|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
13-569 |
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: 1210.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14927 120 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA 172
Cdd:cd14927 200 KPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 EADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPR 252
Cdd:cd14927 280 EADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 253 QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILSI 332
Cdd:cd14927 360 QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 333 LEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKS 412
Cdd:cd14927 440 LEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 413 QNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLV 492
Cdd:cd14927 520 QNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLV 599
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142940 493 LHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14927 600 LHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
1-569 |
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: 1112.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1 MICSGPHSR----CHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQL 76
Cdd:cd01377 99 SVAASSKKKkesgKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 77 PGERGYHVYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALL 156
Cdd:cd01377 179 KGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAIL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 157 HFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFR 236
Cdd:cd01377 259 HLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 237 WLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDL 316
Cdd:cd01377 339 WLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 317 QPCIDLIEKP-LGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLE 395
Cdd:cd01377 419 QPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKKSEAHFILKHYAGDVEYNIDGWLE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 396 KNKDPLNETVVPIFQKSQNRLLATLYENYAGScsteppKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRC 475
Cdd:cd01377 496 KNKDPLNENVVALLKKSSDPLVASLFKDYEES------GGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRC 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 476 IVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDID 555
Cdd:cd01377 570 IIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDGKAACEKILKALQLD 648
|
570
....*....|....
gi 1907142940 556 HTQYQFGHTKVFFK 569
Cdd:cd01377 649 PELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
8-569 |
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: 965.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 8 SRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQ 87
Cdd:cd14929 106 SKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQ 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 88 ILSGKKpELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ 167
Cdd:cd14929 186 ILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 168 REEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD 247
Cdd:cd14929 265 REEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 248 TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL 327
Cdd:cd14929 345 AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKrKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd14929 425 GIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVA 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATLYENYAGSCSTEPpkSGVKeKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVM 487
Cdd:cd14929 504 VFQKSSNRLLASLFENYISTDSAIQ--FGEK-KRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVL 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 488 DSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVF 567
Cdd:cd14929 581 DPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVF 660
|
..
gi 1907142940 568 FK 569
Cdd:cd14929 661 FK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
12-569 |
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: 956.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14913 115 KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14913 195 KKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14913 275 AEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLP 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14913 355 RQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKRKyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14913 435 ILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-EAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd14913 514 SSNRLLAHLYATFA---TADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSL 590
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14913 591 VLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
12-569 |
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: 909.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14917 115 KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14917 195 KKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14917 275 AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQP 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14917 355 RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14917 435 ILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAGScstEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd14917 514 SSLKLLSNLFANYAGA---DAPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPL 590
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14917 591 VMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
12-569 |
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: 888.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14916 116 KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14916 196 KKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14916 276 AEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14916 356 RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRpDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14916 436 ILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAGSCSTEPPKSgvKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd14916 515 SSLKLMATLFSTYASADTGDSGKG--KGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPL 592
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14916 593 VMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
12-569 |
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: 862.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14923 116 QGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14923 196 KKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14923 276 AEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14923 356 RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFS 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14923 436 ILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAGscsTEPPKSGVKEK--RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDS 489
Cdd:cd14923 515 SSLKLLSFLFSNYAG---AEAGDSGGSKKggKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 490 FLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14923 592 YLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
12-569 |
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: 850.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14918 115 QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14918 195 KKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQ 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14918 275 AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQP 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14918 355 RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFS 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14918 435 ILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAgscSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd14918 514 SAMKTLASLFSTYA---SAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHEL 590
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14918 591 VLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
12-569 |
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: 849.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14910 117 QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14910 197 KKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14910 277 AEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14910 357 RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFS 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14910 437 ILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQK 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLyenYAGSCSTEPPKSGVKE-KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSF 490
Cdd:cd14910 516 SSMKTLALL---FSGAAAAEAEEGGGKKgGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHE 592
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 491 LVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14910 593 LVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
4-569 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 849.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 4 SGPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYH 83
Cdd:pfam00063 113 SGSGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYH 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 84 VYYQILSGKKPELQDMLLLSmNPYDYHFCSQ-GVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMK 162
Cdd:pfam00063 193 IFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 163 FKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRI 242
Cdd:pfam00063 272 FKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRI 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 243 NQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCID 321
Cdd:pfam00063 352 NKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCID 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 322 LIE-KPLGILSILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPRPdkkrKYQAHFEVVHYAGVVPYSIVGWLEKNKDP 400
Cdd:pfam00063 431 LIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 401 LNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK-EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPN 479
Cdd:pfam00063 506 LNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKStPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPN 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 480 ENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDIDHTQY 559
Cdd:pfam00063 586 EKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEY 664
|
570
....*....|
gi 1907142940 560 QFGHTKVFFK 569
Cdd:pfam00063 665 QFGKTKIFFR 674
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
12-569 |
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: 848.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14915 117 QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14915 197 KKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14915 277 AEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14915 357 RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFS 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14915 437 ILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQK 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYEnyAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd14915 516 SGMKTLAFLFS--GGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHEL 593
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14915 594 VLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
4-569 |
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: 847.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 4 SGPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYH 83
Cdd:cd14934 103 TGKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYH 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 84 VYYQILSGKKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKF 163
Cdd:cd14934 183 IFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 164 KQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRIN 243
Cdd:cd14934 263 KQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRIN 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 244 QTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLI 323
Cdd:cd14934 343 KTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 EKPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNE 403
Cdd:cd14934 423 EKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 404 TVVPIFQKSQNRLLATLYENyagscstEPPKSGVKeKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKT 483
Cdd:cd14934 503 TVVGLFQKSSLGLLALLFKE-------EEAPAGSK-KQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQ 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 484 PGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDIDHTQYQFGH 563
Cdd:cd14934 575 SGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKASELLLGSIDLDVNEYKIGH 653
|
....*.
gi 1907142940 564 TKVFFK 569
Cdd:cd14934 654 TKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
12-569 |
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: 840.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14912 117 QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14912 197 KKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQ 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14912 277 AEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQP 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14912 357 RQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFS 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14912 437 ILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQK 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENyAGSCSTEPPKSGVKE-KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSF 490
Cdd:cd14912 516 SAMKTLAYLFSG-AQTAEGASAGGGAKKgGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHE 594
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 491 LVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14912 595 LVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
12-569 |
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: 840.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14909 113 KGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14909 193 SVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQ 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14909 273 AEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQK 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPLGILS 331
Cdd:cd14909 353 RQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILS 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd14909 433 ILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKK 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAGscSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd14909 513 SQNKLLIEIFADHAG--QSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHL 590
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTfvDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14909 591 VMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
13-581 |
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: 804.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:smart00242 127 GSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSMnPYDYHFCSQGVT-TVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:smart00242 207 SEELKKELGLKS-PEDYRYLNQGGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEA-DGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKL 250
Cdd:smart00242 286 ASTvKDKEELSNAAELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGI 329
Cdd:smart00242 366 GSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGI 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 330 LSILEEECMFPKASDASFRAKLYDNHSgKSPNFQQPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIF 409
Cdd:smart00242 445 LSLLDEECRFPKGTDQTFLEKLNQHHK-KHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELL 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 410 QKSQNRLLATLYENYAGScsteppksgvKEKRKKaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDS 489
Cdd:smart00242 520 QSSKNPLIASLFPSGVSN----------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDS 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 490 FLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFvDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:smart00242 587 SLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLR 665
|
570
....*....|..
gi 1907142940 570 AGLLGILEELRD 581
Cdd:smart00242 666 PGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
13-902 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 697.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:COG5022 188 SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGD 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSmNPYDYHFCSQG-VTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKqKQREEQ 171
Cdd:COG5022 268 PEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFK-EDRNGA 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:COG5022 346 AIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEK--PLGI 329
Cdd:COG5022 426 ASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGI 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 330 LSILEEECMFPKASDASFRAKLYDN-HSGKSPNFQqprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPI 408
Cdd:COG5022 505 LSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFK-----KSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 409 FQKSQNRLLATLYENYagscsteppksgvkEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMD 488
Cdd:COG5022 580 LKASTNEFVSTLFDDE--------------ENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFD 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 489 SFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFV---DSRKATEKLLGSLDIDHTQYQFGHTK 565
Cdd:COG5022 646 NQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVKSILEELVIDSSKYQIGNTK 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 566 VFFKAGLLGILEELRDQRLAKVLTLLQARSRGRLMRLEYQRMLGGRDALFTIQWNIRAFNAVKNWSWMKLFFKMKPLLRS 645
Cdd:COG5022 726 VFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSL 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 646 AQAEEELAALRAELRGLRGALaTAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKEL 725
Cdd:COG5022 806 LGSRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 726 SERLEDEEEVNAdLAARRRKLEDECTELKKDID-----DLELTLAKAEKEKQATEN-KVKNLTEEMAALDEAVVRLTKEK 799
Cdd:COG5022 885 QELKIDVKSISS-LKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNNiDLEEGPSIEYVKLPELNKLHEVE 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 800 KALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQET---VTDTTQDK 876
Cdd:COG5022 964 SKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASkiiSSESTELS 1043
|
890 900
....*....|....*....|....*.
gi 1907142940 877 QQLEEKLKKKDSELSQLNLRVEDEQL 902
Cdd:COG5022 1044 ILKPLQKLKGLLLLENNQLQARYKAL 1069
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
4-569 |
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: 683.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 4 SGPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYH 83
Cdd:cd00124 105 GSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFH 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 84 VYYQILSGKKPELQDMLLLSMNPYDYHF----CSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFG 159
Cdd:cd00124 185 IFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 160 NMKFKQKQREE--QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRW 237
Cdd:cd00124 265 NIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDW 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 238 LVSRINQTLDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLD 315
Cdd:cd00124 345 LVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PD 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 316 LQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFqqprpDKKRKYQAHFEVVHYAGVVPYSIVGWL 394
Cdd:cd00124 424 NQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF-----SKKRKAKLEFGIKHYAGDVTYDADGFL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 395 EKNKDPLNETVVPIFQKSqnrllatlyenyagscsteppksgvkekrkkaASFqtvsqlhKENLNKLMTNLRATQPHFVR 474
Cdd:cd00124 499 EKNKDTLPPDLVDLLRSG--------------------------------SQF-------RSQLDALMDTLNSTQPHFVR 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 475 CIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDI 554
Cdd:cd00124 540 CIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKA-SDSKKAAVLALLLLLKL 618
|
570
....*....|....*
gi 1907142940 555 DHTQYQFGHTKVFFK 569
Cdd:cd00124 619 DSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
5-569 |
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: 650.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 5 GPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHV 84
Cdd:cd14911 115 AVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 85 YYQILSGKKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFK 164
Cdd:cd14911 195 FYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 165 QKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQ 244
Cdd:cd14911 274 QERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 245 TLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLI 323
Cdd:cd14911 354 SLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLI 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 EKPLGILSILEEECMFPKASDASFRAKLYDNHSgKSPNFqqprpdKKRKYQ--AHFEVVHYAGVVPYSIVGWLEKNKDPL 401
Cdd:cd14911 434 DKPGGIMALLDEECWFPKATDKTFVDKLVSAHS-MHPKF------MKTDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPL 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 402 NETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVK-EKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNE 480
Cdd:cd14911 507 NENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNH 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 481 NKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDIDHTQYQ 560
Cdd:cd14911 587 EKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYR 665
|
....*....
gi 1907142940 561 FGHTKVFFK 569
Cdd:cd14911 666 VGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
12-569 |
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: 627.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14920 113 PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQ-DMLLLSMNpyDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE 170
Cdd:cd14920 193 AGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 171 QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TK 249
Cdd:cd14920 271 QASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 250 LPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL-- 327
Cdd:cd14920 351 RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnp 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 -GILSILEEECMFPKASDASFRAKLyDNHSGKSPNFQQPRpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVV 406
Cdd:cd14920 431 pGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVA 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 407 PIFQKSQNRLLATLYENY-----AGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNEN 481
Cdd:cd14920 507 TLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 482 KTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPdDTFVDSRKATEKLLGSLDIDHTQYQF 561
Cdd:cd14920 587 KRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRI 665
|
....*...
gi 1907142940 562 GHTKVFFK 569
Cdd:cd14920 666 GQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
7-569 |
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: 587.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 7 HSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYY 86
Cdd:cd01380 103 GSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFY 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 87 QILSGK-KPELQDmLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ 165
Cdd:cd01380 183 QLCAAAsLPELKE-LHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 166 KQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQT 245
Cdd:cd01380 262 TRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 246 LDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI 323
Cdd:cd01380 342 LASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLI 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 EKPLGILSILEEECMFPKASDASFRAKLYDNHSGK-SPNFQQPRPDKKRkyqahFEVVHYAGVVPYSIVGWLEKNKDPLN 402
Cdd:cd01380 421 EGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA-----FIVKHFADDVEYQVEGFLEKNRDTVS 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 403 ETVVPIFQKSQNRllatlyenyagscsteppksgvkekrKKaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENK 482
Cdd:cd01380 496 EEHLNVLKASKNR--------------------------KK-----TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEK 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 483 TPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAipDDTFVDSRKATEKLLGSLDIDHTQYQFG 562
Cdd:cd01380 545 LPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--EWLRDDKKKTCENILENLILDPDKYQFG 622
|
....*..
gi 1907142940 563 HTKVFFK 569
Cdd:cd01380 623 KTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
12-569 |
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: 576.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14932 117 HGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14932 197 AGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKL 250
Cdd:cd14932 276 ASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL--- 327
Cdd:cd14932 356 QGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgpp 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEECMFPKASDASFRAKLYdNHSGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd14932 436 GILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKP---KKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVAT 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATLYENY---------AGSCSTEppkSGVKEKRKkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd14932 512 LLNQSTDKFVSELWKDVdrivgldkvAGMGESL---HGAFKTRK--GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIP 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 479 NENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDIDHTQ 558
Cdd:cd14932 587 NHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACVLMVKALELDPNL 665
|
570
....*....|.
gi 1907142940 559 YQFGHTKVFFK 569
Cdd:cd14932 666 YRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
13-569 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 560.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14921 114 GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQ-DMLLLSMNpyDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14921 194 KEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKL 250
Cdd:cd14921 272 ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDkTHR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL--- 327
Cdd:cd14921 352 QGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnpp 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEECMFPKASDASFRAKLYdNHSGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd14921 432 GVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKP---KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTS 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATLYEN---------YAGSCSTEPPKSgvkeKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd14921 508 LLNASSDKFVADLWKDvdrivgldqMAKMTESSLPSA----SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIP 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 479 NENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDIDHTQ 558
Cdd:cd14921 584 NHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNL 662
|
570
....*....|.
gi 1907142940 559 YQFGHTKVFFK 569
Cdd:cd14921 663 YRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
2-569 |
2.49e-178 |
|
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: 553.16 E-value: 2.49e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 2 ICSGPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERG 81
Cdd:cd14919 100 VASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 82 YHVYYQILSGKKPELQDMLLLSmnPYD-YHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGN 160
Cdd:cd14919 180 FHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGN 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 161 MKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVS 240
Cdd:cd14919 258 IVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 241 RINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPC 319
Cdd:cd14919 338 RINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPC 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 320 IDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEK 396
Cdd:cd14919 418 IDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP---KQLKDKADFCIIHYAGKVDYKADEWLMK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 397 NKDPLNETVVPIFQKSQNRLLATLYEN---------YAGSCSTEPPksGVKEKRKkaASFQTVSQLHKENLNKLMTNLRA 467
Cdd:cd14919 494 NMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALP--GAFKTRK--GMFRTVGQLYKEQLAKLMATLRN 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 468 TQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEK 547
Cdd:cd14919 570 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVL 648
|
570 580
....*....|....*....|..
gi 1907142940 548 LLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14919 649 MIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
12-569 |
1.07e-177 |
|
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: 551.59 E-value: 1.07e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd15896 117 HGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd15896 197 AGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKL 250
Cdd:cd15896 276 ASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKPL--- 327
Cdd:cd15896 356 QGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAspp 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd15896 436 GILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---KKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVAT 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATLYENYAGSCSTEpPKSGVKEK----RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKT 483
Cdd:cd15896 512 LLNQSTDKFVSELWKDVDRIVGLD-KVSGMSEMpgafKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKK 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 484 PGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLGSLDIDHTQYQFGH 563
Cdd:cd15896 591 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQ 669
|
....*.
gi 1907142940 564 TKVFFK 569
Cdd:cd15896 670 SKVFFR 675
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
4-569 |
2.19e-177 |
|
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: 549.55 E-value: 2.19e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 4 SGPHSRchqgtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYH 83
Cdd:cd01381 101 SGQHSW-----IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYH 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 84 VYYQILSGKKPELQDMLLLSMnPYDYHFCSQG-VTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMK 162
Cdd:cd01381 176 IFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 163 FKQKQRE--EQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVS 240
Cdd:cd01381 255 FEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVN 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 241 RINQTLDTKLPRQFF---IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQ 317
Cdd:cd01381 335 KINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQ 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 318 PCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHSGKSpNFQQPrpdkKRKYQAHFEVVHYAGVVPYSIVGWLEK 396
Cdd:cd01381 414 DVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNK-NYLKP----KSDLNTSFGINHFAGVVFYDTRGFLEK 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 397 NKDPLNETVVPIFQKSQNRLLATLYENYAGSCSteppksgvkEKRKKAasfQTVSQLHKENLNKLMTNLRATQPHFVRCI 476
Cdd:cd01381 489 NRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 477 VPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSaIPDDTFVDSRKATEKLLGSLDIDH 556
Cdd:cd01381 557 KPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG-IPPAHKTDCRAATRKICCAVLGGD 635
|
570
....*....|...
gi 1907142940 557 TQYQFGHTKVFFK 569
Cdd:cd01381 636 ADYQLGKTKIFLK 648
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
2-569 |
2.47e-174 |
|
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: 542.38 E-value: 2.47e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 2 ICSGPHSRCHQGT---LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPG 78
Cdd:cd14930 100 VASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 79 ERGYHVYYQILSGKKPELQDMLLLSMNPYdYHFCSQGVTTVDNMDDgEELIATDHAMDILGFSVDEKCACYKIVGALLHF 158
Cdd:cd14930 180 ECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPGQER-ELFQETLESLRVLGFSHEEITSMLRMVSAVLQF 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 159 GNMKFKQKQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWL 238
Cdd:cd14930 258 GNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 239 VSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDL 316
Cdd:cd14930 338 VLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 317 QPCIDLIEKPL---GILSILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPRpdkKRKYQAHFEVVHYAGVVPYSIVGW 393
Cdd:cd14930 417 QPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR---HLRDQADFSVLHYAGKVDYKANEW 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 394 LEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKS---GVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQP 470
Cdd:cd14930 493 LMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNP 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 471 HFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtFVDSRKATEKLLG 550
Cdd:cd14930 573 SFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKG-FMDGKQACEKMIQ 651
|
570
....*....|....*....
gi 1907142940 551 SLDIDHTQYQFGHTKVFFK 569
Cdd:cd14930 652 ALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
17-569 |
5.09e-172 |
|
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: 535.59 E-value: 5.09e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 17 DQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPEL 96
Cdd:cd01378 113 DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 97 QDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADg 176
Cdd:cd01378 193 LQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 177 TESADKAAYLMGVSSGDLLKGLLHPRVRVGNEY---VTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ 253
Cdd:cd01378 272 TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGK 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 254 -FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQhmFVL--EQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPLGI 329
Cdd:cd01378 352 kKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 330 LSILEEECMFP-KASDASFRAKLydNHSGKSPNFQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPI 408
Cdd:cd01378 429 FAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKEL 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 409 FQKSQNRLLATLYEnyagscstEPPKSGVKeKRKKAASFQTvsqlhKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMD 488
Cdd:cd01378 507 MQSSSNPFLRSLFP--------EGVDLDSK-KRPPTAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFD 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 489 SFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFvDSRKATEKLLGSLDIDHTQYQFGHTKVFF 568
Cdd:cd01378 573 EELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFI 651
|
.
gi 1907142940 569 K 569
Cdd:cd01378 652 R 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
16-569 |
2.46e-166 |
|
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: 520.73 E-value: 2.46e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 16 EDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKK-- 93
Cdd:cd14883 108 EQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhs 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 94 PELQDMLLLSmNPYDYHFCSQ-GVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA 172
Cdd:cd14883 188 KELKEKLKLG-EPEDYHYLNQsGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 E-ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLP 251
Cdd:cd14883 267 LtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 252 RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEK-PLGIL 330
Cdd:cd14883 347 NSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGIL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 331 SILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPrpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQ 410
Cdd:cd14883 426 KLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---DRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMS 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 411 KSQNRLLATL--YENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMD 488
Cdd:cd14883 502 RSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFD 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 489 SFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTfVDSRKATEKLLGSLDIDHTQYQFGHTKVFF 568
Cdd:cd14883 582 DELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADH-KETCGAVRALMGLGGLPEDEWQVGKTKVFL 660
|
.
gi 1907142940 569 K 569
Cdd:cd14883 661 R 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
11-569 |
5.22e-165 |
|
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: 516.48 E-value: 5.22e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 11 HQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILS 90
Cdd:cd01383 101 GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 91 GKKPELQDMLLLSMnPYDYHFCSQ-GVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE 169
Cdd:cd01383 181 GASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 170 EQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDT- 248
Cdd:cd01383 260 NHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVg 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 249 KLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPL 327
Cdd:cd01383 340 KRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEECMFPKASDASFRAKLyDNHSGKSPNFqqprpdKKRKYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd01383 419 GLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQ 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATLYENYAGSCSTEPPKSgvkeKRKKAASF-QTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGV 486
Cdd:cd01383 491 LLSSCSCQLPQLFASKMLDASRKALPLT----KASGSDSQkQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGV 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 487 MDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTfvDSRKATEKLLGSLDIDHTQYQFGHTKV 566
Cdd:cd01383 567 FDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKL 644
|
...
gi 1907142940 567 FFK 569
Cdd:cd01383 645 FFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
5-569 |
1.52e-153 |
|
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: 485.64 E-value: 1.52e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 5 GPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHV 84
Cdd:cd01384 102 GGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 85 YYQILSGKKPELQDMLLLSmNPYDYHFCSQGVT-TVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKF 163
Cdd:cd01384 182 FYQLCAGAPPEDREKYKLK-DPKQFHYLNQSKCfELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 164 KqkqreEQAEADGTESADK--------AAYLMGVSSGDLLKGLLHpRVRVG-NEYVTKGQSVEQVVFAVGALAKATYDRL 234
Cdd:cd01384 261 S-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCK-RVIVTpDGIITKPLDPDAATLSRDALAKTIYSRL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 235 FRWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgL 314
Cdd:cd01384 335 FDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-V 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 315 DLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKspnfqqPRPDKKRKYQAHFEVVHYAGVVPYSIVGW 393
Cdd:cd01384 414 DNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDH------KRFSKPKLSRTDFTIDHYAGDVTYQTDLF 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 394 LEKNKDplneTVVP----IFQKSQNRLLATLYenyagscstePPKSGvkEKRKKAASFQTVSQLHKENLNKLMTNLRATQ 469
Cdd:cd01384 488 LDKNKD----YVVAehqaLLNASKCPFVAGLF----------PPLPR--EGTSSSSKFSSIGSRFKQQLQELMETLNTTE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 470 PHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAipDDTFVDSRKATEKLL 549
Cdd:cd01384 552 PHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV--LKGSDDEKAACKKIL 629
|
570 580
....*....|....*....|
gi 1907142940 550 GSLDIDhtQYQFGHTKVFFK 569
Cdd:cd01384 630 EKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
11-569 |
1.46e-143 |
|
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: 458.64 E-value: 1.46e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 11 HQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILS 90
Cdd:cd01382 105 GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 91 GKKPELQDMLLlsmnpydyhfcsqgvtTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE 170
Cdd:cd01382 185 GAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 171 ----QAEADGTESADKAAYLMGVSSGDLLKGLLHpRVRVGNEYVTKGQS------VEQVVFAVGALAKATYDRLFRWLVS 240
Cdd:cd01382 249 gggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGGAKGTVikvplkVEEANNARDALAKAIYSKLFDHIVN 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 241 RINQTldtkLPRQ---FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQ 317
Cdd:cd01382 328 RINQC----IPFEtssYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQ 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 318 PCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSgKSPNFQQPRPDKKRKYQA-----HFEVVHYAGVVPYSIV 391
Cdd:cd01382 403 DCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRLSIPRKSKLKIHRNlrddeGFLIRHFAGAVCYETA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 392 GWLEKNKDPLNETVVPIFQKSQNRLLATLYEnyagscSTEPPKSGVKEKRKKaASFQTVSQLHKENLNKLMTNLRATQPH 471
Cdd:cd01382 482 QFIEKNNDALHASLESLICESKDKFIRSLFE------SSTNNNKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTS 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 472 FVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDdtfVDSRKATEKLLGS 551
Cdd:cd01382 555 FIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKA 631
|
570
....*....|....*...
gi 1907142940 552 LDIDHTQYQFGHTKVFFK 569
Cdd:cd01382 632 LGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
3-569 |
1.60e-143 |
|
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: 459.16 E-value: 1.60e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 3 CSGPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF---------GPTGKLASADIDSYLLEKSRVI 73
Cdd:cd14888 99 CAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsGDRGRLCGAKIQTYLLEKVRVC 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 74 FQLPGERGYHVYYQILSG-----------------------KKPELQDMLL-LSMNPYDYHFCSqGVTTVDNMDDGEELI 129
Cdd:cd14888 179 DQQEGERNYHIFYQLCAAareakntglsyeendeklakgadAKPISIDMSSfEPHLKFRYLTKS-SCHELPDVDDLEEFE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 130 ATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA---EADGTESADKAAYLMGVSSGDLLKGLLHPRVRVG 206
Cdd:cd14888 258 STLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDLEKVASLLGVDAEDLLNALCYRTIKTA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 207 NEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 285
Cdd:cd14888 338 HEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQ 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 286 QFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLYDNHSGKSpnfqq 364
Cdd:cd14888 418 QFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHK----- 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 365 pRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPksgvkEKRKka 444
Cdd:cd14888 492 -RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAYLRRGTDGNT-----KKKK-- 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 445 asFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQR 524
Cdd:cd14888 564 --FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYND 641
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1907142940 525 YRILNPsaipddtfvdsrkatekllGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14888 642 YRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
11-569 |
1.12e-140 |
|
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: 451.15 E-value: 1.12e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 11 HQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILS 90
Cdd:cd14890 127 TLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 91 GKKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE 170
Cdd:cd14890 207 GADEALRERLKLQ-TPVEYFYLRGECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 171 QAEADGT-ESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTK 249
Cdd:cd14890 286 VLEDATTlQSLKLAAELLGVNEDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSP 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 250 LPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLG 328
Cdd:cd14890 366 DDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 329 ILSILE--EECMFPKASDAS--FRAKLYDNHSGKS------------PNFQQPRPDKKRkyqaHFEVVHYAGVVPYSIVG 392
Cdd:cd14890 445 KPGIFItlDDCWRFKGEEANkkFVSQLHASFGRKSgsggtrrgssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 393 WLEKNKDPLNETVVPIFQKSQNRLlatlyenyagscsteppksgvkekRKKAASFQTVSQLHkenlnKLMTNLRATQPHF 472
Cdd:cd14890 521 FNEKNNETLNAEMKELIKQSRRSI------------------------REVSVGAQFRTQLQ-----ELMAKISLTNPRY 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 473 VRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVdsrkatEKLLGSL 552
Cdd:cd14890 572 VRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKML 645
|
570
....*....|....*..
gi 1907142940 553 DIDHTQYQFGHTKVFFK 569
Cdd:cd14890 646 GLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
13-569 |
1.92e-139 |
|
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: 447.30 E-value: 1.92e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14872 105 NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSMnpyDYHFCSQ-GVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14872 185 DPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESAD---KAAYLMGVSSGDLLKGLLHPRVRVgneyvtKGQ-------SVEQVVFAVGALAKATYDRLFRWLVSR 241
Cdd:cd14872 262 VSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEI------KGCdptriplTPAQATDACDALAKAAYSRLFDWLVKK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 242 INQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCI 320
Cdd:cd14872 336 INESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 321 DLIEK-PLGILSILEEECMFPKASDASFRAKLYDNHSGKSpNFQqprPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKD 399
Cdd:cd14872 415 DLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKD 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 400 PLNETVVPIFQKSQNRLLATLYenyagscstePPKSGvKEKRKKAasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPN 479
Cdd:cd14872 491 TLQKDLYVLLSSSKNKLIAVLF----------PPSEG-DQKTSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPN 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 480 ENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILnPSAIPDDTFVDSRKATEKLLGSLDIDHTQY 559
Cdd:cd14872 556 QEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKV 634
|
570
....*....|
gi 1907142940 560 QFGHTKVFFK 569
Cdd:cd14872 635 QVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
14-569 |
1.87e-137 |
|
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: 441.33 E-value: 1.87e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKK 93
Cdd:cd01379 107 TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 94 PELQ-DMLLLSMNPYDYHFCSQGVTTVDNMDDG---EELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE 169
Cdd:cd01379 187 EDKKlAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 170 EQ----AEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQT 245
Cdd:cd01379 267 HQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSL 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 246 L--DTKLP-RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCID- 321
Cdd:cd01379 347 LkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDm 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 322 LIEKPLGILSILEEECMFPKASDASFRAKLYDNHsgKSPNFQQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPL 401
Cdd:cd01379 426 FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 402 NETVVPIFQKSQNRLLAtlyenyagscsteppksgvkekrkkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNEN 481
Cdd:cd01379 499 PPDVVQLLRSSENPLVR-----------------------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDS 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 482 KTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAipDDTFVDSRKATEKLLGSLDIDHtqYQF 561
Cdd:cd01379 550 RQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WAL 625
|
....*...
gi 1907142940 562 GHTKVFFK 569
Cdd:cd01379 626 GKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
8-567 |
1.20e-135 |
|
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: 436.91 E-value: 1.20e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 8 SRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQ 87
Cdd:cd14901 119 NATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 88 ILSGKKP-ELQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQK 166
Cdd:cd14901 199 LLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKK 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 167 QREEQAEADGTESADKAAY-LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQT 245
Cdd:cd14901 279 DGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINES 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 246 LDTKLP--RQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI 323
Cdd:cd14901 359 IAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMF 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 E-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKSP----NFQQPRpdkkrkyqAHFEVVHYAGVVPYSIVGWLEKNK 398
Cdd:cd14901 438 EaRPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASfsvsKLQQGK--------RQFVIHHYAGAVCYATDGFCDKNK 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 399 DPLNETVVPIFQKSQNRLLATlyenyagscsteppksgvkekrkkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd14901 510 DHVHSEALALLRTSSNAFLSS-----------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKP 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 479 NENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDI---- 554
Cdd:cd14901 561 NDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnie 640
|
570
....*....|...
gi 1907142940 555 DHTQYQFGHTKVF 567
Cdd:cd14901 641 HLPPFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
13-569 |
2.28e-135 |
|
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: 436.52 E-value: 2.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLED----QIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQI 88
Cdd:cd14903 103 GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 89 LSGKKPELQDMLLLSmNPYDYHFcSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR 168
Cdd:cd14903 183 LASPDVEERLFLDSA-NECAYTG-ANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 169 EEQAE--ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL 246
Cdd:cd14903 261 DDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 247 DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKP 326
Cdd:cd14903 341 GNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 327 LGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVV 406
Cdd:cd14903 420 LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR-----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLS 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 407 PIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRK--KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTP 484
Cdd:cd14903 495 DLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSP 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 485 GVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAipDDTFVDSRKATEKLLGSLDIDH-TQYQFGH 563
Cdd:cd14903 575 TELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGL 652
|
....*.
gi 1907142940 564 TKVFFK 569
Cdd:cd14903 653 TRIYFQ 658
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
17-569 |
5.79e-135 |
|
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: 435.34 E-value: 5.79e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 17 DQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPEL 96
Cdd:cd01387 110 EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 97 QDMLLLsMNPYDYHFCSQGVTT-VDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQRE---EQA 172
Cdd:cd01387 189 RQKYGL-QEAEKYFYLNQGGNCeIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 EADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPR 252
Cdd:cd01387 268 SVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 253 QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EKPLGILS 331
Cdd:cd01387 348 TLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILH 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPRPDkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQK 411
Cdd:cd01387 427 ILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVS 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 412 SQNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFL 491
Cdd:cd01387 501 SRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDV 580
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 492 VLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKAT-EKLLGSLDIDhtQYQFGHTKVFFK 569
Cdd:cd01387 581 VMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLlSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
649-1726 |
1.86e-133 |
|
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: 444.62 E-value: 1.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 649 EEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSER 728
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 729 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQ 808
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 809 ALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDS 888
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 889 ELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCR 968
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 969 KREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASA 1048
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1049 EKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKA 1128
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1129 KGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAiQRTEELEEAKKKLALRLQEAEEGVE 1208
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1209 AANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLR 1288
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1289 HSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLEL 1368
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1369 SQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRL 1448
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1449 LQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLN 1528
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1529 QKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAAL 1608
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1609 RGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEA 1688
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1907142940 1689 EQQASTNLAKYRKAQHELDDAEERADMAETQANKLRAR 1726
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
16-569 |
2.90e-132 |
|
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: 427.67 E-value: 2.90e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 16 EDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPE 95
Cdd:cd14873 118 EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 96 LQDMLLLSmNPYDYHFCSQ-GVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFkqkqreeqAEA 174
Cdd:cd14873 198 EREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 175 DGTESADK-----AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTK 249
Cdd:cd14873 269 GGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 250 lpRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLG 328
Cdd:cd14873 349 --EDFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLG 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 329 ILSILEEECMFPKASDASFRAKLYDNHSgkspnfQQPRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPI 408
Cdd:cd14873 426 LLALINEESHFPQATDSTLLEKLHSQHA------NNHFYVKPRVAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNL 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 409 FQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMD 488
Cdd:cd14873 500 LRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP------TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFD 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 489 SFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtfvDSRKATEKLLGSLDIDHTQYQFGHTKVFF 568
Cdd:cd14873 574 QAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFL 650
|
.
gi 1907142940 569 K 569
Cdd:cd14873 651 R 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
15-569 |
3.81e-129 |
|
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: 419.16 E-value: 3.81e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 15 LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKp 94
Cdd:cd14892 127 IEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 95 ELQDMLLLSMNPYDYHFCSQG-VTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQ--KQREEQ 171
Cdd:cd14892 206 ANENAALELTPAESFLFLNQGnCVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKAAYLMGVSSGDLLKGLLhPRVRVGneyvTKGQSVE------QVVFAVGALAKATYDRLFRWLVSRIN-- 243
Cdd:cd14892 286 AQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINac 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 244 ---QTL-----DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlD 315
Cdd:cd14892 361 hkqQTSgvtggAASPTFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-D 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 316 LQPCIDLIEK-PLGILSILEEECMFP-KASDASFRAKLYDNHSGKSPNFQQPRPDKKrkyqaHFEVVHYAGVVPYSIVGW 393
Cdd:cd14892 440 NQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGF 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 394 LEKNKDPLnetvvpifqksQNRLLATLyenyagscsteppksgvkEKRKKaasFQTvsqlhkeNLNKLMTNLRATQPHFV 473
Cdd:cd14892 515 LAKNNDNL-----------HDDLRDLL------------------RSSSK---FRT-------QLAELMEVLWSTTPSYI 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 474 RCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRIL-------NPSAIPDDTFVDSRKATE 546
Cdd:cd14892 556 KCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEE 635
|
570 580
....*....|....*....|...
gi 1907142940 547 KLLGSLDIDhtQYQFGHTKVFFK 569
Cdd:cd14892 636 IVARALERE--NFQLGRTKVFLR 656
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
16-569 |
1.89e-126 |
|
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: 412.92 E-value: 1.89e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 16 EDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKkPE 95
Cdd:cd01385 110 EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGA-SE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 96 LQDMLLLSMNPYDYHFCSQGVT-TVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQK--QREEQA 172
Cdd:cd01385 189 EERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 EADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL----DT 248
Cdd:cd01385 269 TVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 249 KLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIE-KPL 327
Cdd:cd01385 349 EEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPT 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEECMFPKASDASFRAKlYDNHSGKSPNFQQPrpdkKRKYQAhFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd01385 428 GLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP----QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVA 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATL--------------------YENYAGSCS-----TEPP---------KSGVKEKRKKAASfqTVSQL 453
Cdd:cd01385 502 VLRSSSSAFVRELigidpvavfrwavlraffraMAAFREAGRrraqrTAGHsltlhdrttKSLLHLHKKKKPP--SVSAQ 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 454 HKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAI 533
Cdd:cd01385 580 FQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL 659
|
570 580 590
....*....|....*....|....*....|....*.
gi 1907142940 534 pdDTFVDSRKateKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd01385 660 --ISSKEDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
14-569 |
6.53e-126 |
|
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: 409.82 E-value: 6.53e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG-KLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14891 127 SLDERLMDTNPILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSmNPYDYHFCSQ-GVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14891 207 SAELLKELLLL-SPEDFIYLNQsGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTESADKA----AYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLD 247
Cdd:cd14891 286 EAEIASESDKEAlataAELLGVDEEALEKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 248 TK---LPrqfFIGVLDIAGFEIFE-FNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLI 323
Cdd:cd14891 366 HDpdpLP---YIGVLDIFGFESFEtKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLI 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 -EKPLGILSILEEECMFPKASDASFRAKLYDNHSgKSPNFQQPRPDKKRKyqaHFEVVHYAGVVPYSIVGWLEKNKDpln 402
Cdd:cd14891 442 aSKPNGILPLLDNEARNPNPSDAKLNETLHKTHK-RHPCFPRPHPKDMRE---MFIVKHYAGTVSYTIGSFIDKNND--- 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 403 etvvpIFQKSQNRLLATlyenyagscsteppksgvkekrkkAASFQTVSQlhkenlnKLMTNLRATQPHFVRCIVPNENK 482
Cdd:cd14891 515 -----IIPEDFEDLLAS------------------------SAKFSDQMQ-------ELVDTLEATRCNFIRCIKPNAAM 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 483 TPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAI------PDDTFvdsrkaTEKLLGSLDIDH 556
Cdd:cd14891 559 KVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVtrlfaeNDRTL------TQAILWAFRVPS 632
|
570
....*....|...
gi 1907142940 557 TQYQFGHTKVFFK 569
Cdd:cd14891 633 DAYRLGRTRVFFR 645
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
12-569 |
3.30e-123 |
|
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: 401.76 E-value: 3.30e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14897 106 DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELiatDH----------AMDILGFSVDEKCACYKIVGALLHFGNM 161
Cdd:cd14897 186 MSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSEEL---EYyrqmfhdltnIMKLIGFSEEDISVIFTILAAILHLTNI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 162 KFkqkqrEEQAEADGTESADK-----AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFR 236
Cdd:cd14897 262 VF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFG 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 237 WLVSRINQTLDtklPRQFF--------IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWV 308
Cdd:cd14897 337 WIVGQINRNLW---PDKDFqimtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 309 FIDFGlDLQPCIDLI-EKPLGILSILEEECMFPKASDASFRAKLyDNHSGKSPNFQQPRPDKkrkyqAHFEVVHYAGVVP 387
Cdd:cd14897 414 DIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNR-----VAFGIRHYAEQVT 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 388 YSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRA 467
Cdd:cd14897 487 YDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY-----------------------------FKRSLSDLMTKLNS 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 468 TQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSaiPDDTFVDSRKATEK 547
Cdd:cd14897 538 ADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF--SNKVRSDDLGKCQK 615
|
570 580
....*....|....*....|..
gi 1907142940 548 LLGSLDIDhtQYQFGHTKVFFK 569
Cdd:cd14897 616 ILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
14-528 |
9.68e-119 |
|
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: 389.28 E-value: 9.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKK 93
Cdd:cd14900 133 GIAAKVLQTNILLESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGAS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 94 PE--LQDMLLLSMNpydyhfcsqgvttvdnmddgeeliatdhAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:cd14900 213 EAarKRDMYRRVMD----------------------------AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDR 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEADGTE-------SADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQ 244
Cdd:cd14900 265 LGQLKSDlapssiwSRDAAATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 245 TL-----DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPC 319
Cdd:cd14900 345 FLkmddsSKSHGGLHFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDC 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 320 IDLI-EKPLGILSILEEECMFPKASDASFRAKLYdNHSGKSPNFQQPRPDKKRkyqAHFEVVHYAGVVPYSIVGWLEKNK 398
Cdd:cd14900 424 VNLIsQRPTGILSLIDEECVMPKGSDTTLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 399 DPLNETVVPIFQksqnrllatlyenYAGScsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd14900 500 DVLHQEAVDLFV-------------YGLQ--------------------------FKEQLTTLLETLQQTNPHYVRCLKP 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907142940 479 NENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRIL 528
Cdd:cd14900 541 NDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
14-569 |
5.68e-118 |
|
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: 388.62 E-value: 5.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG-PTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14907 135 SIEQKILSCNPILEAFGNAKTVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSMNP--YDYHFCSQGVT-TVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQ-- 167
Cdd:cd14907 215 DQQLLQQLGLKNQLsgDRYDYLKKSNCyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTld 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 168 REEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL- 246
Cdd:cd14907 295 DNSPCCVKNKETLQIIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIm 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 247 -----DTKLPRQFF--IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVF--IDFgLDLQ 317
Cdd:cd14907 375 pkdekDQQLFQNKYlsIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 318 PCIDLIEK-PLGILSILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEK 396
Cdd:cd14907 454 DVIDLLDKpPIGIFNLLDDSCKLATGTDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREK 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 397 NKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKaasfqTVSQLHKENLNKLMTNLRATQPHFVRCI 476
Cdd:cd14907 529 NKDEISQSIINCIQNSKNRIISSIFSGEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCI 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 477 VPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNpsaipddtfvdsrkatekllgsldidh 556
Cdd:cd14907 604 KPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK--------------------------- 656
|
570
....*....|...
gi 1907142940 557 TQYQFGHTKVFFK 569
Cdd:cd14907 657 KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
15-569 |
4.39e-115 |
|
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: 380.02 E-value: 4.39e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 15 LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKP 94
Cdd:cd14889 111 LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 95 ELQDMLLLsMNPYDYHFCSQGVTTVDNMDD-GEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREE-QA 172
Cdd:cd14889 190 EDRENYGL-LDPGKYRYLNNGAGCKREVQYwKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 EADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLdtkLPR 252
Cdd:cd14889 269 ENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 253 QFF------IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDL-IEK 325
Cdd:cd14889 346 DDSsvelreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNK 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 326 PLGILSILEEECMFPKASDASFRAKLyDNHSGKSPNFQqprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETV 405
Cdd:cd14889 425 PIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG-----KSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASI 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 406 VPIFQKSQNRLLATLYENYAGSCSTEPPKSG---VKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENK 482
Cdd:cd14889 499 RTLFINSATPLLSVLFTATRSRTGTLMPRAKlpqAGSDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 483 TPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRIL-NPSAIPDDtfvdsRKATEKLLGSLDIdhTQYQF 561
Cdd:cd14889 579 VPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlCEPALPGT-----KQSCLRILKATKL--VGWKC 651
|
....*...
gi 1907142940 562 GHTKVFFK 569
Cdd:cd14889 652 GKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
17-569 |
7.85e-109 |
|
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: 361.95 E-value: 7.85e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 17 DQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG-KKPE 95
Cdd:cd14904 111 AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 96 LQDMLLLSMNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEAD 175
Cdd:cd14904 191 RKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 176 GtESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF- 254
Cdd:cd14904 271 G-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKg 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 255 FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKPLGILSILE 334
Cdd:cd14904 350 QIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMN 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 335 EECMFPKASDASFRAKLYDNHS--GKSPNFQQPRPDKkrkyqAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKS 412
Cdd:cd14904 429 DHLRQPRGTEEALVNKIRTNHQtkKDNESIDFPKVKR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLS 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 413 QNRLLATLYENYAGSCSTEPPKSGVKEKRKKAASFQtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLV 492
Cdd:cd14904 504 SLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGSQ-----FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMV 578
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 493 LHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDtfvDSRKATEKLLGSLDIDHT-QYQFGHTKVFFK 569
Cdd:cd14904 579 VEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
17-569 |
2.69e-107 |
|
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: 359.27 E-value: 2.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 17 DQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP-----TGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14895 126 SELLSANPILESFGNARTLRNDNSSRFGKFVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 KKPELQDMLLL-SMNPYDYHFCSQGVTTV--DNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR 168
Cdd:cd14895 206 AADDMKLELQLeLLSAQEFQYISGGQCYQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 169 EEQAEADGTESA------------------DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKAT 230
Cdd:cd14895 286 DEGEEDNGAASApcrlasaspssltvqqhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 231 YDRLFRWLVSRINQTLDTklpRQF--------------FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLE 296
Cdd:cd14895 366 YAFLFQFLVSKVNSASPQ---RQFalnpnkaankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 297 QEEYKREGIDWVFIDFGLDlQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKSpNFQQPRPDKKrkyQA 375
Cdd:cd14895 443 QQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DV 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 376 HFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKA--ASFQTVSQL 453
Cdd:cd14895 518 AFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSvlSSVGIGSQF 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 454 hKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAI 533
Cdd:cd14895 598 -KQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKN 676
|
570 580 590
....*....|....*....|....*....|....*.
gi 1907142940 534 PDDTfvdsrkATEKLLGSLDIDHTqyQFGHTKVFFK 569
Cdd:cd14895 677 ASDA------TASALIETLKVDHA--ELGKTRVFLR 704
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
12-569 |
1.11e-105 |
|
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: 354.21 E-value: 1.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSG 91
Cdd:cd14908 126 KLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 92 ------KKPELQDMLLLSMN-PYDYHFCSQG-VTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKF 163
Cdd:cd14908 206 gdeeehEKYEFHDGITGGLQlPNEFHYTGQGgAPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 164 KQKQREEQAEADGTESADKAAY---LMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVS 240
Cdd:cd14908 286 ESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 241 RINQTLDTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQP 318
Cdd:cd14908 366 TVNSSINWENDKDIrsSVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQD 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 319 CIDLIE-KPLGILSILEEECMFP-KASDASFRAKLYDNHsgkSPNFQQPRPDKKR-------KYQAHFEVVHYAGVVPYS 389
Cdd:cd14908 445 CLDTIQaKKKGILTMLDDECRLGiRGSDANYASRLYETY---LPEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYT 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 390 I-VGWLEKNKDPLNETVVPIFQKSQNrllatlyenyagscsteppksgvkekrkkaasfqtvsqlHKENLNKLMTNLRAT 468
Cdd:cd14908 522 VeTTFCEKNKDEIPLTADSLFESGQQ---------------------------------------FKAQLHSLIEMIEDT 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 469 QPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSaIPDDT----------- 537
Cdd:cd14908 563 DPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPL-IPEVVlswsmerldpq 641
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1907142940 538 -----FVDSRKATEKLLGSLDID----HTQYQFGHTKVFFK 569
Cdd:cd14908 642 klcvkKMCKDLVKGVLSPAMVSMknipEDTMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
13-622 |
6.98e-105 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 356.26 E-value: 6.98e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:PTZ00014 217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDML-LLSMNpyDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQ 171
Cdd:PTZ00014 297 NDEMKEKYkLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 172 AEA-----DGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL 246
Cdd:PTZ00014 375 TDAaaisdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATI 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 247 DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLI-EK 325
Cdd:PTZ00014 455 EPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGK 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 326 PLGILSILEEECMFPKASDASFRAKLYDNHSgKSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETV 405
Cdd:PTZ00014 534 GKSVLSILEDQCLAPGGTDEKFVSSCNTNLK-NNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPEL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 406 VPIFQKSQNRLLATLYEnyagscsteppksGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPG 485
Cdd:PTZ00014 609 VEVVKASPNPLVRDLFE-------------GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 486 VMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTfVDSRKATEKLLGSLDIDHTQYQFGHTK 565
Cdd:PTZ00014 676 DWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTM 754
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 566 VFFKAGLLGILEELRDQRLAKVLTLLQARSrGRLMRLEYQRMLGGR-DALFTIQWNIR 622
Cdd:PTZ00014 755 VFLKKDAAKELTQIQREKLAAWEPLVSVLE-ALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
18-531 |
2.57e-104 |
|
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: 351.12 E-value: 2.57e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 18 QIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQ 97
Cdd:cd14902 130 RILQTNPILESFGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 98 DMLLLS-MNPYDYH---FCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAE 173
Cdd:cd14902 210 DLLGLQkGGKYELLnsyGPSFARKRAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAT 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 174 ADGTESA---DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKL 250
Cdd:cd14902 290 AVTAASRfhlAKCAELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFD 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQFF---------IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCID 321
Cdd:cd14902 370 SAVSIsdedeelatIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 322 LIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGkspnfqqprpdkkrkyQAHFEVVHYAGVVPYSIVGWLEKNKDP 400
Cdd:cd14902 449 LFDdKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDA 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 401 LNETVVPIFQKSQNRLLATL--YENYAGSCSTEPPKSGVKEKRKKAASfqtVSQLHKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd14902 513 LPADASDILSSSSNEVVVAIgaDENRDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKP 589
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 479 NENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPS 531
Cdd:cd14902 590 NEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKCF 642
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
13-569 |
2.88e-100 |
|
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: 337.35 E-value: 2.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14876 108 LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDML-LLSMNPYDY--HFCSQgVTTVDNMDDGEELIATDHAMdilGFSVDEKCACYKIVGALLHFGNMKFKQKQRE 169
Cdd:cd14876 188 DSEMKSKYhLLGLKEYKFlnPKCLD-VPGIDDVADFEEVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 170 EQAEADGTESADK-----AAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQ 244
Cdd:cd14876 264 GVDDAAAISNESLevfkeACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 245 TLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCID-LI 323
Cdd:cd14876 344 TIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLC 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 EKPLGILSILEEECMFPKASDASFRAKLYDNHSGkSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNE 403
Cdd:cd14876 423 GKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKS-NGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRA 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 404 TVVPIFQKSQNRLLATLYEnyagscsteppksGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKT 483
Cdd:cd14876 498 ELVEVVQASTNPVVKALFE-------------GVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 484 PGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTfVDSRKATEKLLGSLDIDHTQYQFGH 563
Cdd:cd14876 565 PLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKS-LDPKVAALKLLESSGLSEDEYAIGK 643
|
....*.
gi 1907142940 564 TKVFFK 569
Cdd:cd14876 644 TMVFLK 649
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
18-569 |
9.34e-97 |
|
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: 327.12 E-value: 9.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 18 QIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQ 97
Cdd:cd14896 111 QPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEER 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 98 DMLLLSmNPYDYHFCSQG-VTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQAEADG 176
Cdd:cd14896 190 EQLSLQ-GPETYYYLNQGgACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 177 TESAD--KAAYLMGVSSgDLLKGLLHPRVRVGN-EYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQ 253
Cdd:cd14896 269 SSWAEihTAARLLQVPP-ERLEGAVTHRVTETPyGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 254 FF--IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDfGLDLQPCIDLI-EKPLGIL 330
Cdd:cd14896 348 SDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLL 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 331 SILEEECMFPKASDASFRAKLYDNHsGKSPNFQQPR---PdkkrkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVP 407
Cdd:cd14896 427 SILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQlplP--------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVE 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 408 IFQKSQNRLLATLYENyagscstEPPKSGVKEKRKKAAS-FQtvsqlhkENLNKLMTNLRATQPHFVRCIVPNENKTPGV 486
Cdd:cd14896 498 MLAQSQLQLVGSLFQE-------AEPQYGLGQGKPTLASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGL 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 487 MDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDdtFVDSRKATEKLLGSLDIDHTQYQFGHTKV 566
Cdd:cd14896 564 FDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKV 641
|
...
gi 1907142940 567 FFK 569
Cdd:cd14896 642 LLK 644
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
4-526 |
9.34e-94 |
|
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: 320.89 E-value: 9.34e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 4 SGPHSRCHQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF-GPTGKLASADIDSYLLEKSRVIFQLPGERGY 82
Cdd:cd14899 125 ISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNF 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 83 HVYYQILSGK----KPELQDMLLLSMNPYDYHFCSQGVTTV--DNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALL 156
Cdd:cd14899 205 HIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 157 HFGNMKFKQ--KQREEQAEADGTESA----------DKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVG 224
Cdd:cd14899 285 HMGNVDFEQipHKGDDTVFADEARVMssttgafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRN 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 225 ALAKATYDRLFRWLVSRINQTL---------------DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 289
Cdd:cd14899 365 ALTMECYRLLFEWLVARVNNKLqrqasapwgadesdvDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFN 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 290 QHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKS--PNFQQPr 366
Cdd:cd14899 445 QYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEhRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHFRSA- 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 367 PDKKRKYQahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATL-----YENYAGSCSTEPPKSGVKEKR 441
Cdd:cd14899 523 PLIQRTTQ--FVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 442 KKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADF 521
Cdd:cd14899 601 KSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQF 680
|
....*
gi 1907142940 522 RQRYR 526
Cdd:cd14899 681 LGRYR 685
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
15-567 |
2.76e-93 |
|
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: 317.56 E-value: 2.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 15 LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKP 94
Cdd:cd14880 120 IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 95 ELQDMLLLSMNPyDYHFCSQGVTTVDNmDDGEeliATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA-- 172
Cdd:cd14880 200 DERLQWHLPEGA-AFSWLPNPERNLEE-DCFE---VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcq 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 -EADGTESADKAAYLMGVSSGDLLKGLlhpRVRVgneyVTKGQsvEQVVFAV-----------GALAKATYDRLFRWLVS 240
Cdd:cd14880 275 pMDDTKESVRTSALLLKLPEDHLLETL---QIRT----IRAGK--QQQVFKKpcsraecdtrrDCLAKLIYARLFDWLVS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 241 RINQTLDTKLPR-QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPC 319
Cdd:cd14880 346 VINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTC 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 320 IDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPRPDKKrkyqAHFEVVHYAGVVPYSIVGWLEKNK 398
Cdd:cd14880 425 LDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE----PSFIVVHYAGPVRYHTAGLVEKNK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 399 DPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSgvkekRKKAASFQTVSQLhKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd14880 501 DPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG-----QSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKP 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 479 NENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLdidhtq 558
Cdd:cd14880 575 NSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSGPHSPYPAKGLSEPV------ 648
|
....*....
gi 1907142940 559 yQFGHTKVF 567
Cdd:cd14880 649 -HCGRTKVF 656
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
12-569 |
3.21e-92 |
|
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: 314.83 E-value: 3.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 12 QGTLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT-GKLASADIDSYLLEKSRVIFQLPGERGYHVYY 86
Cdd:cd14875 113 QRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 87 QILSGKKPELQDMLLLSMNPYDYHFCSQGVTTV------DNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGN 160
Cdd:cd14875 193 EMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLME 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 161 MKFKQKQREEQAEADGTESAdKAAYLMGVSSGDLLKGLLhprVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVS 240
Cdd:cd14875 273 VEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 241 RINQTLDTKL--PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQP 318
Cdd:cd14875 349 FVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSE 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 319 CIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPNFQQPrpdkKRKYQAHFEVVHYAGVVPYSIVGWLEKN 397
Cdd:cd14875 428 CVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKN 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 398 KDPLNETVVPIFQKSQNRLLATLYenyagscSTEPpksgVKEKRKkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIV 477
Cdd:cd14875 504 TDALKEDMYECVSNSTDEFIRTLL-------STEK----GLARRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIK 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 478 PNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADF-RQRYRILNPSAIPDDTFVDSRKATEKLLGS----L 552
Cdd:cd14875 568 PNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlY 647
|
570
....*....|....*..
gi 1907142940 553 DIDHTQYQFGHTKVFFK 569
Cdd:cd14875 648 GWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
19-569 |
4.04e-86 |
|
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: 296.41 E-value: 4.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 19 IIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQD 98
Cdd:cd14886 118 ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 99 ML-LLSMNPYDYHFCSQgVTTVDNMDDGEELIATDHAMDILgFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEA 174
Cdd:cd14886 198 SLgFKSLESYNFLNASK-CYDAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 175 DGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLPRQF 254
Cdd:cd14886 276 SNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARP 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 255 FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKP-LGILSIL 333
Cdd:cd14886 356 WIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 334 EEECMFPKASDASFRAKLydNHSGKSPNFQqprPDKKRkyQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQ 413
Cdd:cd14886 435 EEQCLIQTGSSEKFTSSC--KSKIKNNSFI---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGST 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 414 NRLLATLYENYagscstePPKSGVKEKRKKAASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVL 493
Cdd:cd14886 508 NPIVNKAFSDI-------PNEDGNMKGKFLGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVY 573
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142940 494 HQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNP-SAIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd14886 574 NQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
14-531 |
7.65e-85 |
|
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: 294.58 E-value: 7.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT-GKLASADIDSYLLEKSRvIFQLPGER--GYHVYYQILS 90
Cdd:cd14906 119 SIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVY 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 91 GKKPELQDMLLLSMNPYDYHFCSQGVTTVD---------------NMDDGEELIATDHAMDILGFSVDEKCACYKIVGAL 155
Cdd:cd14906 198 GASKDERSKWGLNNDPSKYRYLDARDDVISsfksqssnknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAI 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 156 LHFGNMKFKQKQ---REEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNE--YVTKGQSVEQVVFAVGALAKAT 230
Cdd:cd14906 278 LHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSL 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 231 YDRLFRWLVSRINQTLDTKLPRQ-----------FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEE 299
Cdd:cd14906 358 YVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 300 YKREGIDWVFIDFgLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKlYDNHSGKSPNFQQPRPDKkrkyqAHFE 378
Cdd:cd14906 438 YLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGSEQSLLEK-YNKQYHNTNQYYQRTLAK-----GTLG 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 379 VVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYagscSTEPPKSgvkekRKKAASFQTVSQLHKENL 458
Cdd:cd14906 511 IKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQ----ITSTTNT-----TKKQTQSNTVSGQFLEQL 581
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 459 NKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPS 531
Cdd:cd14906 582 NQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
13-569 |
8.82e-76 |
|
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: 265.73 E-value: 8.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 13 GTLEDQII-----EANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQ 87
Cdd:cd14937 96 GVKEDNEIsntlwDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 88 ILSGKKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSvDEKCACYKIVGALLHFGNMKFKQ-- 165
Cdd:cd14937 176 IFNGMSQELKNKYKIR-SENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMH-DMKDDLFLTLSGLLLLGNVEYQEie 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 166 ---KQREEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRI 242
Cdd:cd14937 254 kggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 243 NQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDlQPCIDL 322
Cdd:cd14937 334 NNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDL 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 323 IEKPLGILSILEEECMFPKASDASFrAKLYDNHSGKSPNFQQprpdKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLN 402
Cdd:cd14937 413 LRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS----TKKDINKNFVIKHTVSDVTYTITNFISKNKDILP 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 403 ETVVPIFQKSQNRLLATLYENYAGSCSTeppksgvkeKRKKAASFQtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENK 482
Cdd:cd14937 488 SNIVRLLKVSNNKLVRSLYEDVEVSESL---------GRKNLITFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENK 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 483 TPGVMDSFLVLHQLRCNGVLEGIRIcRQGFPNRLLYADFRQRYRILNPSAIPDDTFVDSRKATEKLLGSLDIDhtQYQFG 562
Cdd:cd14937 554 EKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVG 630
|
....*..
gi 1907142940 563 HTKVFFK 569
Cdd:cd14937 631 KTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
14-569 |
6.22e-74 |
|
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: 260.90 E-value: 6.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGK-LASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGK 92
Cdd:cd14878 110 TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 93 KPELQDMLLLSmNPYDYHFCSQG----VTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR 168
Cdd:cd14878 190 SAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 169 EEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTL-- 246
Cdd:cd14878 269 ADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqs 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 247 --DTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLI- 323
Cdd:cd14878 349 qdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFf 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 324 EKPLGILSILEEECMFPKASDASFRAKLYDNHSGKSPN-FQQPRPDKK-----RKYQAHFEVVHYAGVVPYSIVGWLEKN 397
Cdd:cd14878 429 QKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNaVYSPMKDGNgnvalKDQGTAFTVMHYAGRVMYEIVGAIEKN 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 398 KDPLNETVVPIFQKSQNRLLATLYENyagscsteppksgvkekrkKAASfqTVSQLHKeNLNKLMTNLRATQPHFVRCIV 477
Cdd:cd14878 509 KDSLSQNLLFVMKTSENVVINHLFQS-------------------KLVT--IASQLRK-SLADIIGKLQKCTPHFIHCIK 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 478 PNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIpddtfVDSRKATEKLLGSLDIDHT 557
Cdd:cd14878 567 PNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLL-----GEKKKQSAEERCRLVLQQC 641
|
570
....*....|....*
gi 1907142940 558 Q---YQFGHTKVFFK 569
Cdd:cd14878 642 KlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
14-532 |
3.28e-73 |
|
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: 256.75 E-value: 3.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKK 93
Cdd:cd14898 102 SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 94 PELQDMLLlsmnpyDYHFCSQGVTTVDNMDdgEELIATDHAMDILG---FSVDEKCACykivgALLHFGNMKFKQkqrEE 170
Cdd:cd14898 180 LNIKNDFI------DTSSTAGNKESIVQLS--EKYKMTCSAMKSLGianFKSIEDCLL-----GILYLGSIQFVN---DG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 171 QAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKL 250
Cdd:cd14898 244 ILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSG 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQffIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPCIDLIEKPLGIL 330
Cdd:cd14898 324 ERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLM 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 331 SILEEECMFPKASDASFRAKL--YDNHSGKSpnfqqprpdkkrKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNetVVPI 408
Cdd:cd14898 401 DLISEESFNAWGNVKNLLVKIkkYLNGFINT------------KARDKIKVSHYAGDVEYDLRDFLDKNREKGQ--LLIF 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 409 fqksQNRLLATlyenyagscsteppksgvKEKRKKAASFqtvsqlHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMD 488
Cdd:cd14898 467 ----KNLLIND------------------EGSKEDLVKY------FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFD 518
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1907142940 489 SFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSA 532
Cdd:cd14898 519 RDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
22-569 |
2.99e-71 |
|
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: 253.77 E-value: 2.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 22 ANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQDMLL 101
Cdd:cd01386 116 ALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 102 LSMNPYDYHFcsqGVTTVDNMDDGEELIA----TDHAMDILGFSVDEKCACYKIVGALLHFGN---MKFKQKQREEQAEa 174
Cdd:cd01386 196 LNQLAESNSF---GIVPLQKPEDKQKAAAafskLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 175 dgTESADKAAYLMGVSSGDLLK---------GLLHPRVRVGNEYVTKGQSVEQVVFAVGAL---AKATYDRLFRWLVSRI 242
Cdd:cd01386 272 --PEWAQRAAYLLGCTLEELSSaifkhhlsgGPQQSTTSSGQESPARSSSGGPKLTGVEALegfAAGLYSELFAAVVSLI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 243 NQTLDTKLPRQFFIGVLDIAGFEIFEFN------SFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfIDFGLD- 315
Cdd:cd01386 350 NRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPe 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 316 --LQPCIDLIEKPL---------------GILSILEEECMFPKASDASFRAKLYdNHSGKSPNFQQPRPDKKRKYQAHFE 378
Cdd:cd01386 427 lsPGALVALIDQAPqqalvrsdlrdedrrGLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFV 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 379 VVHYAGV--VPYSIVGWLEKNK-DPLNETVVPIFQKSQNRLlatlyenyagscsteppkSGVKekrKKAASFQTvsqlhK 455
Cdd:cd01386 506 LGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQKET------------------AAVK---RKSPCLQI-----K 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 456 ENLNKLMTNLRATQPHFVRCIVPNENKTPGV------------MDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQ 523
Cdd:cd01386 560 FQVDALIDTLRRTGLHFVHCLLPQHNAGKDErstsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRR 639
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907142940 524 RYRILNPS----AIPDDTFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 569
Cdd:cd01386 640 RFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
25-568 |
5.54e-69 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 245.79 E-value: 5.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 25 AMEAFGNAKTLRNDNSSRFGKFIRIHFgPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQDMLLLS- 103
Cdd:cd14881 114 VLRSLGSAKTATNSESSRIGHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 104 MNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFS-VDekcaCYKIVGALLHFGNMKFKQKQREEQAEADGTEsADK 182
Cdd:cd14881 193 YSPANLRYLSHGDTRQNEAEDAARFQAWKACLGILGIPfLD----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKS 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 183 AAYLMGVSSGDLLKGLlhpRVRVGNeyvTKGQSVEQVV------FAVGALAKATYDRLFRWLVSRINQ------TLDTKl 250
Cdd:cd14881 268 VAALLGVSGAALFRGL---TTRTHN---ARGQLVKSVCdanmsnMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTH- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 251 PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDW-VFIDFgLDLQPCIDLIEK-PLG 328
Cdd:cd14881 341 ATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTG 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 329 ILSILEEECMfPKASDASFRAKLYDNHSGkSPNFQQPRPDKKRKyqahFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPI 408
Cdd:cd14881 420 LLSMLDVECS-PRGTAESYVAKIKVQHRQ-NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAV 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 409 FQKSqnrllatlyenyagSCSTeppksgvkekrkkaaSFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMD 488
Cdd:cd14881 494 FYKQ--------------NCNF---------------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFD 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 489 SFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIP---DDTFVDSRKATEKLLGSLDIDH-----TQYQ 560
Cdd:cd14881 545 RGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLrrvEEKALEDCALILQFLEAQPPSKlssvsTSWA 624
|
....*...
gi 1907142940 561 FGHTKVFF 568
Cdd:cd14881 625 LGKRHIFL 632
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
15-568 |
9.54e-64 |
|
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: 230.51 E-value: 9.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 15 LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIfQLP-GERGYHVYYQILSGKK 93
Cdd:cd14879 121 LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVA-SVPtGERNFHVFYYLLAGAS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 94 PELQDMLLLSmNPYDY-----HFCSQGVTTVDNmDDGEELiatDH---AMDILGFSVDEKCACYKIVGALLHFGNMKFKQ 165
Cdd:cd14879 200 PEERQHLGLD-DPSDYallasYGCHPLPLGPGS-DDAEGF---QElktALKTLGFKRKHVAQICQLLAAILHLGNLEFTY 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 166 KQ--REEQAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTkgqsveqvVF--AVGA------LAKATYDRLF 235
Cdd:cd14879 275 DHegGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 236 RWLVSRINQTL-DTKLPRQFFIGVLDIAGFEIF---EFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFID 311
Cdd:cd14879 347 AWVVETINQKLcAPEDDFATFISLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 312 FgLDLQPCIDLI-EKPLGILSILEEEC-MFPKASDASFRAKLYDNHSGKSPnFQQPRPDKKRKYQAHFEVVHYAGVVPYS 389
Cdd:cd14879 427 Y-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYS 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 390 IVGWLEKNKDPLNETVVpifqksqnrllaTLyenyagscsteppksgvkekrkkaasFQTVSQLhKENLNKLMTNLRATQ 469
Cdd:cd14879 505 VEGFLERNGDVLSPDFV------------NL--------------------------LRGATQL-NAALSELLDTLDRTR 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 470 PHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYrilnpsaIPDDTFVDSRKATEKLL 549
Cdd:cd14879 546 LWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCAR 618
|
570
....*....|....*....
gi 1907142940 550 GSLDIDHTQYQFGHTKVFF 568
Cdd:cd14879 619 ANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
27-533 |
5.10e-61 |
|
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: 222.05 E-value: 5.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 27 EAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPELQDMLLLSmNP 106
Cdd:cd14874 109 KSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 107 YDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQR---EEQAEADGTESADK- 182
Cdd:cd14874 188 QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKw 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 183 AAYLMGVSSGDLLKGLLhPRVRVGNEYvtkgqSVEQVVFAVGALAKATYDRLFRWLVSRINQTLDTKLpRQFFIGVLDIA 262
Cdd:cd14874 268 VAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 263 GFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDwvfIDF----GLDLQPCIDLI-EKPLGILSILEEEC 337
Cdd:cd14874 341 GFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDEC 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 338 MFPKASDASFRAKLYDNHSGKSpNFQQPRpdkkRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLL 417
Cdd:cd14874 418 KFPKGSHESYLEHCNLNHTDRS-SYGKAR----NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPII 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 418 ATLYENYAGSCSTEppksgvkekrkkaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLR 497
Cdd:cd14874 493 GLLFESYSSNTSDM---------------IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIK 557
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907142940 498 CNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAI 533
Cdd:cd14874 558 NLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
14-569 |
1.11e-58 |
|
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: 217.21 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 14 TLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKK 93
Cdd:cd14887 119 GLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 94 -PELQDMLLLSMNPYDYhfcsqgvttvdnmdDGEELIAtdhAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQREEQA 172
Cdd:cd14887 199 aAATQKSSAGEGDPEST--------------DLRRITA---AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 173 EADG------------------------------TESADK----AAYLMGVSSGD-----LLKGLLHPRVRVGNEYVTkg 213
Cdd:cd14887 262 KKRKltsvsvgceetaadrshssevkclssglkvTEASRKhlktVARLLGLPPGVegeemLRLALVSRSVRETRSFFD-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 214 qsVEQVVFAVGALAKATYDRLFRWLVSRINQTL-------------DTKLPRQF-FIGVLDIAGFEIFE---FNSFEQLC 276
Cdd:cd14887 340 --LDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDLRnhsKNRLEQLC 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 277 INFTNEKLQQFFNQHMFVLEQEEYKREGidwVFID-----FGLDLQPCIDLIEKP------------------------L 327
Cdd:cd14887 418 INYANERLHCFLLEQLILNEHMLYTQEG---VFQNqdcsaFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslP 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 328 GILSILEEE-CMFPKASDASFRAKLYDNHSGK----SPNFQQPRPDKKRKyQAHFEVVHYAGVVPYSIVGWLEKNKDPLN 402
Cdd:cd14887 495 SSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATS 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 403 ETVvpifqksqnrllatlyENYAGSCSTEPPKSGVKEKRKKAA---SFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPN 479
Cdd:cd14887 574 DEL----------------ERLFLACSTYTRLVGSKKNSGVRAissRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPN 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 480 ENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILNPSAIPDdtFVDSRKATEKLLGSLDIDHTQY 559
Cdd:cd14887 638 RVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRE--ALTPKMFCKIVLMFLEINSNSY 715
|
650
....*....|
gi 1907142940 560 QFGHTKVFFK 569
Cdd:cd14887 716 TFGKTKIFFR 725
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
15-517 |
3.93e-58 |
|
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: 214.77 E-value: 3.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 15 LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF---------GPTGKLASADIDSYLLEKSRVIFQLPGERGYHVY 85
Cdd:cd14884 117 RIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 86 YQILSGKKPELQDMLLLSMNPYDYHFCSQGV------------TTVDNMDDGEELIATD--------HAMDILGFSVDEK 145
Cdd:cd14884 197 YQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQI 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 146 CACYKIVGALLHFGNMKFKQkqreeqaeadgtesadkAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGA 225
Cdd:cd14884 277 NEFFDIIAGILHLGNRAYKA-----------------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 226 LAKATYDRLFRWLVSRINQT----------LDTKLPR--QFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMF 293
Cdd:cd14884 340 LIKFIYKKLFNKIIEDINRNvlkckekdesDNEDIYSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 294 VLEQEEYKREGIDWVFIDFGlDLQPCIDLIEKPLGIL-SILEEECMFPKASDASFRAKLYDNHS----------GKSPNF 362
Cdd:cd14884 420 EKEKRIYARENIICCSDVAP-SYSDTLIFIAKIFRRLdDITKLKNQGQKKTDDHFFRYLLNNERqqqlegkvsyGFVLNH 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 363 QQPRPDKKRKYQAH-FEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRllaTLYENYAGscsteppksgvkekr 441
Cdd:cd14884 499 DADGTAKKQNIKKNiFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNR---FLREANNG--------------- 560
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 442 KKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLL 517
Cdd:cd14884 561 GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
18-568 |
1.25e-47 |
|
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: 184.02 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 18 QIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKK--PE 95
Cdd:cd14893 133 QILHAFTILEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 96 LQDMLLLSMNPYDYHFCSQGVTTVDNMddgeELIATDHAMDILGFSV-----DEKCACYKIVGALLHFGNMKF--KQKQR 168
Cdd:cd14893 213 LRDSLEMNKCVNEFVMLKQADPLATNF----ALDARDYRDLMSSFSAlrirkNQRVEIVRIVAALLHLGNVDFvpDPEGG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 169 EEQAEADGTESADKAAYLMGVSSGDLLKGLL---HPRV------------RVGNEYVT--KGQSVEQVVFAVGALAKATY 231
Cdd:cd14893 289 KSVGGANSTTVSDAQSCALKDPAQILLAAKLlevEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 232 DRLFRWLVSRINQTLDTKLPR---------QFFIGVLDIAGFEIFE--FNSFEQLCINFTNEKLQQFFNQHMFV-----L 295
Cdd:cd14893 369 ESLFNFLVETLNGILGGIFDRyeksnivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 296 EQEEYKREG--IDWVFIDFGLDLQPCIDLIE-KPLGILSILEEECMFPKASDASFRAKLYDNHSG----KSPN----FQQ 364
Cdd:cd14893 449 EDESQQVENrlTVNSNVDITSEQEKCLQLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglSRPNmgadTTN 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 365 PRPDKKRKYQAHFEVVHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENYAGSCSTEPPKSGVKEKRKKA 444
Cdd:cd14893 529 EYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTS 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 445 ASFQTVSQLHKENLN--------------KLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQ 510
Cdd:cd14893 609 SKFRKSASSARESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRS 688
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907142940 511 GFPNRLLYADFRQRYRilnpsaipddTFVDSRKATEKLLGSLD----IDHTQYQFGHTKVFF 568
Cdd:cd14893 689 IFTVHLTYGHFFRRYK----------NVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
18-569 |
1.26e-42 |
|
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: 167.22 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 18 QIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKPE-- 95
Cdd:cd14882 110 RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnr 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 96 LQDMLLLSMNPYDYHFCSQGVTTV----------DNMDDGEELIATDHAMDIlgfsVDEKC-ACYKIVGALLHFGNMKFK 164
Cdd:cd14882 190 LKEYNLKAGRNYRYLRIPPEVPPSklkyrrddpeGNVERYKEFEEILKDLDF----NEEQLeTVRKVLAAILNLGEIRFR 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 165 QKQREeqAEADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSVEQVVFAVGALAKATYDRLFRWLVSRINQ 244
Cdd:cd14882 266 QNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINM 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 245 TLdtKLPRQFF-----IGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFgLDLQPC 319
Cdd:cd14882 344 KM--SFPRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTA 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 320 ID-LIEKPLGILSILEeecmfpkasDASfraklydnHSGKSPNFQQPRPDKKR-----KYQAH-FEVVHYAGVVPYSIVG 392
Cdd:cd14882 421 VDqLMTKPDGLFYIID---------DAS--------RSCQDQNYIMDRIKEKHsqfvkKHSAHeFSVAHYTGRIIYDARE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 393 WLEKNKDPLNETVVPIFQKSQNRLLATLYENyagscsteppkSGVKEKRKKAASFQTVSQlhkENLNKLMTNLRATQPHF 472
Cdd:cd14882 484 FADKNRDFVPPEMIETMRSSLDESVKLMFTN-----------SQVRNMRTLAATFRATSL---ELLKMLSIGANSGGTHF 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 473 VRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILnpsAIPDDTFVDSRKATEKLLgSL 552
Cdd:cd14882 550 VRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LI 625
|
570
....*....|....*..
gi 1907142940 553 DIDHTQYQFGHTKVFFK 569
Cdd:cd14882 626 RLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
15-569 |
7.44e-41 |
|
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: 162.18 E-value: 7.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 15 LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILSGKKP 94
Cdd:cd14905 107 LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 95 ELQDMLLLSmNPYDYHFCSQGVT-TVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMKFKQKQreEQAE 173
Cdd:cd14905 187 EEKAAYQLG-DINSYHYLNQGGSiSVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKN--GKTE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 174 ADGTESADKAAYLMGVSSGDLLKGLLHPRVRVGNEYVTKGQSveqvvfavgaLAKATYDRLFRWLVSRINQTLDtklPRQ 253
Cdd:cd14905 264 VKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRDS----------LARSLYSALFHWIIDFLNSKLK---PTQ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 254 F--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYKREGIDWVFIDFGLDLQPCIDLIEKplgILS 331
Cdd:cd14905 331 YshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IIN 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 332 ILEEECMFPKASDASFRAKLYDNHS-----GKSPNfqqprpdkkrkyqaHFEVVHYAGVVPYSIVGWLEKNKDPLNETVV 406
Cdd:cd14905 408 LLDQESKNINSSDQIFLEKLQNFLSrhhlfGKKPN--------------KFGIEHYFGQFYYDVRGFIIKNRDEILQRTN 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 407 PIFQKSQNRLL----------ATLYE--------NYAG-----------SCSTEPPKSGVKEKRKK-------------- 443
Cdd:cd14905 474 VLHKNSITKYLfsrdgvfninATVAElnqmfdakNTAKksplsivkvllSCGSNNPNNVNNPNNNSgggggggnsgggsg 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 444 --AASFQTVSqlhkeNLNKLMTNlRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGVLEGIRICRQGFP----NRLL 517
Cdd:cd14905 554 sgGSTYTTYS-----STNKAINN-SNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIF 627
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 518 YADF------RQRYRILNPSAIPDDTFVDSrkatekllgsldIDHTQYQFGHTKVFFK 569
Cdd:cd14905 628 FDRFsfffqnQRNFQNLFEKLKENDINIDS------------ILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
11-567 |
1.59e-34 |
|
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: 143.05 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 11 HQGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgPTGKLASADIDSYLLEKSRVIFQLPGERGYHVYYQILS 90
Cdd:cd14938 128 YQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIIN 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 91 GKKPELQDMLLLSmNPYDYHFCSQGVTTVDNMDDGEELIATDHAMDILGFSVDEKCACYKIVGALLHFGNMK-------- 162
Cdd:cd14938 207 GSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafrkk 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 163 ---FKQKQREEQAEADGTESADKAAYLMGVSSGD----LLKGLLHPRVRVGNEYVT-----------KGQSVEQVVFAVG 224
Cdd:cd14938 286 sllMGKNQCGQNINYETILSELENSEDIGLDENVknllLACKLLSFDIETFVKYFTtnyifndsiliKVHNETKIQKKLE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 225 ALAKATYDRLFRWLVSRINQTL-DTKLPRQF--FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNQHMFVLEQEEYK 301
Cdd:cd14938 366 NFIKTCYEELFNWIIYKINEKCtQLQNININtnYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 302 REGIDWVFIDFGLDLQPCID-LIEKPLGIL-SILEEECMfPKASDASFRAKLYDNHSGKSPNFqqPRPDKKRKYQAHFEV 379
Cdd:cd14938 446 EDGIFCEYNSENIDNEPLYNlLVGPTEGSLfSLLENVST-KTIFDKSNLHSSIIRKFSRNSKY--IKKDDITGNKKTFVI 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 380 VHYAGVVPYSIVGWLEKNKDPLNETVVPIFQKSQNRLLATLYENY----AGSCSTEPPKSGVKE-----KRKKAASFQTV 450
Cdd:cd14938 523 THSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEYMRQFCMFYnydnSGNIVEEKRRYSIQSalklfKRRYDTKNQMA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 451 SQLHKENLNKLMTNLRATQPHFVRCIVPNENKTP-GVMDSFLVLHQLRCNGVLEGIRICRQGFPNRLLYADFRQRYRILN 529
Cdd:cd14938 603 VSLLRNNLTELEKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN 682
|
570 580 590
....*....|....*....|....*....|....*...
gi 1907142940 530 PsaipddtfvDSRKATEKLLGSLDIDHTQYQFGHTKVF 567
Cdd:cd14938 683 E---------DLKEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
982-1733 |
4.11e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 117.46 E-value: 4.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 982 EEAVLRHEATVAALRRKQaDSAAELSEQVDSLQRIRQKLEK---EKSELR--------MEVDDLGASVETLARGKASAEK 1050
Cdd:TIGR02168 175 KETERKLERTRENLDRLE-DILNELERQLKSLERQAEKAERykeLKAELRelelallvLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1051 LCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKG 1130
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1131 ALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAiQRTEELEEAKKKLALRLQEAEEGVEaa 1210
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-SKVAQLELQIASLNNEIERLEARLE-- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1211 nakcsSLEKAKLRLQTESEDVTLELERATSAA-----AALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELF 1285
Cdd:TIGR02168 411 -----RLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1286 RLR---HSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALE-----------GEKSELQAALEEAE 1351
Cdd:TIGR02168 486 QLQarlDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalggrlqavvVENLNAAKKAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1352 GALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLD--------AETRArnEALRLKKKM-- 1421
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLD--NALELAKKLrp 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1422 -----------------------EGDLNDLELQ--LGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQA 1476
Cdd:TIGR02168 644 gyrivtldgdlvrpggvitggsaKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1477 LERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEE 1556
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1557 KAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGgKKQVQKLEAKVRELEAELDAEQKKH 1636
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELEALLNER 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1637 AEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYR-KAQHELDDAEERADM 1715
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENK 962
|
810 820
....*....|....*....|....
gi 1907142940 1716 AETQANKLRAR------SRDALGP 1733
Cdd:TIGR02168 963 IEDDEEEARRRlkrlenKIKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
642-1197 |
2.23e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.65 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 642 LLRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAK 721
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 722 VKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKA 801
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 802 LQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEE 881
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 882 KLKKKDSELSQLNLRVEDEQlvgvQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASA 961
Cdd:COG1196 471 EAALLEAALAELLEELAEAA----ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 962 GQREGCRKREAELGRLRRELEEAVLRhEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETL 1041
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1042 ARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQ 1121
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1122 LEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQwrSKYEADAIQRteELEEAKKKLA 1197
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP--EPPDLEELER--ELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
717-1534 |
5.26e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.45 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 717 QLEAKVKELSERLEDEEEvNADLAARRRKLEDECTELKK-----DIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEA 791
Cdd:TIGR02168 190 RLEDILNELERQLKSLER-QAEKAERYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 792 VVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTD 871
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 872 TTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSE 951
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 952 RLEEAGgasagqregCRKREAELGRLRRELEEAVLRHEATVAALRRKQA-------------DSAAELSEQVDSLQRIRQ 1018
Cdd:TIGR02168 429 KLEEAE---------LKELQAELEELEEELEELQEELERLEEALEELREeleeaeqaldaaeRELAQLQARLDSLERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1019 KLE----------KEKSELRMEVDDLGASVETLARGKASAEKLCR-TYEDQLSEAKIKVEELQRQLADASTQRGRLQTEN 1087
Cdd:TIGR02168 500 NLEgfsegvkallKNQSGLSGILGVLSELISVDEGYEAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1088 GELGRLLEEKESMISQLSRGKTSAAqsleelRRQLEEESKAKGALA------HAVQALRHDCDLLREQHEEESEAQAELQ 1161
Cdd:TIGR02168 580 SIKGTEIQGNDREILKNIEGFLGVA------KDLVKFDPKLRKALSyllggvLVVDDLDNALELAKKLRPGYRIVTLDGD 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1162 RLLSKANaeVAQWRSKYEADAIQRTEELEEAKKKLAlrlqEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSA 1241
Cdd:TIGR02168 654 LVRPGGV--ITGGSAKTNSSILERRREIEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1242 AAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELfrlrhshEEALEALETLKRENKNLQEEISDLTDQVSL 1321
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL-------EEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1322 SGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDrKLAEKDEECTNLRRNHQRAVESLQ 1401
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE-SLAAEIEELEELIEELESELEALL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1402 ASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQaaTRLLQAQLKEEQAgRDEEQRLAAELREQGQALERRA 1481
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELR--EKLAQLELRLEGL-EVRIDNLQERLSEEYSLTLEEA 956
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1482 ALLAAELEELRAALEqgERSRRL-------------AEQELLEATERLNLLHSQNTGLLNQKKKLE 1534
Cdd:TIGR02168 957 EALENKIEDDEEEAR--RRLKRLenkikelgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1004-1631 |
1.85e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.40 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1004 AELSEQVDSLQRIRQKLEKEKsELRMEVDDLGASVETLARgkasaeklcRTYEDQLSEAKIKVEELQRQLADASTQRGRL 1083
Cdd:COG1196 196 GELERQLEPLERQAEKAERYR-ELKEELKELEAELLLLKL---------RELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1084 QTENGELGRLLEEKESMISQLsrgktsaaqsleelrrqLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRL 1163
Cdd:COG1196 266 EAELEELRLELEELELELEEA-----------------QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1164 LSKanaevaqwrskyEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAA 1243
Cdd:COG1196 329 EEE------------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1244 ALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSG 1323
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1324 KSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRrnhqRAVESLQAS 1403
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA----LAAALQNIV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1404 LDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAAL 1483
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1484 LAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAIT 1563
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 1564 DAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKkqVQKLEAKVRELEAELDA 1631
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD--LEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
692-1343 |
1.57e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 692 LQLQAEQ----DNLADAEERC--HLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLA 765
Cdd:COG1196 205 LERQAEKaeryRELKEELKELeaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 766 KAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEK 845
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 846 KLRMDTERAKRKLEGDLKltqetvtdttQDKQQLEEKLKKKDSELSQLNLRVEDEQlvgvQLQKKIKELQARAEELEEEL 925
Cdd:COG1196 365 EALLEAEAELAEAEEELE----------ELAEELLEALRAAAELAAQLEELEEAEE----ALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 926 EAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAE 1005
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1006 LSEQVDSLQRirqKLEKEKSELRmevdDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQT 1085
Cdd:COG1196 511 KAALLLAGLR---GLAGAVAVLI----GVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1086 ENGELGRLLEEKESMISQLsrgktsAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLS 1165
Cdd:COG1196 584 ARAALAAALARGAIGAAVD------LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1166 KANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAAL 1245
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1246 DKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTdqvslsgKS 1325
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLE-------EA 810
|
650
....*....|....*...
gi 1907142940 1326 IQELEKAKKALEGEKSEL 1343
Cdd:COG1196 811 RETLEEAIEEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
638-1422 |
1.14e-20 |
|
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: 99.75 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 638 KMKPLLRSAQAEEELAALRAELRGLRGALATA--EAKRQELEETQvsvtQEKNDLALQLQAEQDNLADAEERChlliksk 715
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLrlEELREELEELQ----EELKEAEEELEELTAELQELEEKL------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 716 VQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRL 795
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 796 TKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLEcslEQEKKLRMDTERAKRKLEGdlklTQETVTDTTQD 875
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---LQIASLNNEIERLEARLER----LEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 876 KQQLEEKLKKKDSELSQLNLRVEDEQLVgvQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEE 955
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELE--ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 956 AGGASAG---------QREGCRKREAELGRLRRELEEAVlrheatVAALRrkqADSAAELSEQVDSLQRIRQKLEKEKSE 1026
Cdd:TIGR02168 501 LEGFSEGvkallknqsGLSGILGVLSELISVDEGYEAAI------EAALG---GRLQAVVVENLNAAKKAIAFLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1027 LRM----------EVDDLGASVETLARGKASAEKLCRTYEDQLSEA-------KIKVEELQRQLADAS--TQRGRLQTEN 1087
Cdd:TIGR02168 572 RVTflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggVLVVDDLDNALELAKklRPGYRIVTLD 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1088 GEL----GRLL---EEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAEL 1160
Cdd:TIGR02168 652 GDLvrpgGVITggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1161 QRLLSKANAEVAQWRSKYEADAIQRTEeLEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATS 1240
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1241 AAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEE-------IS 1313
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1314 DLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEeaegaleleetktlRIQLELSQVKAEVDRKLAEKDEEctnLRRNH 1393
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLA--------------QLELRLEGLEVRIDNLQERLSEE---YSLTL 953
|
810 820
....*....|....*....|....*....
gi 1907142940 1394 QRAVESLQASLDAETRARNEALRLKKKME 1422
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
962-1714 |
1.46e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.83 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 962 GQREGCRKREAELGRLRReLEEAVLRHEATvaALRRKQADSAAE----LSEQVDSLQRIRQKLEKEKSELRMEVDDLGAS 1037
Cdd:PTZ00121 1054 GNHEGKAEAKAHVGQDEG-LKPSYKDFDFD--AKEDNRADEATEeafgKAEEAKKTETGKAEEARKAEEAKKKAEDARKA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1038 VETL-ARGKASAEKLCRTYEDQLSEAKIKVEELQRqladASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLE 1116
Cdd:PTZ00121 1131 EEARkAEDARKAEEARKAEDAKRVEIARKAEDARK----AEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1117 ELRRQLEEESKAKGALAHAVQALRHDCDLLREQHE----EESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEA 1192
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1193 K-KKLALRLQEAEEGVEAANAKCSSLEKAKlrlqteSEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELE 1271
Cdd:PTZ00121 1287 EeKKKADEAKKAEEKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1272 AAQREARGLGTELFRLRHSHEEALEALETLKR--ENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEgeksELQAALEE 1349
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEA 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1350 AEGALELEETKTLRIQLELSQvKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAEtRARNEALRLKKKMEGDLNDLE 1429
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADE 1514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1430 LQLGHATRQAMEAQAAtrllQAQLKEEQAGRDEEQRLAAELREqgqalerraallaaeleelRAALEQGERSRRLAEQEL 1509
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKA----EEAKKADEAKKAEEKKKADELKK-------------------AEELKKAEEKKKAEEAKK 1571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1510 LEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKkaitdaammAEELKKEQDTSAHLERMKKTL 1589
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK---------AEELKKAEEEKKKVEQLKKKE 1642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1590 EQTVRELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAElDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARM 1667
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1668 QDLVDKLQSKVKSYKRQFEEAEQQAS---TNLAKYRKAQHELDDAEERAD 1714
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEeakKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
643-1331 |
1.01e-19 |
|
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: 96.66 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 643 LRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKV 722
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 723 KELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEkekqateNKVKNLTEEMAALDEAVVRLTKEKKAL 802
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-------NEIERLEARLERLEDRRERLQQEIEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 803 QEAHQQAlgDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEE- 881
Cdd:TIGR02168 427 LKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGf 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 882 -----KLKKKDSELSQL---------------------------NLRVEDEQ--LVGVQLQKKIK--------------- 912
Cdd:TIGR02168 505 segvkALLKNQSGLSGIlgvlselisvdegyeaaieaalggrlqAVVVENLNaaKKAIAFLKQNElgrvtflpldsikgt 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 913 ELQARAEELEEELEAERAARARVEKQRAEA-------------------ARELEELSERLEE----------AGGASAGQ 963
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnALELAKKLRPGYRivtldgdlvrPGGVITGG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 964 REG------CRKRE-AELGRLRRELEEAVLRHEATVAALRRKQAdsaaELSEQVDSLQRIRQKLEKEKSELRMEVDDLGA 1036
Cdd:TIGR02168 665 SAKtnssilERRREiEELEEKIEELEEKIAELEKALAELRKELE----ELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1037 SVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLE 1116
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1117 ELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEadaiqrteELEEAKKKL 1196
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA--------SLEEALALL 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1197 ALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQR-HLERALEERRRQEEEMQRELEAAQR 1275
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARR 972
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1276 EARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEK 1331
Cdd:TIGR02168 973 RLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
19-509 |
2.74e-19 |
|
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: 94.81 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 19 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPTG---KLASADIDSYLLEKSRVIFQLPGERG------YHVYYQ 87
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGRESGdqnelnFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 88 ILSG-----------KKPELQDM---LLLSMNPYDYH---FCSQGVTTVDNMDDGEELIatdHAMDILGFSVDEKCACYK 150
Cdd:cd14894 329 MVAGvnafpfmrllaKELHLDGIdcsALTYLGRSDHKlagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 151 IVGALLHFGNMKFKQKQREEQAEADGT---ESADKAAYLMGVSSGDLLKGLLHPR-VRVGNEYVTKGQSVE--QVVFAVG 224
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 225 ALAKATYDRLFRWLVSRINQTL----------------DTKLPRQF-FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 287
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAR 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 288 FNQ----------HMFVLEQEEykregiDWVFIdfgldlqpcidlIEKPLGILSILEEECMFPKASDAS----------F 347
Cdd:cd14894 566 EEQviavayssrpHLTARDSEK------DVLFI------------YEHPLGVFASLEELTILHQSENMNaqqeekrnklF 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 348 RAKLYDNHSGKSPNFQQPRPDKKRKYQAHFEVV-----HYAGVVPYSIVGWLEKNKDPL-NETVVPIFQKSQNRLLATLY 421
Cdd:cd14894 628 VRNIYDRNSSRLPEPPRVLSNAKRHTPVLLNVLpfvipHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLN 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 422 ENYAGSCSTEPPKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIVPNENKTPGVMDSFLVLHQLRCNGV 501
Cdd:cd14894 708 ESSQLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787
|
....*...
gi 1907142940 502 LEGIRICR 509
Cdd:cd14894 788 IRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
771-1631 |
3.32e-19 |
|
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: 94.74 E-value: 3.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 771 KQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQA--LGDLQAEEDRVSaLAKAKIRLEQQVEDLECSLEQEKKLr 848
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAerYKELKAELRELE-LALLVLRLEELREELEELQEELKEA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 849 mdtERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDeqlvgvqLQKKIKELQARAEELEEELEAE 928
Cdd:TIGR02168 252 ---EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 929 RAARARVEKQRAEAARELEELSERLEEAggasAGQREGCRKREAELGRLRRELEeavlRHEATVAALRRKQADSAAELSE 1008
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEEL----KEELESLEAELEELEAELEELE----SRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1009 QVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEklcrtyedqLSEAKIKVEELQRQLADASTQRGRLQTENG 1088
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELERLEEALE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1089 ELGRLLEEKESMISQLSRGktsaaqsleelrrqleeeskakgalAHAVQALRHDCDLLREQHEEESEAQAELqrllsKAN 1168
Cdd:TIGR02168 465 ELREELEEAEQALDAAERE-------------------------LAQLQARLDSLERLQENLEGFSEGVKAL-----LKN 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1169 AEVAQWRSKYEADAIQRTEELEEAKKK-LALRLQEAE-EGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALD 1246
Cdd:TIGR02168 515 QSGLSGILGVLSELISVDEGYEAAIEAaLGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREIL 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1247 KKQRHLERALEERRRQEEEMQRELEA-------------AQREARGLGT---------ELFRLRHS--HEEALEALETLK 1302
Cdd:TIGR02168 595 KNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnALELAKKLRPgyrivtldgDLVRPGGVitGGSAKTNSSILE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1303 RENknlqeEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVdrklaek 1382
Cdd:TIGR02168 675 RRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV------- 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1383 dEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGhatrqamEAQAATRLLQAQLKEEQAGRDE 1462
Cdd:TIGR02168 743 -EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-------QLKEELKALREALDELRAELTL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1463 EQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSG 1542
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1543 EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKV 1622
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
....*....
gi 1907142940 1623 RELEAELDA 1631
Cdd:TIGR02168 975 KRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
733-1602 |
3.93e-19 |
|
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: 94.74 E-value: 3.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 733 EEVNADLAarrrKLEDECTELKKDIDDLELTLAKAEKekqatenkVKNLTEEMAALDEAVvrLTKEKKALQEAHQQALGD 812
Cdd:TIGR02168 182 ERTRENLD----RLEDILNELERQLKSLERQAEKAER--------YKELKAELRELELAL--LVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 813 LQAEEDRVSALAKAKIRLEQQVEDLEcsLEQEKKlrmdtERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQ 892
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELR--LEVSEL-----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 893 LNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREA 972
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 973 ELGRLRRELEEAVLRHEatvaalrrKQADSAAELSEQVDSLQriRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLC 1052
Cdd:TIGR02168 401 EIERLEARLERLEDRRE--------RLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1053 RTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKesmiSQLSRGKTSAAQSLEELRRQLEEESKAKGAL 1132
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSELISVDEGYEAAIEAALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1133 AHAV-----QALRHDCDLLrEQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGV 1207
Cdd:TIGR02168 547 LQAVvvenlNAAKKAIAFL-KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1208 EAANAKCSSLEKAKlRLQTESEDVTLELERATsAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRL 1287
Cdd:TIGR02168 626 LVVDDLDNALELAK-KLRPGYRIVTLDGDLVR-PGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAEL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1288 RHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLE 1367
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1368 LSQVKAEVD----------RKLAEKDEECTNLRR---NHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGH 1434
Cdd:TIGR02168 784 IEELEAQIEqlkeelkalrEALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1435 ATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATE 1514
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1515 RLNLLHSQNtgllnqkkkLEVDLAQLSGEVEEAAQERREAE--EKAKKAITDAAMMA----EELKKEQDT----SAHLER 1584
Cdd:TIGR02168 944 RLSEEYSLT---------LEEAEALENKIEDDEEEARRRLKrlENKIKELGPVNLAAieeyEELKERYDFltaqKEDLTE 1014
|
890
....*....|....*...
gi 1907142940 1585 MKKTLEQTVRELQARLEE 1602
Cdd:TIGR02168 1015 AKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1223-1733 |
9.13e-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: 9.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1223 RLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLK 1302
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1303 RENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEK 1382
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1383 DEECTNL-------------RRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLL 1449
Cdd:COG1196 396 AELAAQLeeleeaeeallerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1450 QAQLKEEQAGRDE----EQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTG 1525
Cdd:COG1196 476 EAALAELLEELAEaaarLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1526 LLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMA--------------------EELKKEQDTSAHLERM 1585
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvasdlreadaryyvlgDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1586 KKTLEQTVRELQARLEEAEQAALRGGKK--QVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKN 1663
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1664 LARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAkyrKAQHELDDAEERADMAETQANKLRARsRDALGP 1733
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLERE-IEALGP 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
936-1725 |
1.60e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.82 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 936 EKQRAEAARELEELSERLEEAGGASAGQREGCRK-REAELGRLRRELEEAVLRHEATVAALRRKQADS-AAELSEQVDSL 1013
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1014 QRI---RQKLEKEKS-ELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRqlaDASTQRGRLQTENGE 1089
Cdd:PTZ00121 1176 KKAeaaRKAEEVRKAeELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK---DAEEAKKAEEERNNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1090 LGRLLEEkesmisqlSRGKTSAAQSLEELRRQLEEESKAKGAlahavqalrhdcdllreqheEESEAQAELQRLLSKANA 1169
Cdd:PTZ00121 1253 EIRKFEE--------ARMAHFARRQAAIKAEEARKADELKKA--------------------EEKKKADEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1170 EVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQT---ESEDVTLELERATSAAAALD 1246
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKEEAKKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1247 KKQRHLERALEERRRQEEEMQRELEAAQREARGLGTElfRLRHSHEEALEALETLKR-ENKNLQEEISDLTDQVSLSGKS 1325
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD--EAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1326 IQELEKAKKALEGEKselqaaleeaeGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRRNHQrAVESLQASLD 1405
Cdd:PTZ00121 1463 KKKAEEAKKADEAKK-----------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE-AKKADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1406 AETRARNEALRLKKKMEGDlndlELQLGHATRQAMEAQAATrllqaQLKEEQAGRDEEQRLAAELREQGQALERRAALLA 1485
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKAD----ELKKAEELKKAEEKKKAE-----EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1486 AELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLE----------VDLAQLSGEVEE---AAQERR 1552
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelkkaeeenkIKAAEEAKKAEEdkkKAEEAK 1681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1553 EAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAE 1632
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1633 QKKHAEALKgvrKHERRVKELVYQTEEDRKNLARMQDlvdkLQSKVKSYKRQFEE-AEQQASTNLAKYRKAQHELDDAEE 1711
Cdd:PTZ00121 1762 LKKEEEKKA---EEIRKEKEAVIEEELDEEDEKRRME----VDKKIKDIFDNFANiIEGGKEGNLVINDSKEMEDSAIKE 1834
|
810
....*....|....
gi 1907142940 1712 RADMAETQANKLRA 1725
Cdd:PTZ00121 1835 VADSKNMQLEEADA 1848
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
896-1710 |
1.68e-16 |
|
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: 86.00 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 896 RVEDEQLVGVQLQKKIKELQARAEELEEELEAERAararvekQRAEAARELEELSERLEEAGGASAGQREGCRKREAELG 975
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQ-------QLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 976 RLRRELEEAVLRHEATVAAL---RRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLargkasaeklc 1052
Cdd:pfam01576 75 EILHELESRLEEEEERSQQLqneKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLL----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1053 rtyEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLsrgktsaaqsleelRRQLEEESKAKGAL 1132
Cdd:pfam01576 144 ---EDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDL--------------EERLKKEEKGRQEL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1133 AHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELeEAKKKLALRLQEAEEGVEAANA 1212
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAL-KKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1213 KCSSLEKAKLRLQTESEDVTLELERATSAAAAldkkqrhlerALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHE 1292
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAA----------QQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1293 EAL----EALETLKRENKN-------LQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKT 1361
Cdd:pfam01576 356 QALeeltEQLEQAKRNKANlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1362 LRIQLELSQVKA---EVDRKLAEKDEECTNLRRNHQRAVESLQasldAETRARNEALRLKKKMEGDLNDLELQLGH--AT 1436
Cdd:pfam01576 436 SKLQSELESVSSllnEAEGKNIKLSKDVSSLESQLQDTQELLQ----EETRQKLNLSTRLRQLEDERNSLQEQLEEeeEA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1437 RQAMEAQAATrlLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERL 1516
Cdd:pfam01576 512 KRNVERQLST--LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1517 NLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT------------------ 1578
Cdd:pfam01576 590 DHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAkeelertnkqlraemedl 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1579 ---------SAH-LERMKKTLEQTVRELQARLEE-------AEQAALR---------------------GGKKQVQKLEA 1620
Cdd:pfam01576 670 vsskddvgkNVHeLERSKRALEQQVEEMKTQLEEledelqaTEDAKLRlevnmqalkaqferdlqardeQGEEKRRQLVK 749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1621 KVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYR 1700
Cdd:pfam01576 750 QVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSK 829
|
890
....*....|
gi 1907142940 1701 KAQHELDDAE 1710
Cdd:pfam01576 830 ESEKKLKNLE 839
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
12-49 |
3.43e-15 |
|
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: 75.07 E-value: 3.43e-15
10 20 30
....*....|....*....|....*....|....*...
gi 1907142940 12 QGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 49
Cdd:cd01363 99 TVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
717-1080 |
3.84e-15 |
|
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: 81.64 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 717 QLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLT 796
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 797 KEKKALqeahqqalgdlqaeEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDK 876
Cdd:TIGR02168 761 AEIEEL--------------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 877 QQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEA 956
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 957 GGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLG- 1035
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGp 986
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907142940 1036 ---ASVETLARGKASAEKLCRTYEDqLSEAKIKVEELQRQLADASTQR 1080
Cdd:TIGR02168 987 vnlAAIEEYEELKERYDFLTAQKED-LTEAKETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1105-1737 |
1.40e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1105 SRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRhdcdlLREQHEEESEAQAELQRLLSKANaEVAQWRSKYEADAIQ 1184
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAK-RVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1185 RTEELEEAKKKLALRlqEAEEGVEAANA-KCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQE 1263
Cdd:PTZ00121 1168 EARKAEDAKKAEAAR--KAEEVRKAEELrKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1264 EEMQRELEAAQ-REARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDlTDQVSLSGKSIQELEKAKKALEGEKSE 1342
Cdd:PTZ00121 1246 EEERNNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK-AEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1343 LQAALEEAEGALELEETKTlriQLELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKME 1422
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1423 GDLNDLElQLGHATRQAMEAQAATRLLQAQLKEEQAGRD-EEQRLAAELREQGQALERRAALLAAELEELRAALEQGERS 1501
Cdd:PTZ00121 1402 EDKKKAD-ELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1502 RRLAEQELLEATERLNLLHSQNTGLLNQKKKLEvdlAQLSGEVEEAAQERREAEEKAKkaiTDAAMMAEELKKEQDTSaH 1581
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD---EAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELK-K 1553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1582 LERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKgvRKHERRVK-ELVYQTEED 1660
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKaEELKKAEEE 1631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1661 RKNLARMQDLVDKLQSKVKSYKRQFEE----AEQQASTNLAKYRKAQhELDDAEERADMAETQANKLRARSRDALGPKHK 1736
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
.
gi 1907142940 1737 E 1737
Cdd:PTZ00121 1711 E 1711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1411-1731 |
2.55e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1411 RNEALRLKKKMEGDLN-------DLELQLGHATRQAMEAQAAtRLLQAQLKEEQAG-----RDEEQRLAAELREQGQALE 1478
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERY-RELKEELKELEAEllllkLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1479 RRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKA 1558
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1559 KKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGK------KQVQKLEAKVRELEAELDAE 1632
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEellealRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1633 QKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEER 1712
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330
....*....|....*....
gi 1907142940 1713 ADMAETQANKLRARSRDAL 1731
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVK 511
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
713-1602 |
4.04e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.01 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 713 KSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAV 792
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 793 VRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLeQQVEDLECSLEQEKKlrmdtERAKRKLEGDLKLTQETVTDT 872
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL-QEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 873 TQDKQQLEEKLKKKDSELSQLnlrvedeqlvgvqlqKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSER 952
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEEL---------------EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 953 LEEAGGASAGQREGCRKREAELGRLRRELEEaVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVD 1032
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELAR-QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1033 DLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAA 1112
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1113 QSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEA 1192
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1193 KKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLeleratSAAAALDKKQRHLERALEERRRQEEEMQRELEA 1272
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV------KASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1273 AQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSgKSIQELEKAKKALEGEKSELQAALEEAEG 1352
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE-EEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1353 ALELEETKTLRIQLELSQVKAEVDRKLAEKDEECT-NLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQ 1431
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKeEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1432 LGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELeelraaleqgERSRRLAEQELLE 1511
Cdd:pfam02463 857 ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE----------EKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1512 ATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERM----KK 1587
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLeeekKK 1006
|
890
....*....|....*
gi 1907142940 1588 TLEQTVRELQARLEE 1602
Cdd:pfam02463 1007 LIRAIIEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
643-1330 |
4.78e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 643 LRSAQAEEELAALRAELRGLRGALATAE---AKRQELEETQVSV-TQEKNDLALQLQAEQDNLADAEERchlLIKSKVQL 718
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRREREKAEryqALLKEKREYEGYElLKEKEALERQKEAIERQLASLEEE---LEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 719 EAKVKELSERLEDEEEVNADLaarRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKE 798
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 799 KKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSL----EQEKKLRMDTERAKRK---LEGDLKLTQETVTD 871
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaetrDELKDYREKLEKLKREineLKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 872 TTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSE 951
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 952 RLEEAGGASAGQR----------EGCRKREAELGRLRRE------------LEEAVLRHEATVAA----LRRKQADSAAE 1005
Cdd:TIGR02169 498 QARASEERVRGGRaveevlkasiQGVHGTVAQLGSVGERyataievaagnrLNNVVVEDDAVAKEaielLKRRKAGRATF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1006 LSeqvdsLQRIRQKlEKEKSELRME-----------------------------VDDLGASVETL--------------- 1041
Cdd:TIGR02169 578 LP-----LNKMRDE-RRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMgkyrmvtlegelfek 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1042 -------ARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQS 1114
Cdd:TIGR02169 652 sgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1115 LEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKyeaDAIQRTEELEEAKK 1194
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVS 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1195 KLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQ 1274
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1275 REARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELE 1330
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
648-1343 |
5.20e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 648 AEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKV-QLEAKVKELS 726
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaSLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 727 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKE----KQATENKVKNLTEEMAALDEAVVRLTKEKKAL 802
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyaelKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 803 qEAHQQALGDLQAEEDRvsaLAKAKIRLEQQVEDLECSLEqekklrmDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEK 882
Cdd:TIGR02169 395 -EKLKREINELKRELDR---LQEELQRLSEELADLNAAIA-------GIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 883 LKKKDSELSQLnlrvedeqlvgvqlQKKIKELQARaeeleeeLEAERAARARVEKQRaEAARELEELSERLEEAGGASag 962
Cdd:TIGR02169 464 LSKYEQELYDL--------------KEEYDRVEKE-------LSKLQRELAEAEAQA-RASEERVRGGRAVEEVLKAS-- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 963 qREGCRKREAELGRLRRE------------LEEAVLRHEATVAA----LRRKQA-------------------------- 1000
Cdd:TIGR02169 520 -IQGVHGTVAQLGSVGERyataievaagnrLNNVVVEDDAVAKEaielLKRRKAgratflplnkmrderrdlsilsedgv 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1001 -DSAAELSE-----------------QVDSLQRIRQKLEK-----------EKS------------------ELRMEVDD 1033
Cdd:TIGR02169 599 iGFAVDLVEfdpkyepafkyvfgdtlVVEDIEAARRLMGKyrmvtlegelfEKSgamtggsraprggilfsrSEPAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1034 LGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQ 1113
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1114 SLEELRRQLEEESKAKGALAHAVQALrhdcdllrEQHEEESEAQaELQRLLSKANAEVAQWRSkyeadaiqRTEELEEAK 1193
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDL--------EARLSHSRIP-EIQAELSKLEEEVSRIEA--------RLREIEQKL 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1194 KKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAA 1273
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1274 QREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTdQVSLSGKSIQELEKAKKALEGEKSEL 1343
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
925-1726 |
1.31e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 925 LEAERAARARVEKQRAEA----ARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEAT---VAALRR 997
Cdd:TIGR02169 172 KEKALEELEEVEENIERLdliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIerqLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 998 KQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASV-ETLARGKASAEKLcrtyEDQLSEAKIKVEELQRQLADA 1076
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEAEIASL----ERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1077 STQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEA 1156
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1157 QAELQRLLSKANAEVAQWRSKYeADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELE 1236
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1237 RATSAAAALDKKQRhlerALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEisdlt 1316
Cdd:TIGR02169 487 KLQRELAEAEAQAR----ASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDD----- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1317 dqvslsgksiqelEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDrkLAEKDEECTNLRRNHQR- 1395
Cdd:TIGR02169 558 -------------AVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVD--LVEFDPKYEPAFKYVFGd 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1396 --AVESLQASLDAETRARNEALrlkkkmEGDLNDLELQLGHATRQAMEAQAATRLLQAQLK----EEQAGRDEEQRLAAE 1469
Cdd:TIGR02169 623 tlVVEDIEAARRLMGKYRMVTL------EGELFEKSGAMTGGSRAPRGGILFSRSEPAELQrlreRLEGLKRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1470 LREQgqalerraallaaeleelraaleqgERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQ 1549
Cdd:TIGR02169 697 LRRI-------------------------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1550 ERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkkTLEQTVRELQARLEEAEqaalrggkKQVQKLEAKVRELEAEL 1629
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLE--------EEVSRIEARLREIEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1630 DAE-------QKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKA 1702
Cdd:TIGR02169 822 NRLtlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
810 820
....*....|....*....|....
gi 1907142940 1703 QHELDDAEERADMAETQANKLRAR 1726
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
807-1605 |
1.63e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 807 QQALGDLQAEE---DRVSALAKAKI----RLEQQVEDLECSLEQEKKLR-----------MDTERAKRKLEGDLKLTQET 868
Cdd:TIGR02169 173 EKALEELEEVEeniERLDLIIDEKRqqleRLRREREKAERYQALLKEKReyegyellkekEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 869 VTDTTQDKQQLEEKLKKKDSELSQLNLRV----EDEQLvgvQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAAR 944
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 945 ELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHE---ATVAALRRKQADSAAELS---EQVDSLQRIRQ 1018
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdKEFAETRDELKDYREKLEklkREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1019 KLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKE 1098
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1099 SMISQLSrgktSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQH-----------------EEESEAQAELQ 1161
Cdd:TIGR02169 490 RELAEAE----AQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvvEDDAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1162 rLLSKANAEVAQWRSKYEADAIQRTEEL--EEAKKKLALRLQEAEEGVEAANAKC-------SSLEKAKlRLQTESEDVT 1232
Cdd:TIGR02169 566 -LLKRRKAGRATFLPLNKMRDERRDLSIlsEDGVIGFAVDLVEFDPKYEPAFKYVfgdtlvvEDIEAAR-RLMGKYRMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1233 LE---LERATS------AAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLR-------HSHEEALE 1296
Cdd:TIGR02169 644 LEgelFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSqelsdasRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1297 ALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLR-----IQLELSQV 1371
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1372 KAEVDRKLAEKDEECTNLRRNHQRavESLQASLDAETRARNEALRLKKKMEGD-LNDLELQLGHATRQAMEAQAATRLLQ 1450
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLE--KEYLEKEIQELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1451 AQLKEEQAGRDEeqrLAAELREQgqalerraallaaeleelraaleqgERSRRLAEQELLEATERLNLLHSQNTGLLNQK 1530
Cdd:TIGR02169 882 SRLGDLKKERDE---LEAQLREL-------------------------ERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1531 KKLEVDLAQLSGEVEEAA-----QERREAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAE 1604
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEELsledvQAELQRVEEEIRALEPVNMLAiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
.
gi 1907142940 1605 Q 1605
Cdd:TIGR02169 1014 K 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
739-1100 |
1.14e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 739 LAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEED 818
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 819 RVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLklTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVE 898
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 899 DEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLR 978
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 979 RELEEAvlrhEATVAALRRKQADSAAELSEQVDSLQRIrQKLEKEKSELRMEVDDLGASVETLARGKASAEKLcrtyEDQ 1058
Cdd:TIGR02169 903 RKIEEL----EAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL----EPV 973
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907142940 1059 LSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESM 1100
Cdd:TIGR02169 974 NMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
646-846 |
1.59e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 646 AQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKEL 725
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 726 SERLED------------------EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 787
Cdd:COG4942 103 KEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 788 LDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKK 846
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1058-1729 |
1.70e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.24 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1058 QLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEekesmisqLSRGKTSAAQSleelrrqleeeskakgALAHAVQ 1137
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKREYEGY----------------ELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1138 ALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEadaiQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSL 1217
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1218 EKAKLR----LQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEE 1293
Cdd:TIGR02169 310 IAEKEReledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1294 ALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKA 1373
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1374 EVDRKLAEKD---EECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLElQLGHATRQ---AMEAQAATR 1447
Cdd:TIGR02169 470 ELYDLKEEYDrveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA-QLGSVGERyatAIEVAAGNR 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1448 L--------LQAQ-----LKEEQAGR---------DEEQRLAAELREQGQALERRAALLAAELEELRAALEQG------- 1498
Cdd:TIGR02169 549 LnnvvveddAVAKeaielLKRRKAGRatflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGdtlvved 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1499 -ERSRRLA--------EQELLE-------ATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEE---KAK 1559
Cdd:TIGR02169 629 iEAARRLMgkyrmvtlEGELFEksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENrldELS 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1560 KAITDAAMMAEELKKEQDTsahLERMKKTLEQTVRELQARLEEAEQAaLRGGKKQVQKLEAKVRELEAELDAEQKKHA-- 1637
Cdd:TIGR02169 709 QELSDASRKIGEIEKEIEQ---LEQEEEKLKERLEELEEDLSSLEQE-IENVKSELKELEARIEELEEDLHKLEEALNdl 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1638 EALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSkvKSYKRQFEEAEQQastnlakyrKAQHELDDAEERADMAE 1717
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR--LTLEKEYLEKEIQ---------ELQEQRIDLKEQIKSIE 853
|
730
....*....|..
gi 1907142940 1718 TQANKLRARSRD 1729
Cdd:TIGR02169 854 KEIENLNGKKEE 865
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
638-1431 |
1.73e-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: 66.15 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 638 KMKPLLRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQA--------EQDNLADAEERCH 709
Cdd:pfam02463 148 AMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkaleyyqLKEKLELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 710 LLIKSKV---------QLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQ-------- 772
Cdd:pfam02463 228 YLDYLKLneeridllqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKsellkler 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 773 ---ATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRM 849
Cdd:pfam02463 308 rkvDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 850 DTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQL---NLRVEDEQLVGVQLQKKIKELQARAEELEEELE 926
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIleeEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 927 AERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAEL 1006
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1007 SEQVDSLQRIRQKLEKEKSELRMEVDDLGAsveTLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTE 1086
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGA---RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1087 NGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSK 1166
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1167 ANAEVAQWRSKYEADaiqrtEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALD 1246
Cdd:pfam02463 705 EQREKEELKKLKLEA-----EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1247 KKQRHLERALEERRRQEEEMQRELEAAQREaRGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSI 1326
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEE-LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1327 QELEKAKKALEGEKSE-LQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRRNH---QRAVESLQA 1402
Cdd:pfam02463 859 LEEEITKEELLQELLLkEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEaeiLLKYEEEPE 938
|
810 820
....*....|....*....|....*....
gi 1907142940 1403 SLDAETRARNEALRLKKKMEGDLNDLELQ 1431
Cdd:pfam02463 939 ELLLEEADEKEKEENNKEEEEERNKRLLL 967
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
647-1098 |
3.16e-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: 65.58 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 647 QAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADaeerchllikskvqLEAKVKELS 726
Cdd:pfam01576 542 ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN--------------LEKKQKKFD 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 727 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAAL-------DEAVVRLTKEK 799
Cdd:pfam01576 608 QMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLvsskddvGKNVHELERSK 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 800 KALQEAHQQALGDLQAEEDRVSALAKAKIRLE-----------------------------QQVEDLECSLEQEKKLRMD 850
Cdd:pfam01576 688 RALEQQVEEMKTQLEELEDELQATEDAKLRLEvnmqalkaqferdlqardeqgeekrrqlvKQVRELEAELEDERKQRAQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 851 TERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERA 930
Cdd:pfam01576 768 AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 931 ARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRR--KQADS-AAELS 1007
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKstLQVEQlTTELA 927
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1008 EQVDSLQRI---RQKLEKEKSELRMEVDDLGASV----------------------ETLARGKASAEKLCRTYEDQLSEA 1062
Cdd:pfam01576 928 AERSTSQKSesaRQQLERQNKELKAKLQEMEGTVkskfkssiaaleakiaqleeqlEQESRERQAANKLVRRTEKKLKEV 1007
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907142940 1063 KIKVEELQRQLADASTQRGRLQTENGELGRLLEEKE 1098
Cdd:pfam01576 1008 LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1006-1674 |
2.14e-09 |
|
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: 62.68 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1006 LSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRtYEDQLSEAKIKVEELQRQLADASTQRGRLQT 1085
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETQERINR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1086 ENGELGRLLEEK---------ESMISQLSRGKTSAAQSLEELRRQLEEESKAKGAlAHAVQALRHDCDLLREQHEEESEA 1156
Cdd:TIGR00618 289 ARKAAPLAAHIKavtqieqqaQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1157 QAELQRLLSKANaEVAQWRSKYEADaiqrtEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEdvtLELE 1236
Cdd:TIGR00618 368 REISCQQHTLTQ-HIHTLQQQKTTL-----TQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE---LQQR 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1237 RATSAAAALDK-------KQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQ 1309
Cdd:TIGR00618 439 YAELCAAAITCtaqceklEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1310 EEISDLTDQVSLSG--KSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDrklaekdeect 1387
Cdd:TIGR00618 519 DIDNPGPLTRRMQRgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP----------- 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1388 NLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLA 1467
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1468 AELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLN-LLHSQNTGLLNQKKKLE---VDLAQLSGE 1543
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrEFNEIENASSSLGSDLAareDALNQSLKE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1544 VEEAAQERREAEEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKV 1622
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV 827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907142940 1623 RELEAELDAEQKKHAeALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKL 1674
Cdd:TIGR00618 828 QEEEQFLSRLEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
648-837 |
2.75e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 648 AEEELAALRAELRGLRGALATAEAKRQELEEtQVSVTQEKNDLALQLQAEQDNLADAEerchllikskvQLEAKVKELSE 727
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEA-ELDALQERREALQRLAEYSWDEIDVA-----------SAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 728 RLEDEEEVNADLAARRRKLEdectELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKA-----L 802
Cdd:COG4913 676 ELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907142940 803 QEAHQQALGDLQAE------EDRVSALAKAKIRLEQQVEDL 837
Cdd:COG4913 752 EERFAAALGDAVERelrenlEERIDALRARLNRAEEELERA 792
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1141-1734 |
3.64e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.11 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1141 HDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEAdaiqRTEELEEAKKKLALRLQEAEEgveaanaKCSSLEKA 1220
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAA----RKQELEEILHELESRLEEEEE-------RSQQLQNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1221 KLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALET 1300
Cdd:pfam01576 98 KKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1301 LKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLA 1380
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1381 EKDEECTNLRRnHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLghatRQAMEAQAATRLLQAQLKEE---- 1456
Cdd:pfam01576 258 QKNNALKKIRE-LEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL----EDTLDTTAAQQELRSKREQEvtel 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1457 -QAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEV 1535
Cdd:pfam01576 333 kKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1536 DLAQLSGEVEEAAQERREAEEKAKKAIT---------------------DAAMMAEELKKEQDTSAHLERMKKTLEQTVR 1594
Cdd:pfam01576 413 QLQELQARLSESERQRAELAEKLSKLQSelesvssllneaegkniklskDVSSLESQLQDTQELLQEETRQKLNLSTRLR 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1595 E-------LQARLEEaEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRK----- 1662
Cdd:pfam01576 493 QledernsLQEQLEE-EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAaydkl 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1663 --------------------------NLARMQDLVDKLQSKVKSYKRQFEE----AEQQASTNLAKYRKAQHELDDAEER 1712
Cdd:pfam01576 572 ektknrlqqelddllvdldhqrqlvsNLEKKQKKFDQMLAEEKAISARYAEerdrAEAEAREKETRALSLARALEEALEA 651
|
650 660
....*....|....*....|..
gi 1907142940 1713 ADMAETQANKLRARSRDALGPK 1734
Cdd:pfam01576 652 KEELERTNKQLRAEMEDLVSSK 673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
643-1205 |
3.66e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 643 LRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQL-QAEQDNLADAEERCHLLIKSKVQLEAK 721
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 722 VKELSERLED----EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTK 797
Cdd:COG4913 361 RARLEALLAAlglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 798 EKKALQEAHQQALG-------------DLQAEEDR-----VSALAKAKIRL---EQQVEDLECSLEQEK-KLRMDTERAK 855
Cdd:COG4913 441 RLLALRDALAEALGldeaelpfvgeliEVRPEEERwrgaiERVLGGFALTLlvpPEHYAAALRWVNRLHlRGRLVYERVR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 856 RKLEGDLkltqetvtDTTQDKQQLEEKLKKKDSELS-----QLNLR-----VEDEQlvgvQLQKKIKELQARAEEleeel 925
Cdd:COG4913 521 TGLPDPE--------RPRLDPDSLAGKLDFKPHPFRawleaELGRRfdyvcVDSPE----ELRRHPRAITRAGQV----- 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 926 eaeraararveKQRAEAARELEELSERLEEAGGASAgqregcRKREAELGRLRRELEEAVLRHEATVAALRRKQadsaAE 1005
Cdd:COG4913 584 -----------KGNGTRHEKDDRRRIRSRYVLGFDN------RAKLAALEAELAELEEELAEAEERLEALEAEL----DA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1006 LSEQVDSLQRIRQKLEKEK--SELRMEVDDLGASVETLARGKASAEKLcrtyEDQLSEAKIKVEELQRQLADASTQRGRL 1083
Cdd:COG4913 643 LQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRL 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1084 QTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHdcDLLREQHEEESEAQAELQRL 1163
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID--ALRARLNRAEEELERAMRAF 796
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1907142940 1164 LSKANAEVAQWRSKYEA----DAI---QRTEELEEAKKKLALRLQEAEE 1205
Cdd:COG4913 797 NREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSI 845
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1249-1731 |
3.79e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1249 QRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQV-SLSGKSIQ 1327
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1328 ELEKAKKALEGEKSELQaaleeaegaleleetktlRIQLELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAE 1407
Cdd:COG4913 342 QLEREIERLERELEERE------------------RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1408 TRARNEALRLKKKMEGDLNDLELQLGHATRQAM----EAQAATRLLQAQLKEEQA------------GRDEEQRLAAE-- 1469
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAelpfvgelievrPEEERWRGAIErv 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1470 LREQGQA----LERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHsqntgllnqkkKLEVDLAQLSGEVE 1545
Cdd:COG4913 484 LGGFALTllvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1546 EAAQERR--------EAEEKAKKAITDAAMM-----AEELKKEQDTSAHL------ERMKKTLEQTVRELQARLEEAEQa 1606
Cdd:COG4913 553 AELGRRFdyvcvdspEELRRHPRAITRAGQVkgngtRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEE- 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1607 alrggkkQVQKLEAKVRELEAELDAEQK--KHAEALKGVRKHERRVKELvyqtEEDRKNLARMQDLVDKLQSKVKSYKRQ 1684
Cdd:COG4913 632 -------RLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAALEEQLEELEAE 700
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907142940 1685 FEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRARSRDAL 1731
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
646-1232 |
5.90e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.34 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 646 AQAEEELAALRAELRGLRGALATAEAKRQELeetqvsvTQEKNDLALQLQAEQDNLADaEERCHLLIKSKV-QLEAKVKE 724
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGKNIKL-------SKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDERNS 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 725 LSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQE 804
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 805 AHQQALGDLQAEEDRVSALAKAKIRLEQQVED----------------------------LECSLEQEKKLRMDTERAKR 856
Cdd:pfam01576 581 ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaisaryaeerdraeaeareketralsLARALEEALEAKEELERTNK 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 857 KLEGDLKLTQETVTDTTQDKQQLE----------EKLKKKDSELSQLNLRVEDEQL---VGVQLQKKI--KELQARAEEL 921
Cdd:pfam01576 661 QLRAEMEDLVSSKDDVGKNVHELErskraleqqvEEMKTQLEELEDELQATEDAKLrleVNMQALKAQfeRDLQARDEQG 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 922 EEELEAERAARARVE-------KQRAEAARELEELSERLEEAGG----ASAGQREGC---RKREAELGRLRRELEEAVLR 987
Cdd:pfam01576 741 EEKRRQLVKQVRELEaelederKQRAQAVAAKKKLELDLKELEAqidaANKGREEAVkqlKKLQAQMKDLQRELEEARAS 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 988 HEATVAALR---RKQADSAAE---LSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSE 1061
Cdd:pfam01576 821 RDEILAQSKeseKKLKNLEAEllqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEE 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1062 AKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRgktsaaQSLEELRRQLEEESKAKGALAHAVQALRH 1141
Cdd:pfam01576 901 EQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLER------QNKELKAKLQEMEGTVKSKFKSSIAALEA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1142 DCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEAD---AIQRTEELEEAK---KKLALRLQEAEEGVEAANAkcs 1215
Cdd:pfam01576 975 KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDErrhADQYKDQAEKGNsrmKQLKRQLEEAEEEASRANA--- 1051
|
650
....*....|....*..
gi 1907142940 1216 slekAKLRLQTESEDVT 1232
Cdd:pfam01576 1052 ----ARRKLQRELDDAT 1064
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
646-899 |
1.35e-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: 60.08 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 646 AQAEEELAALRAELRG-----LRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEA 720
Cdd:TIGR02169 775 HKLEEALNDLEARLSHsripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 721 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAvvrltkekk 800
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK--------- 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 801 alqeahqqalgdLQAEEDRVSALAKAKIRLEQQVEDlECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLE 880
Cdd:TIGR02169 926 ------------LEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
250
....*....|....*....
gi 1907142940 881 EKLKKKDSELSQLNLRVED 899
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEE 1011
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
644-1398 |
1.45e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 644 RSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQlEAKVK 723
Cdd:PTZ00121 1088 RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAE-DARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 724 ELSERLEDEEEVNAdlaARRRKLEDECTELKKDIDDLELTLA-KAEKEKQATEnkVKNLTEEMAAldEAVVRLTKEKKAL 802
Cdd:PTZ00121 1167 EEARKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEE--ARKAEDAKKA--EAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 803 QEAHQqalgdlqAEEDRVSALAKA--KIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLE 880
Cdd:PTZ00121 1240 EEAKK-------AEEERNNEEIRKfeEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 881 EKlkKKDSELSQlnlRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKqRAEAARELEELSERLeeaggAS 960
Cdd:PTZ00121 1313 EA--KKADEAKK---KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKK-----AD 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 961 AGQREGCRKREAELGRLRRElEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLE--------KEKSELRMEVD 1032
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAE-EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeakkadeaKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1033 DLGASVETlargKASAEKLCRTYED--QLSEAKIKVEELQRQlADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTS 1110
Cdd:PTZ00121 1461 EAKKKAEE----AKKADEAKKKAEEakKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1111 AAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEvaQWRSKYEADAIQRTEEL- 1189
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAk 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1190 --EEAKKKlALRLQEAEEgveaANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQrhleralEERRRQEEEMQ 1267
Cdd:PTZ00121 1614 kaEEAKIK-AEELKKAEE----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-------EEDKKKAEEAK 1681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1268 RELEAAQREARGLGTE------LFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAkkalEGEKS 1341
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKK 1757
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142940 1342 ELQAALEEAEGALELEETKTLRIQLElsQVKAEVDRKLAEKDEECTNLRRNHQRAVE 1398
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
717-915 |
1.98e-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: 58.62 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 717 QLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLT 796
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 797 KEKK----ALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDT 872
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907142940 873 TQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQ 915
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
820-1050 |
2.06e-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: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 820 VSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEd 899
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 900 eqlvgvQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRR 979
Cdd:COG4942 94 ------ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142940 980 ELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSE---LRMEVDDLGASVETLARGKASAEK 1050
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAElaeLQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
644-1073 |
2.68e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 644 RSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVK 723
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 724 ELSERLEDEEEVNAdlaarrrklEDECTELKKDIDDLELTLAKAEKEKQATEnkvknLTEEMAALDEAVVRLtkekkalq 803
Cdd:PRK02224 437 TARERVEEAEALLE---------AGKCPECGQPVEGSPHVETIEEDRERVEE-----LEAELEDLEEEVEEV-------- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 804 EAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEqEKKLRMDTERA-KRKLEGDLKLTQETVTDTTQDKQQLEEK 882
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE-EKRERAEELRErAAELEAEAEEKREAAAEAEEEAEEAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 883 LKKKDSELSQLNLRVEdeqlvgvqlqkkikELQARAEELEEELEAERAARARVEKQRAEAARELeelserleeaggasag 962
Cdd:PRK02224 574 VAELNSKLAELKERIE--------------SLERIRTLLAAIADAEDEIERLREKREALAELND---------------- 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 963 QRegcRKREAELGRLRRELEEAVLRHEATVAALRRKQADSA--------AELSEQVDSLQR----IRQKLEkEKSELRME 1030
Cdd:PRK02224 624 ER---RERLAEKRERKRELEAEFDEARIEEAREDKERAEEYleqveeklDELREERDDLQAeigaVENELE-ELEELRER 699
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907142940 1031 VDDLGASVETLARGKASAEKLCRTYEDQLSEAKIK-VEELQRQL 1073
Cdd:PRK02224 700 REALENRVEALEALYDEAEELESMYGDLRAELRQRnVETLERML 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1146-1712 |
3.84e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1146 LREQHEEESEAQAELQRLLSKANAEVAQWRSkyeADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKL--- 1222
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQRRL---ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgng 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1223 -----RLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQREleaAQREARGLGTELFRLRHSHEEALEA 1297
Cdd:COG4913 337 gdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1298 LETLKRENKNLQEEISDLTDQVSLSGksiQELEKAKKALEgekSELQAALEEaegaleleetktLRIQLELSQVKAE--- 1374
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIP---ARLLALRDALA---EALGLDEAE------------LPFVGELIEVRPEeer 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1375 -----------------VDRKLAEKDEECTNLRRNHQRAV-ESLQASLDAETRARNEALRLKKKMEGDLND----LELQL 1432
Cdd:COG4913 476 wrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPDPERPRLDPDSLAGKLDFKPHPfrawLEAEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1433 GHA-------------------TRQAM------------------------EAQAATRLLQAQLKEEQAGRDEEQRLAAE 1469
Cdd:COG4913 556 GRRfdyvcvdspeelrrhpraiTRAGQvkgngtrhekddrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1470 LREQGQALerraallaaeleelraaleqgeRSRRLAEQELLEATERlnllhsqntgllnqkkklEVDLAQLSGEVEEAAQ 1549
Cdd:COG4913 636 LEAELDAL----------------------QERREALQRLAEYSWD------------------EIDVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1550 ERREAeEKAKKAITDAAMMAEELKKEQDTsahLERMKKTLEQTVRELQARLEEAEQaalrggkkQVQKLEAKVRELEAEL 1629
Cdd:COG4913 676 ELERL-DASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE--------ELDELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1630 DAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNL-ARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDD 1708
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEERIDALrARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDR 823
|
....
gi 1907142940 1709 AEER 1712
Cdd:COG4913 824 LEED 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
720-943 |
4.01e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 720 AKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEK 799
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 800 KALQEAHQQALGDLQaeedRVSALAKAKIRLEQQ-VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQ 878
Cdd:COG4942 100 EAQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907142940 879 LEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAA 943
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
644-1106 |
4.30e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 644 RSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVK 723
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 724 ELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQ 803
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 804 EAHQQALGDLQA-----------EEDRVSALAKAkirlEQQVEDLECSLEQekkLRMDTERAKRKLEgdlklTQETVTDT 872
Cdd:PRK02224 440 ERVEEAEALLEAgkcpecgqpveGSPHVETIEED----RERVEELEAELED---LEEEVEEVEERLE-----RAEDLVEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 873 TQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAeeleeeleaeraararvEKQRAEAARELEELSER 952
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA-----------------EEKREAAAEAEEEAEEA 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 953 LEEAgGASAGQREGCRKREAELGRLrRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKlekeKSELRMEVD 1032
Cdd:PRK02224 571 REEV-AELNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER----KRELEAEFD 644
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142940 1033 DlgASVETLARGKASAEklcrTYEDQLSEakiKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSR 1106
Cdd:PRK02224 645 E--ARIEEAREDKERAE----EYLEQVEE---KLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
718-1315 |
5.41e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 718 LEAKVKELSERLEDEEEVNADLAARRRKLED----------ECTELKKDIDDLELTLAKAEKEKqatenkvknlteemAA 787
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEvleeheerreELETLEAEIEDLRETIAETERER--------------EE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 788 LDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEkklRMDTERAKRKLEGdlkltqe 867
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC---RVAAQAHNEEAES------- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 868 tvtdTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARele 947
Cdd:PRK02224 347 ----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 948 elserleeaggasagQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEkeksEL 1027
Cdd:PRK02224 420 ---------------ERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVE----EL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1028 RMEVDDLGASVETLARGKASAEKLCRTyEDQLSEAKIKVEELQRQLADastQRGRLQTENGELGRLLEEKESMISQlSRG 1107
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAE---RRETIEEKRERAEELRERAAELEAE-AEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1108 KTSAAQSLEELRRQLEEESKA----KGALAHAVQALRHdcdlLREQHEEESEAQAELQRLLSK--ANAEVAQWRSKYEAD 1181
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAElnskLAELKERIESLER----IRTLLAAIADAEDEIERLREKreALAELNDERRERLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1182 AIQRTEELEEAKKKLAL-----RLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERatsaaaaldkkqrhleral 1256
Cdd:PRK02224 632 KRERKRELEAEFDEARIeeareDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE------------------- 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 1257 eerrrqeeemqreLEaaqrearglgtELFRLRHSHEEALEALETLKRENKNLQEEISDL 1315
Cdd:PRK02224 693 -------------LE-----------ELRERREALENRVEALEALYDEAEELESMYGDL 727
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
715-1090 |
7.43e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.21 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 715 KVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVR 794
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 795 LTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQ 874
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 875 DKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAAreleelserle 954
Cdd:pfam07888 193 EFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 955 eaggASAGQREgcrKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELS----------EQVDSLQRIRQKLEKEK 1024
Cdd:pfam07888 262 ----SMAAQRD---RTQAELHQARLQAAQLTLQLADASLALREGRARWAQEREtlqqsaeadkDRIEKLSAELQRLEERL 334
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1025 SELRMEvdDLGASVEtLARGKASAEKlcrtyedQLSEAKIKVEELQRQLADASTQRGRLQTENGEL 1090
Cdd:pfam07888 335 QEERME--REKLEVE-LGREKDCNRV-------QLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
650-838 |
1.23e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 650 EELAALRAELRGLRGALATAEAKR---QELEETQVSVTQEKNDL--------ALQLQAEQDNLADAEERCHLLIKSKVQL 718
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIellEPIRELAERYAAARERLaeleylraALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 719 EAKVKELSERLEDEEEVNADLAARRRKLE-DECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTK 797
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907142940 798 EKKALQEAHQQALGDLQAEEDRvsaLAKAKIRLEQQVEDLE 838
Cdd:COG4913 388 EAAALLEALEEELEALEEALAE---AEAALRDLRRELRELE 425
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
644-942 |
1.26e-07 |
|
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: 57.00 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 644 RSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQ----DNLADAEERCHLLIKSKVQ-L 718
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEEVSRIEARLReI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 719 EAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKE 798
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 799 KKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLEcsleqekklrmdterakrklegDLKLTQETVTDTTQDKQQ 878
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE----------------------DPKGEDEEIPEEELSLED 955
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142940 879 LEEKLKKKDSELSQL---NLRVEDEQlvgVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEA 942
Cdd:TIGR02169 956 VQAELQRVEEEIRALepvNMLAIQEY---EEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
637-1083 |
1.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 637 FKMKPLLRSAQAEEELAALRAELRGLRGALATAEAKRQELEEtqvsvtqekndlalqlqaeqdnladaeerchlLIKSKV 716
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE--------------------------------LKKKLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 717 QLEAKVKELSERLEDEEEVNAdLAARRRKLEDECTELkkDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLT 796
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 797 KEKKALQEAHQQ--ALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRmdteRAKRKLEGDLKLTQETVTDTTQ 874
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESELIKLKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 875 DKQ--QLEEKLKKKDSE-----------LSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAE 941
Cdd:PRK03918 502 AEQlkELEEKLKKYNLEelekkaeeyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 942 AARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADsAAELSEQVDSLQRI----- 1016
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEELEKKyseee 660
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1017 RQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQL---SEAKIKVEELQRQLADASTQRGRL 1083
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELeerEKAKKELEKLEKALERVEELREKV 730
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1544-1726 |
1.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1544 VEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTL--EQTVRELQARLEEAEQ--AALRGGKKQVQKLE 1619
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAelERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1620 AKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQskVKSYKRQFEEAEQQASTNLAKy 1699
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL--RALLEERFAAALGDAVERELR- 768
|
170 180
....*....|....*....|....*..
gi 1907142940 1700 RKAQHELDDAEERADMAETQANKLRAR 1726
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1248 |
2.44e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 999 QADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLargkasaeklcrtyEDQLSEAKIKVEELQRQLADAST 1078
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------ERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1079 QRGRLQTENGELGRLLEEKESMISQLSRgktSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQA 1158
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1159 ELQRLLSKANAEVAQWRSKYeadaiqrtEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERA 1238
Cdd:COG4942 161 ELAALRAELEAERAELEALL--------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|
gi 1907142940 1239 TSAAAALDKK 1248
Cdd:COG4942 233 EAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
717-1106 |
2.86e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 717 QLEAKVKELSErLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATE--NKVKNLTEEMAALDEAVVR 794
Cdd:COG4717 72 ELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 795 LTKEKKALQEAHQQalgdlqaEEDRVSALAKAKIRLEQQVEDLecSLEQEKKLRmDTERAKRKLEGDLKLTQETVTDTTQ 874
Cdd:COG4717 151 LEERLEELRELEEE-------LEELEAELAELQEELEELLEQL--SLATEEELQ-DLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 875 DKQQLEEKLKKKDSELSQLNLRVEDEQ-------------------------------------LVGVQLQKKIKELQAR 917
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEarlllliaaallallglggsllsliltiagvlflvlgLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 918 AEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREgCRKREAELGRLRRELEEAVLRHEATvAALRR 997
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-LQELLREAEELEEELQLEELEQEIA-ALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 998 KQADSAAELSEQVDSLQRiRQKLEKEKSELRMEVDDLGASVETLARGKASAEklcrtYEDQLSEAKIKVEELQRQLADAS 1077
Cdd:COG4717 379 AGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....*
gi 1907142940 1078 TQRGRLQTE------NGELGRLLEEKESMISQLSR 1106
Cdd:COG4717 453 EELAELEAEleqleeDGELAELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1610 |
2.93e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1387 TNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQL----KEEQAGRDE 1462
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1463 EQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRL------AEQELLEA-TERLNLLHSQNTGLLNQKKKLEV 1535
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylapARREQAEElRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907142940 1536 DLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1610
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1146-1724 |
3.94e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1146 LREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLalrlqEAEEgveaanakcssleKAKLRLQ 1225
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKII-----EAQR-------------KAIQELQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1226 TESEDVTLELERATSAAAALDKKQ---RHLERALEERRRQEEEMQRELEAAQREARGLGTEL------------------ 1284
Cdd:pfam05483 127 FENEKVSLKLEEEIQENKDLIKENnatRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLnnniekmilafeelrvqa 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1285 --------FRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQEL------EKAKKALEGEKSELQAALEEA 1350
Cdd:pfam05483 207 enarlemhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflleeSRDKANQLEEKTKLQDENLKE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1351 EGALELEETKTLR-----IQLELSQVKA-EVDRKLAEK-------DEECTNLRRNHQRAVESLQAS-LDAETRARNEALR 1416
Cdd:pfam05483 287 LIEKKDHLTKELEdikmsLQRSMSTQKAlEEDLQIATKticqlteEKEAQMEELNKAKAAHSFVVTeFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1417 L-KKKMEGDLNDLELQLGHATRQAMEAQAATRL----------LQAQLKEEQAGRDEE---QRLAAELREQGQALERRAA 1482
Cdd:pfam05483 367 TeQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleeLKKILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1483 LLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAI 1562
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCK 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1563 TDAAMMAEELKKEQDTSAHL----ERMKKTLEQTVRELQARLEEAEQAAlRGGKKQVQKLEAKVRELEAELDAEQKKHAE 1638
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLrdelESVREEFIQKGDEVKCKLDKSEENA-RSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1639 ALKGVRKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAET 1718
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAD 685
|
....*.
gi 1907142940 1719 QANKLR 1724
Cdd:pfam05483 686 EAVKLQ 691
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
691-1315 |
1.29e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 691 ALQLQAEQDNLADAEERCHLLiksKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKkdiddleltlAKAEKE 770
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHL---HFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKR----------DELNGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 771 KQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQAL----GDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKK 846
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 847 L---RMDTERAKRKLEGDLKLTQEtvtdtTQDKQQLEEKLKkkdSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEE 923
Cdd:pfam12128 390 RdiaGIKDKLAKIREARDRQLAVA-----EDDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 924 ELEAERAARARVEKQRAE---AARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEAT----VAALR 996
Cdd:pfam12128 462 LLLQLENFDERIERAREEqeaANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtlLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 997 RKQADSAAELSEQVDSLQRIRQKLEKEKSEL----------------RMEVDDLGASVETLARGKASAEKLCRT------ 1054
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRIDVPEWAASEEELRERLDKAEEALQSarekqa 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1055 -YEDQLSEAKIKVEELQRQLADASTQrgrLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKakgALA 1133
Cdd:pfam12128 622 aAEEQLVQANGELEKASREETFARTA---LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK---QLD 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1134 HAVQALRHDCDllREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLqeAEEGVEaanak 1213
Cdd:pfam12128 696 KKHQAWLEEQK--EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL--ASLGVD----- 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1214 csslEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGlgtELFRLRHSHEE 1293
Cdd:pfam12128 767 ----PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ---QLARLIADTKL 839
|
650 660
....*....|....*....|..
gi 1907142940 1294 ALEALETLKRENKNLQEEISDL 1315
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSEN 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1499-1722 |
1.34e-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: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1499 ERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT 1578
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1579 SAHLER-MKKTLEQTVRELQARLEEAEQAALRGG--KKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVY 1655
Cdd:COG4942 106 LAELLRaLYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142940 1656 QTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANK 1722
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1505-1732 |
1.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1505 AEQELLEATERLNLLhsqntgllnqkkklevdlaqlsGEVEEAAQERREAEEKAkkAITDAAMMAEELKKEQDTSAHLER 1584
Cdd:COG4913 240 AHEALEDAREQIELL----------------------EPIRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1585 MKKTLEQTVRELQARLEEAEQAaLRGGKKQVQKLEAKVR--------ELEAELDAEQKKHAEALKGVRKHERRVKELVYQ 1656
Cdd:COG4913 296 ELEELRAELARLEAELERLEAR-LDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1657 TEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELddAEERADMAETQAN------KLRARSRDA 1730
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEIASLERRKSNiparllALRDALAEA 452
|
..
gi 1907142940 1731 LG 1732
Cdd:COG4913 453 LG 454
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
688-914 |
1.65e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 688 NDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKA 767
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 768 EKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKL 847
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142940 848 RMDTERAKRKLEGDLKLTQETVTDTTQD-------KQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKEL 914
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKElkklneeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
977-1684 |
1.74e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 977 LRRELEEAVLRHEATVAALRRKQADSAAELSE---QVDSLQRIRQKLEKEKSELRmevDDLGASVETLARGKAsaeklcr 1053
Cdd:pfam15921 90 LQRRLNESNELHEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR---NQLQNTVHELEAAKC------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1054 TYEDQLSEAKIKVEELQRQLAdasTQRGRLQTENGEL-------GRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEES 1126
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMML---SHEGVLQEIRSILvdfeeasGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1127 KAK-GALAHAVQALRHDC----DLLREQHEEE-----SEAQAELQRLLSKANAEVAQWRS-------------------- 1176
Cdd:pfam15921 237 KGRiFPVEDQLEALKSESqnkiELLLQQHQDRieqliSEHEVEITGLTEKASSARSQANSiqsqleiiqeqarnqnsmym 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1177 ----KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHL 1252
Cdd:pfam15921 317 rqlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1253 ERALEERRRQEEEMQRELEAAQREARGLGTELFRLrhshEEALEALET-----LKRENKNLQ------EEISDLTDQVSl 1321
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL----EALLKAMKSecqgqMERQMAAIQgkneslEKVSSLTAQLE- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1322 sgKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQL---ELSQVKAEVDRKLAE----KDEEctnlrrNHQ 1394
Cdd:pfam15921 472 --STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAtnaEITKLRSRVDLKLQElqhlKNEG------DHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1395 RAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHaTRQAMEAQaatrllQAQLKEEQAGRDEEQRLAAELREQG 1474
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR-TAGAMQVE------KAQLEKEINDRRLELQEFKILKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1475 QALERRAALLAAELEELRAALEQGERSRRLAEQEL-LEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERRE 1553
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIkQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1554 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRE-------LQARLEEAEQAaLRGGKKQVQKLEAKVRELE 1626
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAkrgqidaLQSKIQFLEEA-MTNANKEKHFLKEEKNKLS 775
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907142940 1627 AELDA---EQKKHAEALKGVRKHERRVKELVYQTEE--DRKNL--ARMQDLVDKLQSKVKSYKRQ 1684
Cdd:pfam15921 776 QELSTvatEKNKMAGELEVLRSQERRLKEKVANMEValDKASLqfAECQDIIQRQEQESVRLKLQ 840
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
451-478 |
1.89e-06 |
|
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: 49.65 E-value: 1.89e-06
10 20
....*....|....*....|....*...
gi 1907142940 451 SQLHKENLNKLMTNLRATQPHFVRCIVP 478
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
638-822 |
1.90e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.08 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 638 KMKPLLRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERchllikskvq 717
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 718 lEAKVKELSERLEDEEEVNAdlaarrrkledecteLKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTK 797
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA---------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180
....*....|....*....|....*
gi 1907142940 798 EKKALQEAHQQALGDLQAEEDRVSA 822
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEELEA 163
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
654-1202 |
2.88e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.45 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 654 ALRAELRGLRGALATAEAKRQELEETQVSVTQE-----KNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAK----VKE 724
Cdd:pfam07111 112 AGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKrageAKQ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 725 LSERLEDEEEVNADLAARRRKLEDECT---ELKKDIDDL---ELTLAKAEKEKQATENKVKNLTEEMAALDEAV------ 792
Cdd:pfam07111 192 LAEAQKEAELLRKQLSKTQEELEAQVTlveSLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVellqvr 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 793 VRLTKEKKALQEAHQ----QALGDLQAEEDRvsalaKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQET 868
Cdd:pfam07111 272 VQSLTHMLALQEEELtrkiQPSDSLEPEFPK-----KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 869 VTDTTQDKQQLEEKLKKKDSElsqlnlrVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARV--EKQRAEAAREL 946
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAE-------VEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVvnAMSSTQIWLET 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 947 EELSERLEEAGGASAGQR--EGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADsaAELSEQVDSLQRIRQKLEKE- 1023
Cdd:pfam07111 420 TMTRVEQAVARIPSLSNRlsYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVD--ADLSLELEQLREERNRLDAEl 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1024 KSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQ 1103
Cdd:pfam07111 498 QLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQ 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1104 LSRGKTSAAQS--LEELRRQLEEESKAKGALAHAVQALRHdcdlLREQHEEESEAQAELQRLLSKANAEVAQWRSKyead 1181
Cdd:pfam07111 578 ALQEKVAEVETrlREQLSDTKRRLNEARREQAKAVVSLRQ----IQHRATQEKERNQELRRLQDEARKEEGQRLAR---- 649
|
570 580
....*....|....*....|.
gi 1907142940 1182 aiqRTEELEEAKKKLALRLQE 1202
Cdd:pfam07111 650 ---RVQELERDKNLMLATLQQ 667
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
770-1472 |
5.76e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 770 EKQATENKVKNLTEEMAALDEA---VVRLTKEKKALQ------EAHQQALGDLQAEEDRVSAL-----AKAKIRLEQQVE 835
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAheaLEDAREQIELLEpirelaERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 836 DLECSLEQEKKLRMDTERAKRKLEGDL-KLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEdeqlvgvQLQKKIKEL 914
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRA-------RLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 915 QARAEELEEEleaeraararVEKQRAEAARELEelserleeaggASAGQREGCRKREAELGRLRRELEEAVLRHEATVAA 994
Cdd:COG4913 372 GLPLPASAEE----------FAALRAEAAALLE-----------ALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 995 LRRKQADSAAELseqVDSLQRIRQKLEKEKSELR-----MEVDDLGASVETlargkaSAEKLCRTY-------EDQLSEA 1062
Cdd:COG4913 431 LERRKSNIPARL---LALRDALAEALGLDEAELPfvgelIEVRPEEERWRG------AIERVLGGFaltllvpPEHYAAA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1063 KIKVEELQrqladastQRGRLQTE-----NGELGRLLEEKESMISQLSrgktsaaqsleelrrqleeeSKAKGALAHAVQ 1137
Cdd:COG4913 502 LRWVNRLH--------LRGRLVYErvrtgLPDPERPRLDPDSLAGKLD--------------------FKPHPFRAWLEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1138 ALRHDCDLLREQHEEE--SEAQAELQRLLSKANAEVAQ------WRSKY--EADAIQRTEELEEAKKKLALRLQEAEEGV 1207
Cdd:COG4913 554 ELGRRFDYVCVDSPEElrRHPRAITRAGQVKGNGTRHEkddrrrIRSRYvlGFDNRAKLAALEAELAELEEELAEAEERL 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1208 EAANAKCSSLEKAKLRLQTESEDVTLELERAtSAAAALDKKQRhleraleerrrqeeeMQRELEAAQREARGLGTELfrl 1287
Cdd:COG4913 634 EALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEA---------------ELERLDASSDDLAALEEQL--- 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1288 rhshEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLE 1367
Cdd:COG4913 695 ----EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1368 LSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGD-LNDLELQLGHATRQAMEAQAAT 1446
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERFKELLNENSIEFVAD 850
|
730 740
....*....|....*....|....*..
gi 1907142940 1447 rlLQAQLKEE-QAGRDEEQRLAAELRE 1472
Cdd:COG4913 851 --LLSKLRRAiREIKERIDPLNDSLKR 875
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1543-1652 |
6.15e-06 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 50.37 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1543 EVEEAAQERREAEEKAKKAITDAAMMAEELkkeqdtsahlERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEaKV 1622
Cdd:pfam07767 206 EAEKKRLKEEEKLERVLEKIAESAATAEAR----------EEKRKTKAQRNKEKRRKEEEREAKEEKALKKKLAQLE-RL 274
|
90 100 110
....*....|....*....|....*....|
gi 1907142940 1623 RELEAELDAEQKKHAEALKGVRKHERRVKE 1652
Cdd:pfam07767 275 KEIAKEIAEKEKEREEKAEARKREKRKKKK 304
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
654-899 |
7.05e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 654 ALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKV-KELSERLEDE 732
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSA 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 733 EEVNADLAARRRKLEDECTELKKDIDD--LELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQAL 810
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 811 GDLQAEEDRVSalakakiRLEQQVEDLECSLEQEKKLRM-------------------------DTERAKRKLEGDL-KL 864
Cdd:pfam12128 761 ASLGVDPDVIA-------KLKREIRTLERKIERIAVRRQevlryfdwyqetwlqrrprlatqlsNIERAISELQQQLaRL 833
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907142940 865 TQETVTDTTQ--------DKQQ--LEEKLKKKDSELSQLNLRVED 899
Cdd:pfam12128 834 IADTKLRRAKlemerkasEKQQvrLSENLRGLRCEMSKLATLKED 878
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1544-1683 |
8.10e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 50.63 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1544 VEEAAQERREAE--EKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEqaalrggkKQVQKLEAK 1621
Cdd:COG2433 378 IEEALEELIEKElpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD--------ERIERLERE 449
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907142940 1622 VRELEAELDAEQKKHAEalkgVRKHERRVKELvyqteedRKNLARMQDLVDKLQSKVKSYKR 1683
Cdd:COG2433 450 LSEARSEERREIRKDRE----ISRLDREIERL-------ERELEEERERIEELKRKLERLKE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1270-1713 |
9.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1270 LEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEE 1349
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1350 aegaleleetktlriqLELSQVKAEVDRKLAEKDEECTNLR------RNHQRAVESLQASLDAETRARNEALR-LKKKME 1422
Cdd:COG4717 128 ----------------LPLYQELEALEAELAELPERLEELEerleelRELEEELEELEAELAELQEELEELLEqLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1423 GDLNDLELQLGHATRQAMEAQAATRLLQAQLK--EEQAGRDEEQRLAAELREQGQALE---------------------- 1478
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEelEEELEQLENELEAAALEERLKEARlllliaaallallglggsllsl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1479 -------------------RRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQ 1539
Cdd:COG4717 272 iltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1540 LSGEVEEAAQERR-EAEEKAKKAITDAAMMA--EELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQvq 1616
Cdd:COG4717 352 LLREAEELEEELQlEELEQEIAALLAEAGVEdeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1617 kLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELvyqtEEDrknlarmqDLVDKLQSKVKSYKRQFEEAEQQAstnl 1696
Cdd:COG4717 430 -LEEELEELEEELEELEEELEELREELAELEAELEQL----EED--------GELAELLQELEELKAELRELAEEW---- 492
|
490
....*....|....*..
gi 1907142940 1697 AKYRKAQHELDDAEERA 1713
Cdd:COG4717 493 AALKLALELLEEAREEY 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
644-1033 |
1.09e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 644 RSAQAEEELAALRAELRGLRGALATAEAKRQELEetqvsVTQEKNDLALQLQAEQDNLADAEERchllIKSKVQLEAKVK 723
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERLEELEER----LEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 724 ELSERLED-EEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKAL 802
Cdd:COG4717 167 ELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 803 QE-----------AHQQALGDLQAEEDRVSALA---------------KAKIRLEQQVEDLECSLEQEKKLRMDTERAKR 856
Cdd:COG4717 247 EArlllliaaallALLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 857 KLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRvedeqlvgvQLQKKIKELqaRAEELEEELEAERAARARVE 936
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE---------ELEQEIAAL--LAEAGVEDEEELRAALEQAE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 937 KQRAEAARELEELSERLEEAGGASAGQREGCRKR-EAELGRLRRELEEAvlrhEATVAALRRKQADSAAELS--EQVDSL 1013
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEEL----EEELEELREELAELEAELEqlEEDGEL 471
|
410 420
....*....|....*....|
gi 1907142940 1014 QRIRQKLEKEKSELRMEVDD 1033
Cdd:COG4717 472 AELLQELEELKAELRELAEE 491
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
645-836 |
2.08e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 645 SAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERchlLIKSKVQLEAKVKE 724
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 725 LSERL------------------------------------EDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAE 768
Cdd:COG3883 88 LGERAralyrsggsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 769 KEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVED 836
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1582-1703 |
2.26e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1582 LERMKK-TLEQTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALkgvrkheRRVKELV 1654
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907142940 1655 YQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAkyRKAQ 1703
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ 190
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
670-1344 |
2.94e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 670 EAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDE 749
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 750 CTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQAlgDLQAEEDRVSALAKAKIR 829
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL--SKAEKNSLTETLKKEVKS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 830 LEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETvtdTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGV--QL 907
Cdd:TIGR00606 506 LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK---MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWlhSK 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 908 QKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGgasagqreGCRKREAELGRLRRELEEAVlR 987
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC--------GSQDEESDLERLKEEIEKSS-K 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 988 HEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVE 1067
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1068 ----ELQRQLADASTQRGRLQTENGELGRL---LEEKESMISQLSRGKTSAA--------------QSLEELRRQLEEES 1126
Cdd:TIGR00606 734 grqsIIDLKEKEIPELRNKLQKVNRDIQRLkndIEEQETLLGTIMPEEESAKvcltdvtimerfqmELKDVERKIAQQAA 813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1127 KAKGA-LAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYE---------ADAIQRTEELEEAKKKL 1196
Cdd:TIGR00606 814 KLQGSdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNelkseklqiGTNLQRRQQFEEQLVEL 893
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1197 ALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELEraTSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQRE 1276
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE--TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY 971
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907142940 1277 ARGLGTELFRLRHSHEEALEALETLKRENKNLQEEI-------SDLTDQVSLSGKS--IQELEKAKKALEGEKSELQ 1344
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqkiqeRWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQ 1048
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
649-868 |
3.71e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 649 EEELAALRAELRglrgalaTAEAKRQELEETQ--VSVTQEKNDLALQLQAEQDNLADAEERchlliksKVQLEAKVKELS 726
Cdd:COG3206 181 EEQLPELRKELE-------EAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 727 ERLEDEEEVNADLAArrrklEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVvrltkeKKALQEAH 806
Cdd:COG3206 247 AQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 807 QQALGDLQAEEDRVSALAKAKIRLEQQVEDLEcSLEQE-KKLRMDTERAKRKLEGDLKLTQET 868
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAElRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1552-1715 |
3.91e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1552 REAEEKAKKAITDAAMMAEELKKEQDTSA--HLERMKKTLEQTVRELQARLEEAEQaALRGGKKQVQKLEAKVRELEAEL 1629
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEKELRERRNELQKLEK-RLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1630 DAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMqdlvdklqSKVKSYKRQFEEAEQQASTNLAKYRKAQHEldDA 1709
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--------TAEEAKEILLEKVEEEARHEAAVLIKEIEE--EA 182
|
....*.
gi 1907142940 1710 EERADM 1715
Cdd:PRK12704 183 KEEADK 188
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
718-1455 |
4.88e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 718 LEAKVKELSERLEDEEEVN--ADLAARRR--------KLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAA 787
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDqyTQLALMEFakkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 788 LDEAVVRLTKEKKALQEAH--QQALGDLQAEEDRVSALAKakiRLEQQVEDLECSLEQEKklrmdterakrklegdLKLT 865
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEA---VLEETQERINRARKAAP----------------LAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 866 QETVTDTTQDKQQLEEKLKKKDSELSQLNlrvedEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARE 945
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLL-----MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 946 LEELSERLEeaggASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKS 1025
Cdd:TIGR00618 374 QHTLTQHIH----TLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1026 ELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLadastqrgrlqtENGELGRLLEEKESMISQls 1105
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL------------ELQEEPCPLCGSCIHPNP-- 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1106 rgKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQ----HEEESEAQAELQRLLSKANA--EVAQWRSKYE 1179
Cdd:TIGR00618 516 --ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQraslKEQMQEIQQSFSILTQCDNRskEDIPNLQNIT 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1180 ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKcssLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERA-LEE 1258
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL---QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSiRVL 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1259 RRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQE-------EISDLTDQVSLSGKSIQELEK 1331
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienasssLGSDLAAREDALNQSLKELMH 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1332 AKKALEGEKSELQAALEEAEGALELEETKTLRIQLELS---QVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAET 1408
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQffnRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907142940 1409 RARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQLKE 1455
Cdd:TIGR00618 831 EQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
642-899 |
5.03e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 642 LLRSAQAEEELAALRAELRGLRGALATAE-AKRQeleetqvsVTQEKNDLalqlqaeQDNLADAEERCHLLIKSKVQLEA 720
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASErARRQ--------AQQERDEL-------ADEIASGASGKSALQDEKRRLEA 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 721 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVvrLTKEKK 800
Cdd:pfam01576 890 RIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV--KSKFKS 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 801 ALQEahqqalgdlqaeedrvsalakakirLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLE 880
Cdd:pfam01576 968 SIAA-------------------------LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
250
....*....|....*....
gi 1907142940 881 EKLKKKDSELSQLNLRVED 899
Cdd:pfam01576 1023 DQAEKGNSRMKQLKRQLEE 1041
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1499-1708 |
5.38e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.36 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1499 ERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAE------EKAKKAIT--------- 1563
Cdd:PLN02939 141 EKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEileeqlEKLRNELLirgateglc 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1564 --------------------DAAMMAEELKKEQDTS---AHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEA 1620
Cdd:PLN02939 221 vhslskeldvlkeenmllkdDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1621 KVRELEAELDAEQKKHAEA---LKGVRKHERRVKELVYQTEEdrKNLARMQ-DLVDKLQSKVKSYKRQFEEAEQQASTNL 1696
Cdd:PLN02939 301 KVENLQDLLDRATNQVEKAalvLDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYI 378
|
250
....*....|..
gi 1907142940 1697 AKYRKAQHELDD 1708
Cdd:PLN02939 379 QLYQESIKEFQD 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
700-1337 |
5.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 700 NLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLED---ECTELKKDIDDLELTLAKAEKEKQaten 776
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEVK---- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 777 KVKNLTEEMAALDEAVVRLTKEKKALQEahqqalgDLQAEEDRVSALAKAKIRLEQQVEDLEcSLEQEKKLRMDTERAKR 856
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEE-------KIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 857 KLEGDLKLTQETVTDTTQDKQQLEEKLKkkdsELSQLNLRVEdeqlvgvQLQKKIKELQARAEELEEELEAERAARARVE 936
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLE-------ELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 937 kqraeaareleelserleeaggasagQREGCRKREA--ELGRLRRELEEAVLRHEatvaalrrkqadsaaELSEQVDSLQ 1014
Cdd:PRK03918 373 --------------------------ELERLKKRLTglTPEKLEKELEELEKAKE---------------EIEEEISKIT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1015 RIRQKLEKEKSELRMEVDDLgasvetlargkASAEKLCRTYEDQLSEAKIK--VEELQRQLADASTQRGRLQTENGELGR 1092
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEEL-----------KKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRK 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1093 LLEEKESMI---SQLSRGKTSAAQsleelrrQLEEESKAKGalaHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANA 1169
Cdd:PRK03918 481 ELRELEKVLkkeSELIKLKELAEQ-------LKELEEKLKK---YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1170 EVAQWRSKyeADAIQRTEELEEAKKKLALRLQE-AEEGVEAANAKCSSLEKAK---LRLQTESEDVTLELERATSAAAAL 1245
Cdd:PRK03918 551 LEELKKKL--AELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYneyLELKDAEKELEREEKELKKLEEEL 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1246 DKKqrhlERALEERRRQEEEMQRELEAAQR-----EARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVS 1320
Cdd:PRK03918 629 DKA----FEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
650
....*....|....*..
gi 1907142940 1321 LSGKSIQELEKAKKALE 1337
Cdd:PRK03918 705 EREKAKKELEKLEKALE 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1439-1700 |
6.34e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1439 AMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQgqalerrAALLAAELEELRAALEQGERSRRLAEQELLEATERLNL 1518
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1519 LHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKeqdTSAHLERMKKTLEQTVRELQA 1598
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY---LAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1599 RLEEAEQAalrggKKQVQKLEAKVRELEAELDAEQKKHAEALKgvrKHERRVKELVYQTEEDRKNLARMQDLVDKLQskv 1678
Cdd:COG4942 165 LRAELEAE-----RAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE--- 233
|
250 260
....*....|....*....|..
gi 1907142940 1679 ksyKRQFEEAEQQASTNLAKYR 1700
Cdd:COG4942 234 ---AEAAAAAERTPAAGFAALK 252
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
644-857 |
7.54e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 644 RSAQAEEELAALRAELRGLRGALATAEAKrQELEETQVSVTQEKNDLALQLQAEQDNLADAEERchllIKSKVQLEAKVK 723
Cdd:PRK05035 464 REKAAREARHKKAAEARAAKDKDAVAAAL-ARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR----KAQARARQAEKQ 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 724 ELSERLEDEEEVNADLA---ARRRKLEDECTELKKDIDDL------ELTLAKAEKEKQATENKVKNLTEEMAALDEAVVR 794
Cdd:PRK05035 539 AAAAADPKKAAVAAAIArakAKKAAQQAANAEAEEEVDPKkaavaaAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVA 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 795 LTKEKKALQEAHQQALGDLQAEED----RVS-ALAKAKIRLEQQVEDLECSLEQE--KKLRMDTERAKRK 857
Cdd:PRK05035 619 AAIARAKAKKAEQQANAEPEEPVDprkaAVAaAIARAKARKAAQQQANAEPEEAEdpKKAAVAAAIARAK 688
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1144-1694 |
8.37e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1144 DLLREQHEEESEAQAELQRLlsKANAEVAQwRSKYEADAI--------QRTEELEEAKKKLALRLQEAEEGVEAANAKCS 1215
Cdd:PRK02224 206 ERLNGLESELAELDEEIERY--EEQREQAR-ETRDEADEVleeheerrEELETLEAEIEDLRETIAETEREREELAEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1216 SLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEAL 1295
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1296 EALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKA--KKALEGEKSELQAALEEAEGALELEETKTLRIQL-ELSQVK 1372
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELREREAELEATLrTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1373 AEVDRKLAE-KDEECTnlrrnhQRAVESLQASLDAETRARNEALRLK-KKMEGDLNDLELQLGHATRQAMEAQAATRLLQ 1450
Cdd:PRK02224 443 EEAEALLEAgKCPECG------QPVEGSPHVETIEEDRERVEELEAElEDLEEEVEEVEERLERAEDLVEAEDRIERLEE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1451 -----AQLKEEQAGRDEEQRL-AAELREQGQALERRAALLaaeleelraaleqgERSRRLAEQELLEATERLNLLHSQNT 1524
Cdd:PRK02224 517 rredlEELIAERRETIEEKRErAEELRERAAELEAEAEEK--------------REAAAEAEEEAEEAREEVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1525 GLLNQKKKLEvDLAQLSGEVEEAAQERREAEEKAKKaitdaamMAEELKKEQDTSAHLERMKKTLEQTVRElqARLEEAE 1604
Cdd:PRK02224 583 ELKERIESLE-RIRTLLAAIADAEDEIERLREKREA-------LAELNDERRERLAEKRERKRELEAEFDE--ARIEEAR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1605 QAALRgGKKQVQKLEAKVRELEAELDAEQKkhaeALKGVrkhERRVKELvyqtEEDRKNLARMQDLVDKLQSkvksykrQ 1684
Cdd:PRK02224 653 EDKER-AEEYLEQVEEKLDELREERDDLQA----EIGAV---ENELEEL----EELRERREALENRVEALEA-------L 713
|
570
....*....|
gi 1907142940 1685 FEEAEQQAST 1694
Cdd:PRK02224 714 YDEAEELESM 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1372-1700 |
1.04e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1372 KAEVDRKLAEKDEECTNL--RRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDL-------ELQLGHATRQAMEA 1442
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIrqeerkrELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1443 QAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGE---RSRRLAEQELLEATERLNLL 1519
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEarqREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1520 HSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKaitdaaMMAEELKKEQDTSAHLERMKKTLEQTVRELQAR 1599
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK------ILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1600 LEEAEQAalrggkkqvqkleakvRELEAELDAEQKKhaealkgvrKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVK 1679
Cdd:pfam17380 529 IYEEERR----------------REAEEERRKQQEM---------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
330 340
....*....|....*....|..
gi 1907142940 1680 SYKRQFE-EAEQQASTNLAKYR 1700
Cdd:pfam17380 584 SEKARAEyEATTPITTIKPIYR 605
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
737-966 |
1.23e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 737 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAE 816
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 817 EDRVSAL---------------AKAKIRLEQQVEDLecsLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEE 881
Cdd:COG3883 99 GGSVSYLdvllgsesfsdfldrLSALSKIADADADL---LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 882 KLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASA 961
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
....*
gi 1907142940 962 GQREG 966
Cdd:COG3883 256 GAAAG 260
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
646-1315 |
1.29e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 646 AQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKndlalQLQAEQDNLADAEERCHLLIKsKVQLEAKVKEL 725
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-----ELRAQEAVLEETQERINRARK-AAPLAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 726 SERLEDEEEVNADLAARRRKLEDE---CTELKKDIDDLElTLAKAEKEKQATENKVKNLTEEMAALDEavvRLTKEKKAL 802
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIRE---ISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 803 QEAHQQAlGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQqlEEK 882
Cdd:TIGR00618 379 QHIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ--CEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 883 LKKKDSELSQLNLRVEDEQLVgvQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAggasag 962
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQ--TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT------ 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 963 qregCRKREAELGRLRRELEEAVLRHEATvaALRRKQADSAAELSEQVDSLQRIRQKLEKEKSE---LRMEVDDLGASVE 1039
Cdd:TIGR00618 528 ----RRMQRGEQTYAQLETSEEDVYHQLT--SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTE 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1040 TLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRgkTSAAQSLEELR 1119
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR--VLPKELLASRQ 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1120 RQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALR 1199
Cdd:TIGR00618 680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKAR 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1200 LQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARG 1279
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE 839
|
650 660 670
....*....|....*....|....*....|....*....
gi 1907142940 1280 LGTELFRLRH---SHEEALEALETLKRENKNLQEEISDL 1315
Cdd:TIGR00618 840 KSATLGEITHqllKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1286-1732 |
1.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1286 RLRHSHEEALEALETL--KRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGAleleetktlr 1363
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER---------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1364 iQLELSQVKAEVDrKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQ 1443
Cdd:PRK02224 250 -REELETLEAEIE-DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1444 AATR--LLQAQLKEEQAGRDEEQrlAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHS 1521
Cdd:PRK02224 328 DRLEecRVAAQAHNEEAESLRED--ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1522 QNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAitdAAMMAE----ELKKEQDTSAHLERMKKTLEQtVRELQ 1597
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEA---EALLEAgkcpECGQPVEGSPHVETIEEDRER-VEELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1598 ARLEEAEQaalrggkkQVQKLEAKVRELEAELDAEqkKHAEALKGVRKH-ERRVKELVYQTEEDRKNLARMQDLVDKLQS 1676
Cdd:PRK02224 482 AELEDLEE--------EVEEVEERLERAEDLVEAE--DRIERLEERREDlEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 1677 KVKSYKRQFEEAEQQAST---NLAKYRKAQHELDDAEERADMAETQANkLRARSRDALG 1732
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIE 609
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
646-770 |
1.59e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 646 AQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEK--NDLALQLQAEQDNLADAEERchlLIKSKVQLEAKVK 723
Cdd:COG1579 48 EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLEDE---ILELMERIEELEE 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907142940 724 ELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKE 770
Cdd:COG1579 125 ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
638-941 |
1.66e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 638 KMKPLLRSAQAEEELAALRAELRGLRGALATAEAKRQ--ELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSK 715
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 716 vqlEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDiddlELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRL 795
Cdd:PTZ00121 1591 ---EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 796 TKEKKALQEAHQQALGDLQAEEDRVSAlAKAKIRLEQQVEDLEcsleqekKLRMDTERAKRKLEGDLKLTQETVTDTTQD 875
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKA-AEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 876 KQQLEEKLKKKDSelsqlnLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAE 941
Cdd:PTZ00121 1736 KKEAEEDKKKAEE------AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1505-1730 |
2.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1505 AEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1584
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1585 MK--KTLEQTVRELQA--RLEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEED 1660
Cdd:COG3883 108 LLgsESFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1661 RKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRARSRDA 1730
Cdd:COG3883 188 SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1543-1705 |
2.15e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.10 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1543 EVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEE----AEQAALRGGKKQVQKL 1618
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERkqrlQLQAAQERARQQQEEF 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1619 EAKVRELeaeldaEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQdlvdklQSKVKSYKRQFEEAEQQASTNLAK 1698
Cdd:pfam15709 429 RRKLQEL------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA------EEERLEYQRQKQEAEEKARLEAEE 496
|
....*..
gi 1907142940 1699 YRKAQHE 1705
Cdd:pfam15709 497 RRQKEEE 503
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
672-1198 |
2.15e-04 |
|
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: 46.25 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 672 KRQELEETQVSVTQEKN---DLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLED 748
Cdd:pfam05483 238 KEKQVSLLLIQITEKENkmkDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 749 ECTELKKDIDDL----ELTLAKAEKEKQATENKVKNLTEEMAALDEAvvrLTKEKKALQEAHQQ---ALGDLQAEEDRVS 821
Cdd:pfam05483 318 DLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEEL---LRTEQQRLEKNEDQlkiITMELQKKSSELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 822 ALAKAKIRLEQQVEDLECSLEQEKKLrMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKkkdselSQLNLRVEDEQ 901
Cdd:pfam05483 395 EMTKFKNNKEVELEELKKILAEDEKL-LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLE------IQLTAIKTSEE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 902 LVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRK----REAELgRL 977
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQienlEEKEM-NL 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 978 RRELE---EAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRT 1054
Cdd:pfam05483 547 RDELEsvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1055 YEDQLSEAKIKVEELQRQLADASTQRGRL-QTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALA 1133
Cdd:pfam05483 627 ENKQLNAYEIKVNKLELELASAKQKFEEIiDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1134 HAVQALRHDCD-----------LLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLAL 1198
Cdd:pfam05483 707 ALMEKHKHQYDkiieerdselgLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1505-1703 |
2.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1505 AEQELLEATERLNLLHSQN--TGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAhl 1582
Cdd:COG3206 187 LRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1583 ermKKTLEQTVRELQARLEEAEQaalRGGKK--QVQKLEAKVRELEAELDAEQKKHAEALKG-VRKHERRVKELVYQTEE 1659
Cdd:COG3206 265 ---IQQLRAQLAELEAELAELSA---RYTPNhpDVIALRAQIAALRAQLQQEAQRILASLEAeLEALQAREASLQAQLAQ 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907142940 1660 DRKNLARMQdlvdKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQ 1703
Cdd:COG3206 339 LEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
641-802 |
2.34e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 641 PLLRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEA 720
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 721 KVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLE---LT----LAKAEKEKQATENKVKNLTEEMAALDEAVV 793
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaieeYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
....*....
gi 1907142940 794 RLTKEKKAL 802
Cdd:COG1196 820 EIDRETRER 828
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
719-881 |
2.51e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 719 EAKvKELSERLEDEEEVNADLAARRRKLEDEctelkkdiddleltLAKAEKEKQATENKVKNLTEEMAALDEavvRLTKE 798
Cdd:PRK00409 506 EAK-KLIGEDKEKLNELIASLEELERELEQK--------------AEEAEALLKEAEKLKEELEEKKEKLQE---EEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 799 KKALQEAHQQALGDLQAEEDRVsalakakIRLEQQVEDLECSLEQEKKLrmdtERAKRKLEGDLKLTQETVTDTTQDKQQ 878
Cdd:PRK00409 568 LEEAEKEAQQAIKEAKKEADEI-------IKELRQLQKGGYASVKAHEL----IEARKRLNKANEKKEKKKKKQKEKQEE 636
|
...
gi 1907142940 879 LEE 881
Cdd:PRK00409 637 LKV 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
873-1112 |
2.59e-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: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 873 TQDKQQLEEKLKKKDSELSQLNLRVEdeqlvgvQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSER 952
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 953 LEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRkqadSAAELSEQVDSLQRIRQKLEKEKSELRMEVD 1032
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR----RLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1033 DLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAA 1112
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
712-901 |
3.24e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 712 IKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEA 791
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 792 VVRltKEKKALQEAHQQALGDLQAEEDR--------VSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAK----RKLE 859
Cdd:pfam17380 364 RIR--QEEIAMEISRMRELERLQMERQQknervrqeLEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLE 441
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907142940 860 GDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDEQ 901
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
971-1193 |
3.58e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 971 EAELGRLRRELEEAvlrhEATVAALRRKQadSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEK 1050
Cdd:COG3206 181 EEQLPELRKELEEA----EAALEEFRQKN--GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1051 LCRTYED--QLSEAKIKVEELQRQLADASTqrgRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRqleeeska 1128
Cdd:COG3206 255 ALPELLQspVIQQLRAQLAELEAELAELSA---RYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE-------- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907142940 1129 kgALAHAVQALRHDCDLLREQHEEESEAQAELQRLlsKANAEVAqwRSKYEAdAIQRTEELEEAK 1193
Cdd:COG3206 324 --ALQAREASLQAQLAQLEARLAELPELEAELRRL--EREVEVA--RELYES-LLQRLEEARLAE 381
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
658-914 |
3.92e-04 |
|
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: 45.48 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 658 ELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNA 737
Cdd:pfam05483 409 ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNI 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 738 DLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEE 817
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 818 DRVsalakakirlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRV 897
Cdd:pfam05483 569 DKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV 638
|
250
....*....|....*..
gi 1907142940 898 EDEQLVGVQLQKKIKEL 914
Cdd:pfam05483 639 NKLELELASAKQKFEEI 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1155-1578 |
4.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1155 EAQAELQRLLSKANAEVAQWRSKYE--ADAIQRTEELEEAKKKLALRLQEAEEGVEAANAkCSSLEKAKLRLQTESEDVT 1232
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEelEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1233 LELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEI 1312
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1313 SDLTDQVsLSGKSIQELEKAKK---------ALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKD 1383
Cdd:COG4717 230 EQLENEL-EAAALEERLKEARLllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1384 EEcTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRL------LQAQLKEEQ 1457
Cdd:COG4717 309 AL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1458 AGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLA--EQELLEATERLNLLHSQNTGLLNQKKKLEV 1535
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEelEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907142940 1536 D--LAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDT 1578
Cdd:COG4717 468 DgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
651-843 |
4.21e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 651 ELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSkvQLEAKVKELSERlE 730
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-A 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 731 DEEEVNADLAARRRKLEdecTELKKDIDDLELTLAKAekeKQATENKVKNLTEEMAALDEAVVRLT------------KE 798
Cdd:COG4913 763 VERELRENLEERIDALR---ARLNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDrleedglpeyeeRF 836
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907142940 799 KKALQEAHQQALGDLQaeedrvSALAKAKIRLEQQVEDLECSLEQ 843
Cdd:COG4913 837 KELLNENSIEFVADLL------SKLRRAIREIKERIDPLNDSLKR 875
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1065-1473 |
4.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1065 KVEELQRQLADASTQRGRLQTENGELGRLLEEKESMisQLSRGKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCD 1144
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1145 LLREQHEEESEAQAELQRL---LSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAK 1221
Cdd:COG4717 150 ELEERLEELRELEEELEELeaeLAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1222 LRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLG-TELFRLRHSHEEALEALET 1300
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLfLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1301 LKRENKNLQEEISDLTDQVSLSGK-SIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVD-RK 1378
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1379 LAEKDEECTNLRRnhqrAVESLQASLDAETRARNEALRlkkkmEGDLNDLELQLGHATRQAMEAQAATRLLQAQLKEEQA 1458
Cdd:COG4717 390 ALEQAEEYQELKE----ELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410
....*....|....*..
gi 1907142940 1459 GRD--EEQRLAAELREQ 1473
Cdd:COG4717 461 ELEqlEEDGELAELLQE 477
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
981-1687 |
5.09e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 981 LEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETL-ARGKASAEKLCRTYEDQL 1059
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAAdAAVAKDRSELEALEDQHG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1060 SEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEEL---RRQLEEESKAKGALAHAV 1136
Cdd:pfam12128 333 AFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagIKDKLAKIREARDRQLAV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1137 Q--ALRHDCDLLREQHEEESEAQAELQRLLSKANAEVaqwrsKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKC 1214
Cdd:pfam12128 413 AedDLQALESELREQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATATPELLLQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1215 SSLEKAKLRLQTESEDVTLELERATsaAAALDKKQRHLERALEERRRQEEEMQRELEAA----QREARGLGTELFRLRHS 1290
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQAS--RRLEERQSALDELELQLFPQAGTLLHFLRKEApdweQSIGKVISPELLHRTDL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1291 HEEALEAleTLKRENK----NLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQaaleeaegaleleetktlRIQL 1366
Cdd:pfam12128 566 DPEVWDG--SVGGELNlygvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA------------------AAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1367 ELSQVKAEVDR-KLAEKDEECT--NLRRNHQRAVESLQASLDAETRARNEAlrlKKKMEGDLNDLELQlghatrqameaq 1443
Cdd:pfam12128 626 QLVQANGELEKaSREETFARTAlkNARLDLRRLFDEKQSEKDKKNKALAER---KDSANERLNSLEAQ------------ 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1444 aatrlLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEaTERLNLLhsqn 1523
Cdd:pfam12128 691 -----LKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE-TWYKRDL---- 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1524 tgllnqkKKLEVDLAQLSGeveeAAQERREAEEKakkaITDAAmmaeelKKEQDTSAHLERMKKTLEQTVRELQARLEEA 1603
Cdd:pfam12128 761 -------ASLGVDPDVIAK----LKREIRTLERK----IERIA------VRRQEVLRYFDWYQETWLQRRPRLATQLSNI 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1604 EQAALRgGKKQVQKLEAKVR----ELEAELDAEQKKHAEA---LKGVRKHERRVKELV--YQTEEDRKNLARMQDLVDKL 1674
Cdd:pfam12128 820 ERAISE-LQQQLARLIADTKlrraKLEMERKASEKQQVRLsenLRGLRCEMSKLATLKedANSEQAQGSIGERLAQLEDL 898
|
730
....*....|...
gi 1907142940 1675 QSKVKSYKRQFEE 1687
Cdd:pfam12128 899 KLKRDYLSESVKK 911
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
983-1247 |
5.37e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.29 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 983 EAVLRHE-ATVAALRRKQADSAAELSEQVDSLQRIRQKLEKE----------KSELRMEVDDLGASVETLARGKASAEKL 1051
Cdd:pfam19220 54 EALLAQErAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLeaalreaeaaKEELRIELRDKTAQAEALERQLAAETEQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1052 CRTYED-------QLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRgktsaaqsleelrrqleE 1124
Cdd:pfam19220 134 NRALEEenkalreEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTR-----------------R 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1125 ESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEAdAIQRTEELEEAKKKLALRLQEAE 1204
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEA-LTARAAATEQLLAEARNQLRDRD 275
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907142940 1205 EGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDK 1247
Cdd:pfam19220 276 EAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQR 318
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1001-1244 |
5.38e-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: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1001 DSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLAD--AST 1078
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraRAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1079 QRGRLQTenGELGRLLEEK--ESMISQLSRGKTSAAQsleeLRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEA 1156
Cdd:COG3883 96 YRSGGSV--SYLDVLLGSEsfSDFLDRLSALSKIADA----DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1157 QAELQRLLSKANAEVAQWRSKyEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELE 1236
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
....*...
gi 1907142940 1237 RATSAAAA 1244
Cdd:COG3883 249 AGAAGAAG 256
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
650-1043 |
5.40e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 650 EELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLAdaeerchlLIKSKVQLEAK-------V 722
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLN--------LVQTALRQQEKieryqedL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 723 KELSERLEDEEEVNADLAARRrkledectelkkdiddleltlAKAEKEKQATENKVKNLTEEMA----ALDEAVVRLTKE 798
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL---------------------AEAEARLEAAEEEVDSLKSQLAdyqqALDVQQTRAIQY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 799 KKALQ---EAHQQ-ALGDLQAE--EDRvsaLAKAKIRLEQQVEDLecsLEQEKKLRmDTERAKRKLEGDLKLTQETVTDT 872
Cdd:COG3096 416 QQAVQaleKARALcGLPDLTPEnaEDY---LAAFRAKEQQATEEV---LELEQKLS-VADAARRQFEKAYELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 873 TQD------KQQLEE---------KLKKKDSELSQLNLRVEDEQlvgvQLQKKIKELQARAEELEEELEAERAARARVEK 937
Cdd:COG3096 489 ERSqawqtaRELLRRyrsqqalaqRLQQLRAQLAELEQRLRQQQ----NAERLLEEFCQRIGQQLDAAEELEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 938 QRAEAARELEElserleeaggaSAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRIR 1017
Cdd:COG3096 565 QLEELEEQAAE-----------AVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQ 633
|
410 420
....*....|....*....|....*.
gi 1907142940 1018 QKLEKEKsELRMEVDDLGASVETLAR 1043
Cdd:COG3096 634 QLLERER-EATVERDELAARKQALES 658
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
742-893 |
6.06e-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: 44.63 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 742 RRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKE----KKALQEAhQQALGDLQAEE 817
Cdd:pfam05667 329 LQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQykvkKKTLDLL-PDAEENIAKLQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 818 DRVSALAKAKIRLEQQ-----VEDLEcSLEQEKKLRMDTE-RAKRKLEgDLKLTQETVtdttqdkQQLEEKLKKKDSELS 891
Cdd:pfam05667 408 ALVDASAQRLVELAGQwekhrVPLIE-EYRALKEAKSNKEdESQRKLE-EIKELREKI-------KEVAEEAKQKEELYK 478
|
..
gi 1907142940 892 QL 893
Cdd:pfam05667 479 QL 480
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
650-914 |
7.06e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 650 EELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKvQLEAKVKELSERL 729
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIE-RYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 730 EDEEEVNADLAARRRKLEDECTELKKDIDDL--------------------------------------ELTLAKAEKEK 771
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELksqladyqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 772 QATENKVKNLTEEMAAL-------DEAVVRLTKEKKALQ---------EAHQQALGDL-QAEEDRvsALAKAKIRLEQQV 834
Cdd:PRK04863 445 EEFQAKEQEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQR--HLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 835 EDLECSLEQEKKLrmdtERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKEL 914
Cdd:PRK04863 523 SELEQRLRQQQRA----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
670-914 |
8.11e-04 |
|
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: 44.24 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 670 EAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDE 749
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 750 CTELKKDIDDLELTLAKAEKEKQATE-------NKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSA 822
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 823 LAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRK---LEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVED 899
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE 271
|
250
....*....|....*
gi 1907142940 900 EQLVGVQLQKKIKEL 914
Cdd:TIGR04523 272 KQKELEQNNKKIKEL 286
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1535-1732 |
8.26e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.68 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1535 VDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQdtSAHLERMKKTLEQTVRELQARleEAEQAALRGGKKQ 1614
Cdd:TIGR02794 43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--AAEQARQKELEQRAAAEKAAK--QAEQAAKQAEEKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1615 VQKLEAKVRELE-----AELDAEQKKHAEALKgvrKHERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAE 1689
Cdd:TIGR02794 119 KQAEEAKAKQAAeakakAEAEAERKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907142940 1690 QQASTNLAKYRKAQHELDDAE-ERADMAETQANKLRARSRDALG 1732
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEaAAAAAAEAERKADEAELGDIFG 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
763-964 |
9.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 763 TLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSAL----AKAKIRLEQQVEDLE 838
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeiAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 839 CSLEQEKKLRMDTERAKRKLEGD---------------LKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLV 903
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907142940 904 GVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQR 964
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1545-1641 |
9.96e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1545 EEAAQERREAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEA 1620
Cdd:COG2268 242 AEAELAKKKAEERREaetaRAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAA 321
|
90 100
....*....|....*....|....
gi 1907142940 1621 KVRElEAELDAEQ---KKHAEALK 1641
Cdd:COG2268 322 EAEA-EAEAEAIRakgLAEAEGKR 344
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
716-889 |
1.01e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.07 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 716 VQLEAKVKELSERLEDEEEVNADLAAR-------RRKLEDECTELKKDIDDLELTLAKA----EKEKQATENKVKNLTEE 784
Cdd:pfam09726 398 VRLEQDIKKLKAELQASRQTEQELRSQissltslERSLKSELGQLRQENDLLQTKLHNAvsakQKDKQTVQQLEKRLKAE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 785 MAALDEAVVRLTKEKKALQEAHQQAlgdlqaeeDRVSALAKAKIRleqqvedlECSlEQEKKLRMDTERAKRKLEGDLKL 864
Cdd:pfam09726 478 QEARASAEKQLAEEKKRKKEEEATA--------ARAVALAAASRG--------ECT-ESLKQRKRELESEIKKLTHDIKL 540
|
170 180
....*....|....*....|....*.
gi 1907142940 865 TQETVTDTTQDKQQLEE-KLKKKDSE 889
Cdd:pfam09726 541 KEEQIRELEIKVQELRKyKESEKDTE 566
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-1251 |
1.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 778 VKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRK 857
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 858 LEgdlkltqetvtdTTQDKQQLEEKLKKKDSELSQLNLRVEDEQlvgvQLQKKIKELQARAEELEEELEAERAARARVEK 937
Cdd:COG4717 128 LP------------LYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 938 QR-AEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAELSEQVDSLQRI 1016
Cdd:COG4717 192 EElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1017 RQKLEKeksELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEE 1096
Cdd:COG4717 272 ILTIAG---VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1097 KESMISQLSRGKTSAAQSLEELRRQLEEESkakgALAHAVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRS 1176
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAE----AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1177 KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLE------KAKLRLQTESEDVTLELERATSAAAALDKKQR 1250
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelaELLQELEELKAELRELAEEWAALKLALELLEE 504
|
.
gi 1907142940 1251 H 1251
Cdd:COG4717 505 A 505
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1504-1726 |
1.31e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1504 LAEQELLEATERLNLLHSQNT-GLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKaitdaammaeeLKKEQDTSAhl 1582
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA-----------LKDDNDEET-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1583 ermKKTLE-QTVRELQARLEEAE------QAALRGGKKQVQKLEAKVRELEAELDAEQKKHAE---ALKGVR------KH 1646
Cdd:PRK11281 115 ---RETLStLSLRQLESRLAQTLdqlqnaQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQirnLLKGGKvggkalRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1647 ERRVK---ELVY---QTEEDRKNLA---RMQDLvDKLQSKVKSYKRQFEEAEQQASTNL--AKYRK-AQHELDDAEERAD 1714
Cdd:PRK11281 192 SQRVLlqaEQALlnaQNDLQRKSLEgntQLQDL-LQKQRDYLTARIQRLEHQLQLLQEAinSKRLTlSEKTVQEAQSQDE 270
|
250
....*....|..
gi 1907142940 1715 MAETQANKLRAR 1726
Cdd:PRK11281 271 AARIQANPLVAQ 282
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1504-1728 |
1.53e-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: 43.46 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1504 LAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKaitdaammaeelKKEQDTSAHLE 1583
Cdd:NF033838 101 LYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKD------------QKEEDRRNYPT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1584 RMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKlEAKVRELEAELDAEQKKhAEALKGVRKHERRVKELVYQTEEDRKN 1663
Cdd:NF033838 169 NTYKTLELEIAESDVEVKKAELELVKEEAKEPRD-EEKIKQAKAKVESKKAE-ATRLEKIKTDREKAEEEAKRRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1664 LARMQDLVDKLQSKVKSYKRQF---EEAEQQASTNLAKYR--------------KAQHELDDAEERADMAETQANKLRAR 1726
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRGvlgEPATPDKKENDAKSSdssvgeetlpspslKPEKKVAEAEKKVEEAKKKAKDQKEE 326
|
..
gi 1907142940 1727 SR 1728
Cdd:NF033838 327 DR 328
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
879-1344 |
1.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 879 LEEKLKKKDSELSQLNLRVEDEQLVGVQ-LQKKIKELQARAEELEEELEAERAararVEKQRAEAARELEELSERLeeag 957
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREEL---- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 958 gASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRrkqadsaaELSEQVDSLQRIRQKLEKEKSELRMEVDDLGAS 1037
Cdd:COG4717 119 -EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1038 ----VETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTEngelgRLLEEKESMISQLSR--GKTSA 1111
Cdd:COG4717 190 teeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----ERLKEARLLLLIAAAllALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1112 AQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRLlskANAEVAQWRSKYEADAIQRTEELEE 1191
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1192 AKKKLAlRLQEAEEGVEAANakcsslEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELE 1271
Cdd:COG4717 342 LLDRIE-ELQELLREAEELE------EELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 1272 AAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSiQELEKAKKALEGEKSELQ 1344
Cdd:COG4717 415 LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELR 486
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1460-1737 |
1.71e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1460 RDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLHsqnTGLLNQKK-------- 1531
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQ---TALRQQEKieryqedl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1532 -KLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELK------KEQDTSA--------HLERMKKTLEQTvrEL 1596
Cdd:COG3096 357 eELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqalDVQQTRAiqyqqavqALEKARALCGLP--DL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1597 QARLEEAEQAALRGgkkQVQKLEAKVRELEAEL---DAEQKKHAEALKGVRKH----ER-----RVKELVYQTEEDRKNL 1664
Cdd:COG3096 435 TPENAEDYLAAFRA---KEQQATEEVLELEQKLsvaDAARRQFEKAYELVCKIagevERsqawqTARELLRRYRSQQALA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1665 ARMQDLVDKLQ------SKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRARS------RDALG 1732
Cdd:COG3096 512 QRLQQLRAQLAeleqrlRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRselrqqLEQLR 591
|
....*
gi 1907142940 1733 PKHKE 1737
Cdd:COG3096 592 ARIKE 596
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1544-1736 |
1.79e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1544 VEEAAQERREAEE-KAKKAITDAAMMAEELKKEQDTSAHL-ERMKKTLEqTVRELQARLEEAEQAALRGGKK---QVQKL 1618
Cdd:PLN03188 1041 TDESPEKKLEQERlRWTEAESKWISLAEELRTELDASRALaEKQKHELD-TEKRCAEELKEAMQMAMEGHARmleQYADL 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1619 EAKVRELEAELDAEQK-----KHAEALKGVRKHERR--------VKELVYQTEEDRKNLarmQDLVDKLQSKVksykRQF 1685
Cdd:PLN03188 1120 EEKHIQLLARHRRIQEgiddvKKAAARAGVRGAESKfinalaaeISALKVEREKERRYL---RDENKSLQAQL----RDT 1192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907142940 1686 EEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRaRSRDALGPKHK 1736
Cdd:PLN03188 1193 AEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAY-KQIDKLKRKHE 1242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
650-1651 |
1.86e-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: 43.11 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 650 EELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKnDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERL 729
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 730 EDEEEVNADLAARRRKLEDECTELKKDIDDLEltlakaEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQeaHQQA 809
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDCQRELEKLNKERRLLNQEKTELL--VEQG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 810 LGDLQAEEDRVSALAKAKIRLEQQ----VEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKK 885
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 886 KDSELSQLNLRVEDEQlvgVQLQKKIKELQARAEeleeeleaeraararvEKQRAEAARELEELSErleeaggasagqrE 965
Cdd:TIGR00606 431 IRDEKKGLGRTIELKK---EILEKKQEELKFVIK----------------ELQQLEGSSDRILELD-------------Q 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 966 GCRKREAELGRLRRE-------LEEAVLRHE-ATVAALRRKQADSAAELSEQVDSLQRIrQKLEKEKSELRMEVDDLGAS 1037
Cdd:TIGR00606 479 ELRKAERELSKAEKNsltetlkKEVKSLQNEkADLDRKLRKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1038 VETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSlee 1117
Cdd:TIGR00606 558 HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS--- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1118 lrrqleeeskakgalahavQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEA------DAIQRTEELEE 1191
Cdd:TIGR00606 635 -------------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqRVFQTEAELQE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1192 AKKKLALRLQEAEEgveaanaKCSSLEKAKLRLQTESEDVtleLERATSAAAALDKKQRhleraleerrrqeeemqrELE 1271
Cdd:TIGR00606 696 FISDLQSKLRLAPD-------KLKSTESELKKKEKRRDEM---LGLAPGRQSIIDLKEK------------------EIP 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1272 AAQREARGLGTELFRLRHSHEEALEALETLKREnknlQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAaleeae 1351
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE----EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG------ 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1352 galeleetktlriqLELSQVKAEVDRKLAEKDEEctnLRRNHQRAVESLQASLDaetraRNEALRLKKKMEGDLNDLELQ 1431
Cdd:TIGR00606 818 --------------SDLDRTVQQVNQEKQEKQHE---LDTVVSKIELNRKLIQD-----QQEQIQHLKSKTNELKSEKLQ 875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1432 LGHAT--RQAMEAQAATRLlqaqlkeeqagrDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQEL 1509
Cdd:TIGR00606 876 IGTNLqrRQQFEEQLVELS------------TEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1510 LEATERLNLLHSQNTGLLN--------QKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDtsaH 1581
Cdd:TIGR00606 944 NDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQD---N 1020
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1582 LERMKKtlEQTVRELQarlEEAEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVK 1651
Cdd:TIGR00606 1021 LTLRKR--ENELKEVE---EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1217-1698 |
1.99e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1217 LEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAA------QREARGLGTELFRLRH- 1289
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQeeqlkkQQLLKQLRARIEELRAq 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1290 --SHEEALEALEtLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEET-KTLRIQL 1366
Cdd:TIGR00618 276 eaVLEETQERIN-RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLlQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1367 ELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDL------NDLELQLGHATRQ-- 1438
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDtrtsafRDLQGQLAHAKKQqe 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1439 ------AMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEA 1512
Cdd:TIGR00618 435 lqqryaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1513 TERLNLLHSQNT-----GLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMA-----------------E 1570
Cdd:TIGR00618 515 PARQDIDNPGPLtrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTqcdnrskedipnlqnitV 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1571 ELKKEQDTSAHLERMKKTLEQT-VRELQARLEEAEQAALRGGKKQ-VQKLEAKVRELEAELDAEQKKHAEALKGV---RK 1645
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQCSQeLALKLTALHALQLTLTQERVREHALSIRVlpkEL 674
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 1646 HERRVKELVY------QTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAK 1698
Cdd:TIGR00618 675 LASRQLALQKmqsekeQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD 733
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
677-899 |
2.23e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 677 EETQVSVTQEKNDL--------ALQLQAEQDNlADAEErchlLIKSKVQLEAKVKELSERLEDEEEvnADLAARRRKLED 748
Cdd:PRK00409 505 EEAKKLIGEDKEKLneliasleELERELEQKA-EEAEA----LLKEAEKLKEELEEKKEKLQEEED--KLLEEAEKEAQQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 749 ECTELKKDIDDLELTLAKAEKEKQaTENKVKNLTEEMAALDEAVVRLTKEKKAL-QEAHQQALGDlqaeedrvsalaKAK 827
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGY-ASVKAHELIEARKRLNKANEKKEKKKKKQkEKQEELKVGD------------EVK 644
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 828 IR-LEQQVEDLECSLEQEKKLRMDTERAKRKLEgDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVED 899
Cdd:PRK00409 645 YLsLGQKGEVLSIPDDKEAIVQAGIMKMKVPLS-DLEKIQKPKKKKKKKPKTVKPKPRTVSLELDLRGMRYEE 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1017-1250 |
2.24e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1017 RQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEE 1096
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1097 KESMISQLsrgktsaaqsleelrrqleeeskakgaLAHAVQALRHDCDLLREQHEEESEAQAELQRLlskanAEVAQWRS 1176
Cdd:COG4942 102 QKEELAEL---------------------------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYL-----KYLAPARR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142940 1177 KYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQR 1250
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1183-1726 |
2.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1183 IQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEKAKLRLQTESEDVTLELERATSAAAALDK------KQRHLERAL 1256
Cdd:PRK03918 154 ILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElreeleKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1257 EERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLqEEISDLTDQVSLSGKSIQELEKAKKAL 1336
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1337 EGEKSELQAALEEAEGALELEETKTLRIQlELSQVKAEVDRKLA--EKDEECTNLRRNHQRAVESLQASLDAET-----R 1409
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLTGLTpekleK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1410 ARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAA-TRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAEL 1488
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAiEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1489 EELRAaleqgERSRRLAEQE-LLEATERLNLLHSqntgLLNQKKKLEVDLAQLSGE-VEEAAQERREAEEKAKKAITDAA 1566
Cdd:PRK03918 472 EEKER-----KLRKELRELEkVLKKESELIKLKE----LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1567 MMAEELKKEQDtsahLERMKKTLEQTVRELQARLEEAEQAALRGGKKQVQKLEAKVRELEaELDAEQKKHAEALKGVRKH 1646
Cdd:PRK03918 543 SLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKELERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1647 ERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNL-----AKYRKAQHELDDAEERADMAETQAN 1721
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREEIKKTLE 697
|
....*
gi 1907142940 1722 KLRAR 1726
Cdd:PRK03918 698 KLKEE 702
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
747-966 |
2.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 747 EDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVSALAKA 826
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 827 KIR-------------------LEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKD 887
Cdd:COG3883 95 LYRsggsvsyldvllgsesfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 888 SELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREG 966
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAG 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1363-1603 |
2.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1363 RIQLELSQVKAEVDRkLAEKDEECTNLRRNHQRA--VESLQASLDAETRARNEAL--RLKKKMEGDLNDLELQLGHATRQ 1438
Cdd:COG4913 239 RAHEALEDAREQIEL-LEPIRELAERYAAARERLaeLEYLRAALRLWFAQRRLELleAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1439 AMEAQAATRLLQAQLkeEQAGRDEEQRLAAELREQGQalerraallaaeleelraalEQGERSRRLAEQELLEATERLNL 1518
Cdd:COG4913 318 LDALREELDELEAQI--RGNGGDRLEQLEREIERLER--------------------ELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1519 LHSQnTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAitdaammAEELKKEQDTSAHLERMKKTLEQTVRELQA 1598
Cdd:COG4913 376 PASA-EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL-------RRELRELEAEIASLERRKSNIPARLLALRD 447
|
....*
gi 1907142940 1599 RLEEA 1603
Cdd:COG4913 448 ALAEA 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1535-1706 |
3.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1535 VDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQaALRGGKKQ 1614
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1615 VQkleakVRELEAELDAEQKKHAEAlkgvrkhERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQAST 1694
Cdd:COG1579 89 KE-----YEALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|..
gi 1907142940 1695 NLAKYRKAQHEL 1706
Cdd:COG1579 157 ELEELEAEREEL 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1056-1629 |
3.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1056 EDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKtsaaqsleelrRQLEEESKAKGALAHA 1135
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE-----------KELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1136 VQALRHDCDLLREQHEEESEAQAELQRLLSKANA--EVAQWRSKYEadaiqrtEELEEAKKKLAlRLQEAEEGVEAANAK 1213
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYL-------DELREIEKRLS-RLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1214 CSSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLEraleerrrqeeemqrelEAAQREARGLGTELFRLRHSHEE 1293
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-----------------ELERLKKRLTGLTPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1294 ALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKAL--------EGEKSELQAALEEAEGALELEETKTLRIQ 1365
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1366 LELSQVKAEVDRKLAEKDEectnLRRNHQ-----RAVESLQASLDAETRARNEalRLKKKMEGDLNDLELQLGHATRQAM 1440
Cdd:PRK03918 476 RKLRKELRELEKVLKKESE----LIKLKElaeqlKELEEKLKKYNLEELEKKA--EEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1441 EAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEqgerSRRLAEQELLEATERLNLLH 1520
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL----ELKDAEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1521 SQNTGLLNQKKKLEVDLAQLSGEVEEAaqERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARL 1600
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580 590
....*....|....*....|....*....|....
gi 1907142940 1601 EEAEQAA-----LRGGKKQVQKLEAKVRELEAEL 1629
Cdd:PRK03918 704 EEREKAKkelekLEKALERVEELREKVKKYKALL 737
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
718-915 |
3.60e-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: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 718 LEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTK 797
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 798 EKKALQE---AHQQALGDLQ---AEEDRV-SALAKAKIRLEQQVEDlecSLEQEKKLRMDTERAKRKLEGDLKLTQETVT 870
Cdd:pfam10174 423 RVKSLQTdssNTDTALTTLEealSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907142940 871 DTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQ 915
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
643-1091 |
3.75e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 643 LRSAQAEEELAALRAELRGLRGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNladAEERChLLIKSKVQLEAKV 722
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL---QEEPC-PLCGSCIHPNPAR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 723 KELSE------RLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLT 796
Cdd:TIGR00618 518 QDIDNpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 797 KEKKALQEAHQQALGDLQAEEDRVS-ALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQD 875
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 876 KQQLEEKLKKKDSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEaeraararvekqrAEAARELEELSERLEE 955
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASS-------------SLGSDLAAREDALNQS 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 956 AGGASAGQREGCRKreaelgrlrRELEEAVLRHEATVAALR-RKQADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDD- 1033
Cdd:TIGR00618 745 LKELMHQARTVLKA---------RTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSd 815
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907142940 1034 ---LGASVETLARGKASAEKLCRTYEDQLSEAK---IKVEELQRQLADASTQRGRLQTENGELG 1091
Cdd:TIGR00618 816 ediLNLQCETLVQEEEQFLSRLEEKSATLGEIThqlLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
634-1111 |
3.78e-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: 42.34 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 634 KLFFKMKPLLRSAQAEEELAALRAELRGLRGALATAE--AKRQELEETQVSVTQEKNDLALQLQAEQDNLADAE------ 705
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 706 ERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAARRRKLEDECTELKKDID-------DLELTLAKAEKEKQATENKV 778
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 779 KNLTEEMAALDEAVVRLTKekkalQEAHQQALGDLQAEEDRVSA----LAKAKIRLEQQVEDLECSLEQEKKLRMDTERA 854
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 855 KRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNLRVEDEQLVgvqLQKKIKELQARAEELEEELEAERAARAR 934
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI---IDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 935 VEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAVLRHEATVAALRRKQADSAAEL---SEQVD 1011
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELdtvVSKIE 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1012 SLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLcrtyEDQLSEAKIKVEELQRQLADASTQRGRLQTengELG 1091
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQF----EEQLVELSTEVQSLIREIKDAKEQDSPLET---FLE 919
|
490 500
....*....|....*....|
gi 1907142940 1092 RLLEEKESMISQLSRGKTSA 1111
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKA 939
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
712-874 |
3.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 712 IKSKVQLEAKVKELSERLEDEEEVNAdlaaRRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDea 791
Cdd:PRK12704 54 IKKEALLEAKEEIHKLRNEFEKELRE----RRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 792 vvrltKEKKALQEAHQQALGDLQaeedRVSALAKAKIRlEQQVEDLECSLEQEKKLRMDTERAKRKLEGDlKLTQETVTD 871
Cdd:PRK12704 128 -----KKEEELEELIEEQLQELE----RISGLTAEEAK-EILLEKVEEEARHEAAVLIKEIEEEAKEEAD-KKAKEILAQ 196
|
...
gi 1907142940 872 TTQ 874
Cdd:PRK12704 197 AIQ 199
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
647-838 |
4.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 647 QAEEELAALRAELRGLRGALATAEAKRQELEETQvsvtqekNDLALQLQAEQdNLADAEERCHLLIKSKVQLEAKVKELS 726
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-------QRLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 727 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLeltlakaekEKQATenkvknlteEMAALDEAVVRLTKEKKALQEAH 806
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRL---------AARAP---------AWLAAQDALARLREQSGEEFEDS 626
|
170 180 190
....*....|....*....|....*....|..
gi 1907142940 807 QQALGDLQAEEDRVSALAKAKIRLEQQVEDLE 838
Cdd:PRK04863 627 QDVTEYMQQLLERERELTVERDELAARKQALD 658
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1531-1705 |
5.14e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1531 KKLEVDLAQLSGEVEEAAQERREAEEKAKKAITdAAMMAEELKKEQDTSAHLERMKKTLEQTVRELQARLEEAEQAALRG 1610
Cdd:pfam01442 7 DELSTYAEELQEQLGPVAQELVDRLEKETEALR-ERLQKDLEEVRAKLEPYLEELQAKLGQNVEELRQRLEPYTEELRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1611 GKKQVQKLEAKVRELEAELDAEQKKHAEALKGvrKHERRVKELVYQTEEdrknlaRMQDLVDKLQSKVKSYKRQFEEAEQ 1690
Cdd:pfam01442 86 LNADAEELQEKLAPYGEELRERLEQNVDALRA--RLAPYAEELRQKLAE------RLEELKESLAPYAEEVQAQLSQRLQ 157
|
170
....*....|....*
gi 1907142940 1691 QASTNLAKYRKAQHE 1705
Cdd:pfam01442 158 ELREKLEPQAEDLRE 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
742-1420 |
5.24e-03 |
|
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: 41.54 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 742 RRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAEEDRVS 821
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 822 ALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLK-------KKDSELSQLN 894
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNllekeklNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 895 LRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAareleelserleeaggasagqregcRKREAEL 974
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI-------------------------NEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 975 GRLRRELEEAVLRHEATVAALRRKQadsaaelsEQVDSLQRIRQKLEKEKSELRMEVDDLGASVE-----TLARGKASAE 1049
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQ--------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1050 KLCRTYEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSleelrrqleeeskak 1129
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE--------------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1130 galahaVQALRHDCDLLREQHEEESEAQAELQrllskanaevaqwrskyeadaiQRTEELEEAKKKLALRLQEAEEGVEA 1209
Cdd:TIGR04523 386 ------IKNLESQINDLESKIQNQEKLNQQKD----------------------EQIKKLQQEKELLEKEIERLKETIIK 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1210 ANAKCSSLEKAKLRLQTESEDvtleleratsaaaaLDKKQRHLERALEERRRQEEEMQRELEAAQREArglgtelfrlrh 1289
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKN--------------LDNTRESLETQLKVLSRSINKIKQNLEQKQKEL------------ 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1290 shEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKT--LRIQLE 1367
Cdd:TIGR04523 492 --KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKeiDEKNKE 569
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907142940 1368 LSQVK----------AEVDRKLAEKDEECTNLrRNHQRAVESLQASLDAE---TRARNEALRLKKK 1420
Cdd:TIGR04523 570 IEELKqtqkslkkkqEEKQELIDQKEKEKKDL-IKEIEEKEKKISSLEKElekAKKENEKLSSIIK 634
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1336-1689 |
5.34e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1336 LEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAEVDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEAL 1415
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1416 RLKKKMEgdlndLELQLGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAAL 1495
Cdd:pfam02463 272 KENKEEE-----KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1496 EQGERSRRLAEQELLEATERLNLLHSQNtglLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKE 1575
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEE---LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1576 QDTSAHLERMKKTLEQTVRELQARLEEAEQ--AALRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKEL 1653
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELekQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907142940 1654 VYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAE 1689
Cdd:pfam02463 504 KARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1272-1473 |
5.50e-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: 41.29 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1272 AAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEeae 1351
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1352 galeleetktlRIQLELSQVKAEVDRKLAEkdeECTNLRRNHQRAVESLQASLDAETRAR-----NEALR-LKKKMEGDL 1425
Cdd:COG4942 94 -----------ELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARReQAEELRADL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907142940 1426 NDLELQLGHATRQAMEAQAATRLLQAQLKEEQAGRDEEQRLAAELREQ 1473
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1497-1724 |
5.61e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1497 QGERSRRLAEQELLEATERLNLLHSQNTGLLNQKKKLEVDLAQLSGEVEEAAQERREAEEKAKKAITDAAMMAEELKKEQ 1576
Cdd:COG1340 26 ELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1577 DTSAHLERMKKTLEQTVRELQAR---LEE--------AEQAALRGGKKQVQKLEAKVRELEAELDAEQKKhaealkgVRK 1645
Cdd:COG1340 106 KAGGSIDKLRKEIERLEWRQQTEvlsPEEekelvekiKELEKELEKAKKALEKNEKLKELRAELKELRKE-------AEE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 1646 HERRVKELVYQTEEDRKNLARMQDLVDKLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLR 1724
Cdd:COG1340 179 IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK 257
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
663-1195 |
5.77e-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: 41.26 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 663 RGALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAAR 742
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 743 RRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQ-------------- 808
Cdd:pfam05557 106 ISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRikelefeiqsqeqd 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 809 --ALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKlTQETVTDTTQDKQQLEEKLK-- 884
Cdd:pfam05557 186 seIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEK-YREEAATLELEKEKLEQELQsw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 885 KKDSELSQLNLRVEDEqlvgvqLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSerleeaggasaGQR 964
Cdd:pfam05557 265 VKLAQDTGLNLRSPED------LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYL-----------KKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 965 EGCRKREAELGRLRRELEEAVLrheatvaaLRRKQADSAAELSEQVDS---LQRIRQKLEKEKSELRMEVDDLGASVETL 1041
Cdd:pfam05557 328 EDLNKKLKRHKALVRRLQRRVL--------LLTKERDGYRAILESYDKeltMSNYSPQLLERIEEAEDMTQKMQAHNEEM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1042 ARGKASAEKLCRTYEDQLS--EAKIKVEELQRQLADASTQ-------RGRLQTENGELGRLLEEKESMISQLSR---GKT 1109
Cdd:pfam05557 400 EAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSkeevdslRRKLETLELERQRLREQKNELEMELERrclQGD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1110 SAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEAQAELQRL----LSKANAEVAQWRSKYE-ADA-I 1183
Cdd:pfam05557 480 YDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLpettSTMNFKEVLDLRKELEsAELkN 559
|
570
....*....|..
gi 1907142940 1184 QRTEELEEAKKK 1195
Cdd:pfam05557 560 QRLKEVFQAKIQ 571
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1595-1732 |
5.91e-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: 40.29 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1595 ELQARLEEAEQAaLRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKELVYQTEEDRKNLARMQDL--VD 1672
Cdd:COG1579 14 ELDSELDRLEHR-LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1673 KLQSKVKSYKRQFEEAEQQASTNLAKYRKAQHELDDAEERADMAETQANKLRARSRDALG 1732
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
648-915 |
6.49e-03 |
|
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: 41.21 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 648 AEEELAALRAELRGLRGAL-------ATAEAKRQELEE-----TQVSVTQEKNDLALQlqaeqdNLADAEERCHLLIKSK 715
Cdd:pfam05622 109 LAEEAQALKDEMDILRESSdkvkkleATVETYKKKLEDlgdlrRQVKLLEERNAEYMQ------RTLQLEEELKKANALR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 716 VQLEA---KVKELSERLEDE--------------EEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQA----- 773
Cdd:pfam05622 183 GQLETykrQVQELHGKLSEEskkadklefeykklEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQAdalls 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 774 -TENKVKNLTEEM--AALDEAVVRLTKEKKALQEA----HQQALGDLQAEEDRVSA----------LAKAKIR-LEQQVE 835
Cdd:pfam05622 263 pSSDPGDNLAAEImpAEIREKLIRLQHENKMLRLGqegsYRERLTELQQLLEDANRrkneletqnrLANQRILeLQQQVE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 836 DLECSLEQEKKLRMDTERAKRKLEgdlkltqetvtdttqdkqQLEEKLKKKDSELSQLNLRVED-EQLVGVQLQKKIKEL 914
Cdd:pfam05622 343 ELQKALQEQGSKAEDSSLLKQKLE------------------EHLEKLHEAQSELQKKKEQIEElEPKQDSNLAQKIDEL 404
|
.
gi 1907142940 915 Q 915
Cdd:pfam05622 405 Q 405
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1530-1689 |
6.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1530 KKKLEVDLAQLSGEVEEAAQERREAEEKAKKAitdaammaEELKKEqdtsahLERMKKTLEQTVRELQAR-------LEE 1602
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEA--------EALLKE------AEKLKEELEEKKEKLQEEedklleeAEK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1603 AEQAALRGGKKQVQKLEAKVRELEAELDAEQKKHaealkgvrkherrvkelvyQTEEDRKNLARMQDLVDKLQSKVKSYK 1682
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQKGGYASVKAH-------------------ELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
....*..
gi 1907142940 1683 RQFEEAE 1689
Cdd:PRK00409 635 EELKVGD 641
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1055-1501 |
6.94e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1055 YEDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQSLEELRRQLEEESKAKGALAH 1134
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1135 AVQALRHDCDLLREQHEEESEAQAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKC 1214
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1215 SSLEKAKLRLQTESEDVTLELERATSAAAALDKKQRHLERALEERRRQEEEMQRELEAAQREARGLGTELFRLRHSHEEA 1294
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1295 LEALETLKRENKNLQEEISDLTDQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTLRIQLELSQVKAE 1374
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1375 VDRKLAEKDEECTNLRRNHQRAVESLQASLDAETRARNEALRLKKKMEGDLNDLELQLGHATRQAMEAQAATRLLQAQLK 1454
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1907142940 1455 EEQAGRDEEQRLAAELREQGQALERRAALLAAELEELRAALEQGERS 1501
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
906-1113 |
6.94e-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: 40.90 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 906 QLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQREGCRKREAELGRLRRELEEAV 985
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 986 LRHEATVAALRRK----------QADSAAELSEQVDSLQRIRQKLEKEKSELRMEVDDLGASVETLARGKASAEKLCRTY 1055
Cdd:COG4942 104 EELAELLRALYRLgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907142940 1056 EDQLSEAKIKVEELQRQLADASTQRGRLQTENGELGRLLEEKESMISQLSRGKTSAAQ 1113
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
665-889 |
6.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 665 ALATAEAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERchlLIKSKVQLEAKVKELSERLEDEEEVNADLAARRR 744
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE---YNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 745 KLEDECTELKK---DIDDLELTLakaekekQATE-----NKVKNLTEEMAALDEAVVRLTKEKKALQEAHQQALGDLQAE 816
Cdd:COG3883 87 ELGERARALYRsggSVSYLDVLL-------GSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 817 EDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSE 889
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1575-1652 |
7.79e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1575 EQDTSAHLERMKKTLEQTVRELQARLEEAEQAA--LRGGKKQVQKLEAKVRELEAELDAEQKKHAEALKGVRKHERRVKE 1652
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQqeLVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITD 223
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
649-781 |
8.23e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 649 EEELAALRAELRGLRGALATAEAKRQELEEtqvSVTQEKNDLAlQLQAEQDNLADAEERchlLIKSKVQLEAKVKELSER 728
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQD---SVANLRASLS-AAEAERSRLQALLAE---LAGAGAAAEGRAGELAQE 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907142940 729 LEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNL 781
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
587-850 |
9.04e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 587 VLTLLQARSRGrLMRLEyqRMLGGRDALfTIQWNIRAFNAVKNWSWMKLFFKMKplLRSAQAEEELAALRAELrGLRGAL 666
Cdd:PLN02939 144 ILLLNQARLQA-LEDLE--KILTEKEAL-QGKINILEMRLSETDARIKLAAQEK--IHVEILEEQLEKLRNEL-LIRGAT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 667 ATAEAKRQELEetqVSVTQEKN----DLALQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELSERLEDEEEVNADLAAr 742
Cdd:PLN02939 217 EGLCVHSLSKE---LDVLKEENmllkDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 743 rrkLEDECteLKKDIDDLELTLAKAEK----------EKQATENKVKNLTEemaALDEAVVrlTKEKKALQEAHQQALGD 812
Cdd:PLN02939 293 ---LQYDC--WWEKVENLQDLLDRATNqvekaalvldQNQDLRDKVDKLEA---SLKEANV--SKFSSYKVELLQQKLKL 362
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907142940 813 LQAEEDRVSALAKAKIRLEQQV-----EDLECSLEQEKKLRMD 850
Cdd:PLN02939 363 LEERLQASDHEIHSYIQLYQESikefqDTLSKLKEESKKRSLE 405
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
647-965 |
9.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 647 QAEEELAALRAELRGLRGALataEAKRQELEETQVSVTQEKNdlalQLQAEQDNLADAEERCHLLIKSKVQLEAKVKELS 726
Cdd:COG4372 35 KALFELDKLQEELEQLREEL---EQAREELEQLEEELEQARS----ELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 727 ERLEDEEEVNADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTKEKKALQEAH 806
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 807 QQALGDLQAEEDRVSALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKK 886
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907142940 887 DSELSQLNLRVEDEQLVGVQLQKKIKELQARAEELEEELEAERAARARVEKQRAEAARELEELSERLEEAGGASAGQRE 965
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
842-1672 |
9.34e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 842 EQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKKDSELSQLNlrvedeqlvgvQLQKKIKELQARAEEL 921
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ-----------QSHAYLTQKREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 922 EEELEAERAARARVEKQRAEaareleelserleeaggasagqregcrkrEAELGRLRRELEEA-----VLRHEATVAALR 996
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQ-----------------------------EAVLEETQERINRArkaapLAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 997 RKQADSAAELSEQVDSLQRIRQKlekekselRMEVDDLGASVETLARGKASAEKLCRTYEDQLSEAKIKVEELQRQLADa 1076
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMK--------RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1077 sTQRGRLQTENGElgrLLEEKESMISQLSRgKTSAAQSLEELRRQLEEESKAKGALAHAVQALRHDCDLLREQHEEESEA 1156
Cdd:TIGR00618 378 -TQHIHTLQQQKT---TLTQKLQSLCKELD-ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1157 QAELQRLLSKANAEVAQWRSKYEADAIQRTEELEEAKKKLALRLQEAEEGVEAANAKCSSLEkAKLRLQTESEDVTLELE 1236
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1237 RATSAAAALDKkqrhleraleerrrqeeemqrELEAAQREARGLGTELFRLRHSHEEALEALETLKRENKNLQEEISDLT 1316
Cdd:TIGR00618 532 RGEQTYAQLET---------------------SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1317 DQVSLSGKSIQELEKAKKALEGEKSELQAALEEAEGALELEETKTlRIQLELSQVKAEVDRKLAE--KDEECTNLRRNHQ 1394
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ-QCSQELALKLTALHALQLTltQERVREHALSIRV 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1395 RAVESLQASLDAETRARNEALRLKKKMEG------DLNDLELQLGHATRQAMEAQAATRLLQAQLK-EEQAGRDEEQRLA 1467
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMlaqcqtLLRELETHIEEYDREFNEIENASSSLGSDLAaREDALNQSLKELM 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1468 AELREQGQALERRAALLAAELEELRAALEQGERSRRLAEQELLEATERLNLLhsqNTGLLNQKKKLEVDLAQLSGEVEEA 1547
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL---KTLEAEIGQEIPSDEDILNLQCETL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 1548 AQERREAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKTleqtvrelQARLEEAEQAALRGGKKQVQKLEAKVRELEA 1627
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE--------QAKIIQLSDKLNGINQIKIQFDGDALIKFLH 898
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1907142940 1628 ELDAEQKKHAEALKGVRKHERrvkelvYQTEEDRKNLARMQDLVD 1672
Cdd:TIGR00618 899 EITLYANVRLANQSEGRFHGR------YADSHVNARKYQGLALLV 937
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
670-915 |
9.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 670 EAKRQELEETQVSVTQEKNDLALQLQAEQDNLADAEERCHLlikskVQLEAKVKELSERLEdeeevnadlaarrrklede 749
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL-----VDLSEEAKLLLQQLS------------------- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 750 ctelkkdidDLELTLAKAEKEKQATENKVKNLTEEMAALDEAVVRLTkEKKALQEAHQQaLGDLQAEEDRVSALAKAK-- 827
Cdd:COG3206 223 ---------ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL-QSPVIQQLRAQ-LAELEAELAELSARYTPNhp 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 828 --IRLEQQVEDLECSLEQEkklrmdTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLK---KKDSELSQLNLRVEDEQL 902
Cdd:COG3206 292 dvIALRAQIAALRAQLQQE------AQRILASLEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARE 365
|
250
....*....|...
gi 1907142940 903 VGVQLQKKIKELQ 915
Cdd:COG3206 366 LYESLLQRLEEAR 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
737-886 |
9.87e-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: 39.52 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907142940 737 ADLAARRRKLEDECTELKKDIDDLELTLAKAEKEKQATENKVKNLTEEMAALDEavvRLTKEKKALQEAH-QQALGDLQA 815
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRnNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907142940 816 EEDrvsALAKAKIRLEQQVEDLECSLEQEKKLRMDTERAKRKLEGDLKLTQETVTDTTQDKQQLEEKLKKK 886
Cdd:COG1579 97 EIE---SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| |
