEKSE--------------AELTSKT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1384 KARNEAIRlrKKMEGDLNEMEIQLSHANRQAAESQKlvrqlqaqikdlqielddtlrhnddlKEQAAALERRNNLLLAEV 1463
Cdd:NF033838 120 KKELDAAF--EQFKKDTLEPGKKVAEATKKVEEAEK--------------------------KAKDQKEEDRRNYPTNTY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1464 EELRAALEQAERGRKLAEQELLEATERVnllhSQNTGLINH-KKKIEADLAQlSSEVEEAVQECRNAEEKAKKaiTDAAM 1542
Cdd:NF033838 172 KTLELEIAESDVEVKKAELELVKEEAKE----PRDEEKIKQaKAKVESKKAE-ATRLEKIKTDREKAEEEAKR--RADAK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1543 MAEELKKEQDTSAHlERMKKNMEQTIKDLQMRLDEAEQIAlKGGKKQIQKLEARVRELEGEldieqKKNAETQKGIRKYE 1622
Cdd:NF033838 245 LKEAVEKNVATSEQ-DKPKRRAKRGVLGEPATPDKKENDA-KSSDSSVGEETLPSPSLKPE-----KKVAEAEKKVEEAK 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1623 RRVKEltyQTEEDRKNLA--RMQDL---IDKLQSKVKSYKRQF--EEAEQQANSNLVKYRKVQHELDDAE 1685
Cdd:NF033838 318 KKAKD---QKEEDRRNYPtnTYKTLeleIAESDVKVKEAELELvkEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1342-1487 |
6.35e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.99 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1342 ELSQIKADVERKLAEKD-EEFENLRRNHQRAMDSMQA---TLDAEAKArnEAIR-LRKKMEGDLNEMEIQLSHANRQAAE 1416
Cdd:COG3524 169 QLSERAREDAVRFAEEEvERAEERLRDAREALLAFRNrngILDPEATA--EALLqLIATLEGQLAELEAELAALRSYLSP 246
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1417 SQKLVRQLQAQIKDLQIELddtlrhnDDLKEQAAALERRNNL--LLAEVEELRAALEQAERGRKLAEQELLEA 1487
Cdd:COG3524 247 NSPQVRQLRRRIAALEKQI-------AAERARLTGASGGDSLasLLAEYERLELEREFAEKAYTSALAALEQA 312
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1188-1345 |
6.59e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1188 KCSSLEKTKHRLQTEIEDLSIDLERansaaaaLDKKQRNFDRILAEWKQKFEETQAELESSQKESRSL----STELFKLK 1263
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKL-------LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1264 NAyeesldnLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKtLRIQLEL 1343
Cdd:smart00787 211 EK-------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEK-LKEQLKL 282
|
..
gi 2077626420 1344 SQ 1345
Cdd:smart00787 283 LQ 284
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1270-1552 |
6.81e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.30 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1270 LDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKVKKALEGEKSDIQAALEEAEGALEHEESKTLRIQLELS----- 1344
Cdd:pfam18971 548 LNNLAITSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYDEVKKAQKDLEKSlrkre 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1345 QIKADVERKLAEKDEEFENLRRNHQ--RAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSH------------- 1409
Cdd:pfam18971 628 HLEKEVEKKLESKSGNKNKMEAKAQanSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKiskdlkdfsksfd 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1410 -----ANRQAAESQKLVRQLQAQIKDLQIelddtlrhnddlkeqaaalerrNNLLLAEVEELRAALEQAERGRKLAEQEL 1484
Cdd:pfam18971 708 efkngKNKDFSKAEETLKALKGSVKDLGI----------------------NPEWISKVENLNAALNEFKNGKNKDFSKV 765
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2077626420 1485 LEAteRVNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEK-AKKAITDAAMMAEELKKEQD 1552
Cdd:pfam18971 766 TQA--KSDLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVlADLKNFSKEQLAQQAQKNED 832
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1531-1704 |
6.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1531 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIalkggkKQIQKLEARVRELEGELDIEQKK 1610
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1611 NAETQKGIRKYERRVKELtyqtEEDRKNLARMQDLIDKLQSKVK-SYKRQFEEAEQQANSNLVKYRKVQHELDDAEERAD 1689
Cdd:COG4717 148 LEELEERLEELRELEEEL----EELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*
gi 2077626420 1690 IAETQVNKLRSRTRD 1704
Cdd:COG4717 224 ELEEELEQLENELEA 238
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
670-818 |
7.22e-03 |
|
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: 40.43 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 670 QAEQDNLADAEERCDLLIKTKIQLEAKVKELMERLedeeemnadltskkRKLEDECAELKKDIDDLELTL-AKVEKEKHA 748
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKL--------------TDFENQTEKDQTALETLEKALkDLLTDEGGA 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2077626420 749 TENK-VKNLIEEMAALDEIIAKLTKEKkalQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQ 818
Cdd:cd22656 176 IARKeIKDLQKELEKLNEEYAAKLKAK---IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGP 243
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
696-778 |
7.23e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 696 KVKELMERLEDEEEMNAdlTSKKRKLEDECAELKKDIDDLELTLAKVEKEkhatenkVKNLIEEMAALDEIIAKLTKEKK 775
Cdd:PRK05771 54 KLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIE 124
|
...
gi 2077626420 776 ALQ 778
Cdd:PRK05771 125 RLE 127
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1028-1176 |
7.23e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1028 RTYEDQLSEAKSKVDELQRQLAEVSTQRGRLQTENGELSRLLEEKESFINQLSRGKTSFTQTIEELKrQLEEETKSKNAL 1107
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLA-QAQIDLARRRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1108 AHALQASRHDCDLLREQYEEEVEAKGELQRTLSKANAEVAQWRTKY----ETDAIQRTEELEEAKKKLAIRLQ 1176
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENqaevRSELSGAQLQIAEAEAELKLAKL 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1421-1605 |
7.91e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1421 VRQLQAQIKDLQiELD---DTLRHN-DDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHS 1496
Cdd:COG1579 2 MPEDLRALLDLQ-ELDselDRLEHRlKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1497 QNTGLINHKkkieaDLAQLSSEVEEAVQECRNAEEKAKKAItdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQMRLD 1576
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....*....
gi 2077626420 1577 EAEQIAlkggKKQIQKLEARVRELEGELD 1605
Cdd:COG1579 149 EELAEL----EAELEELEAEREELAAKIP 173
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
619-800 |
8.35e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 39.94 E-value: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 619 RSAQTEKEMATLKEEFQKLKEALEKSEVKRKELEEKQITMIQEKNDLSlhlqaeqDNLADAEERCDLLIKTKIQLEaKVK 698
Cdd:pfam15934 45 EQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLQSMITGYSDIS-------ENNRLKEEIHDLKQKNCVQAR-VVR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 699 ELMERLEDEEEMNADLTSKKRKL----EDECAELK---KDIDDLELTLAKVEKEKHATENKVKNLIEEMAALdeiiaklt 771
Cdd:pfam15934 117 KMGLELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL-------- 188
|
170 180 190
....*....|....*....|....*....|...
gi 2077626420 772 KEKKALQEAHQQALDD----LQAEEDKVNTLTK 800
Cdd:pfam15934 189 KEKDAKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1233-1312 |
8.63e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.10 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1233 EWKQKFEETQAELESSQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISLSGKTIHELEKvKKALE 1312
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK-KRLLE 210
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1425-1616 |
9.40e-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: 39.63 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1425 QAQIKDLQIELDDTLRHNDDLKEQAAALERRNNLL--------------LAEVEELRAALEQAERGRKLAEQELLEATER 1490
Cdd:pfam00261 14 EERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLeeelerteerlaeaLEKLEEAEKAADESERGRKVLENRALKDEEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1491 VNLLHSQNTGLINHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE-------RMKKN 1563
Cdd:pfam00261 94 MEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekasEREDK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1564 MEQTIKDLQMRLDEAEQIALKgGKKQIQKLEARVRELEGELDIEQKKNAETQK 1616
Cdd:pfam00261 174 YEEQIRFLTEKLKEAETRAEF-AERSVQKLEKEVDRLEDELEAEKEKYKAISE 225
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1276-1424 |
9.47e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1276 LKRENKNLQEEIADLTDQISLSGKTIHELEK---VKKALEGEKSDIQAALEEAEGALEHEES-KTLRIQLELSQIKADVE 1351
Cdd:COG2268 214 IAIAQANREAEEAELEQEREIETARIAEAEAelaKKKAEERREAETARAEAEAAYEIAEANAeREVQRQLEIAEREREIE 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2077626420 1352 RKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAESQKLVRQL 1424
Cdd:COG2268 294 LQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKL 366
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1239-1582 |
9.81e-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: 40.71 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1239 EETQAELESSQKESRSLSTELFKLKNAYEESLD-NLETLKRENKNLQEEIADLTDQISLSGKTiHELEKVKKALEGEKsd 1317
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNeNANNLIKQFENTKEKIAEYTKSIDIKKAT-ESLEEQLAAAEAEQ-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1318 iqaaleEAEGALEHEESKTLRIQLELSQIKADVERKLAEKDEEFENLRRNHQRAmdsmqatlDAEAKARNEAIRLRKKME 1397
Cdd:COG5185 326 ------ELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELS--------KSSEELDSFKDTIESTKE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1398 GDLNemeiqlshanrqaaesqkLVRQLQAQIKDLQIELDDTLRHNDDlkeqaaalerrnnlllaEVEELRAALEQAERGR 1477
Cdd:COG5185 392 SLDE------------------IPQNQRGYAQEILATLEDTLKAADR-----------------QIEELQRQIEQATSSN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077626420 1478 KLAEQELLEATERVNLlhsqntgliNHKKKIEADLAQLSSEVEEAVQECRNAEEKAKKAITDAAMMAEELK-KEQDTSAH 1556
Cdd:COG5185 437 EEVSKLLNELISELNK---------VMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKaTLEKLRAK 507
|
330 340
....*....|....*....|....*.
gi 2077626420 1557 LERMKKNMEQTIKDLQMRLDEAEQIA 1582
Cdd:COG5185 508 LERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| |
